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Information on EC 3.2.1.21 - beta-glucosidase
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EC Tree
3.2.1.21 beta-glucosidaseIUBMB Comments
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
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Word Map
- 3.2.1.21
- cellobiose
- cellulase
- beta-galactosidase
- glycoside
- lysosomal
- alpha-glucosidase
- gaucher
- trichoderma
- aglycone
- endoglucanase
- glycosidases
-
cellulolytic
- almond
- xylanase
- reesei
- beta-xylosidase
-
saccharification
- alpha-mannosidase
- p-nitrophenyl
- alpha-galactosidase
-
lignocellulosic
- urease
- cellobiohydrolase
- avicel
-
cellulosic
- straw
- glucosylceramide
- cassava
- beta-n-acetylglucosaminidase
- xylan
- beta-d-glucopyranoside
- cmcase
- hemicellulose
-
microcrystalline
- beta-mannosidase
- arylamidase
- arbutin
- cellulomonas
-
transglucosylation
- stover
- alpha-l-fucosidase
- alpha-l-arabinofuranosidase
- cellotetraose
- bagasse
- azoreductase
- carboxymethylcellulase
- endo-beta-1,4-glucanase
- cellodextrins
- glucocerebroside
-
xylanolytic
- industry
- biofuel production
- medicine
- nutrition
- degradation
- analysis
- synthesis
- food industry
- molecular biology
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
beta-glucosidase, linamarase, beta-glu, emulsin, bglu1, zm-p60.1, bgl1b, cel3a, novozyme 188, t-cell inhibitor, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-glucosidase
A1
amygdalase
-
-
-
-
amygdalinase
-
-
-
-
arbutinase
-
-
-
-
aryl-beta-glucosidase
-
-
-
-
AT5A_15831
beta-1,6-glucosidase
-
-
-
-
beta-D-glucosidase
beta-D-glucoside glucohydrolase
beta-Glcase
beta-glu
beta-glucosidase
beta-glucosidase 1
beta-glucosidase B
beta-glucosidase I
beta-glucoside hydrolase
-
-
-
-
betaG
BG
BG1
BGA
Bgl
BGL1
BGL1A
BGL1B
Bgl2
Bgl3
bgl3a
Bgl3B
BGL50
BglA
BglB
BglD5
Bglhi
BglHi2
BglI
BglII
BglP
BGLPf
BGlu1
bifunctional exo-beta-glucosidase/N-acetyl-beta-glucosaminidase
Cba3
CBG
CC1G_08724
Cel3A
CelB
cellobiase
elaterase
-
-
-
-
emulsin
-
-
-
-
FPG
GBA3
gentiobiase
GH1 beta-glucosidase
GH3 beta-glucosidase
Gh3-4
Glu1
HiBgl3A
HiBgl3B
HiBgl3C
Hore_15280
ICHG
limarase
-
-
-
-
Lin1840
linamarase
MeBglD2
beta-glucosidase/galactosidase/fucosidase activity, cf. 3.2.1.23 and 3.2.1.38
Novozyme 188
-
-
-
-
OsTAGG
-
OsTAGG1 and OsTAGG2, detected by CM-Sepharose chromatography, at least two isoforms in rice panicles
p-nitrophenyl beta-glucosidase
-
-
-
-
piceid-beta-D-glucosidase
primeverosidase
-
-
-
-
RuBGX1
gene name, beta-glucosidase/xylosidase activity, EC 3.2.1.37 and 3.2.1.21
salicilinase
-
-
-
-
SSO3039
T-cell inhibitor
-
-
-
-
Tnap_0656
Tpbgl
TpBGL1
TpBGL3
Tpebgl3
Tpen_1494
tuberonic acid glucoside (TAG)-hydrolyzing beta-glucosidase
-
a specific beta-glucosidase hydrolyzing tuberonic acid beta-D-glucose
vicianase
-
-
-
-
ZmGlu1
additional information
beta-D-glucosidase
-
-
-
-
beta-D-glucoside glucohydrolase
-
-
-
-
beta-glucosidase
belongs to glycosyl hydrolase family 3, GH3
BGA
-
-
-
-
bifunctional exo-beta-glucosidase/N-acetyl-beta-glucosaminidase
-
bifunctional exo-beta-glucosidase/N-acetyl-beta-glucosaminidase
-
-
cellobiase
-
-
-
-
gentiobiase
-
-
-
-
additional information
-
the enzyme belongs to the glycosyl hydrolase family 3
additional information
-
the enzyme belongs to the glycosyl hydrolase family 3
-
additional information
-
the enzyme belongs to the glycosyl hydrolase family 3
additional information
-
the enzyme belongs to the glycosyl hydrolase family 3
additional information
the enzyme belongs to the glycosyl hydrolase family 1
additional information
the enzyme belongs to the glycosyl hydrolase family 1
additional information
the enzyme belongs to the glycosyl hydrolase family 1
additional information
the enzyme belongs to the glycosyl hydrolase family 1
additional information
the enzyme belongs to the glycoside hydrolase family 1
additional information
the enzyme belongs to the glycosyl hydrolase family 1
additional information
the enzyme belongs to the glycoside hydrolase family 1
additional information
the enzyme belongs to the glycosyl hydrolase family 1
additional information
the enzyme belongs to the glycosyl hydrolase family 1
additional information
the enzyme belongs to the glycosyl hydrolase family 1
-
additional information
the enzyme belongs to the glycosyl hydrolase family 1
-
additional information
-
the enzyme belongs to the glycosyl hydrolase family 3
additional information
the enzyme belongs to the glycosyl hydrolase family 1
additional information
the enzyme belongs to the glycosyl hydrolase family 1
-
additional information
-
the enzyme belongs to the glycosyl hydrolase family 3
additional information
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
the enzyme belongs to the glycosyl hydrolase family 3
-
additional information
-
the enzyme belongs to the glycosyl hydrolase family 3
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
celloheptaose + 6 H2O = 7 beta-D-glucose
Wide specificity for beta-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides
-
-
-
celloheptaose + 6 H2O = 7 beta-D-glucose
reaction and kinetic mechanisms
-
celloheptaose + 6 H2O = 7 beta-D-glucose
residues E173 and E362 are essential for catalytic activity
celloheptaose + 6 H2O = 7 beta-D-glucose
structural basis for substrate specificity, residues N259, F261, and S462 are important, substrate binding mode and structure
-
celloheptaose + 6 H2O = 7 beta-D-glucose
substrate binding mode and structure
celloheptaose + 6 H2O = 7 beta-D-glucose
the enzyme contains a His residue which is important for catalytic activity
-
celloheptaose + 6 H2O = 7 beta-D-glucose
molecular basis of the catalytic mechanism involving the acid/base Glu167 and the nucleophilic Glu356, the structure of BglB shows that several polar residues narrow the active site pocket and contour additional subsites, detailed substrate-binding mode and oligosaccharide-enzyme recognition pattern of BglB, overview, oligomerization in BglA can assist in fine-tuning the specificity of the active centre by modulating the loops surrounding the cavity
celloheptaose + 6 H2O = 7 beta-D-glucose
the conserved Asp287 is the potential nucleophile in the catalytic center
celloheptaose + 6 H2O = 7 beta-D-glucose
the putative acid/base catalyst is Glu170
celloheptaose + 6 H2O = 7 beta-D-glucose
the two catalytic glutamate residues are located on strand 4, the acid/base Glu165, and on strand 7,the nucleophile Glu373
celloheptaose + 6 H2O = 7 beta-D-glucose
the two glutamic acid residues Glu172 and Glu370 are essential for enzyme activity of CellG
celloheptaose + 6 H2O = 7 beta-D-glucose
Trp49 is important for transglucosylation catalytic activity
-
celloheptaose + 6 H2O = 7 beta-D-glucose
W293 of the SDW segment, which is the residue next to the nucleophile D292 in family 3 BGL, is very important for hydrolytic reaction as a binder to a substrate. G294 of the SDWG sequence might play an important role in catalysis, interaction between the sugar rings and aromatic ring of W293 at the entrance of the catalytic pocket enhances the substrate recognition of beta-glucosidase
-
celloheptaose + 6 H2O = 7 beta-D-glucose
double replacement mechanism, retaining the configuration. A water molecule may be involved in the stabilization of transition states through a sugar 2-hydroxyl oxygen
celloheptaose + 6 H2O = 7 beta-D-glucose
the conserved Asp287 is the potential nucleophile in the catalytic center
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
beta-D-glucoside glucohydrolase
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
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CAS REGISTRY NUMBER
COMMENTARY
9001-22-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1-4)-beta-D-glucosyl-D-mannobiose + H2O
beta-D-glucose + D-mannobiose
-
-
-
?
(1-4)-beta-D-glucosyl-D-mannose + H2O
beta-D-glucose + D-mannose
-
-
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
HCN + ?
(S)-citronellyl beta-D-glucopyranoside + H2O
(S)-citronellol + beta-D-glucose
-
high activity, no activity with (S)-citronellyl beta-D-galactopyranoside or (S)-citronellyl beta-D-xylopyranoside
-
-
?
(Z)-3-hexenyl beta-D-glucopyranoside + H2O
(Z)-3-hexenol + beta-D-glucose
-
high activity, no activity with (Z)-3-hexenyl beta-D-galactopyranoside or Z-3-hexenyl beta-D-xylopyranoside
-
-
?
17beta-estradiol 17-beta-D-glucoside + H2O
beta-D-glucose + 17beta-estradiol
-
-
-
?
17beta-estradiol-3'-beta-D-glucoside + H2O
beta-D-glucose + 17beta-estradiol
-
poor activity
-
?
2,3-dinitrophenyl-beta-D-glucopyranoside + H2O
2,3-dinitrophenol + beta-D-glucose
-
-
-
-
?
2,4-dihydroxy-1,4-benzoxazin-3-one-beta-D-glucoside + H2O
2,4-dihydroxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one glucoside + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2,4-dinitrophenyl beta-D-glucopyranoside + H2O
2,4-dinitrophenol + D-glucopyranose
-
-
-
?
2,4-dinitrophenyl-2-deoxy-2-fluoro-beta-D-glucopyranoside + H2O
?
-
-
-
?
2,4-dinitrophenyl-beta-D-galactoside + H2O
2,4-dinitrophenol + beta-D-galactose
-
-
-
?
2,4-dinitrophenyl-beta-D-glucopyranoside + H2O
2,4-dinitrophenol + beta-D-glucose
-
-
-
-
?
2-chloro-4-nitrophenyl beta-D-glucopyranoside + H2O
2-chloro-4-nitrophenol + D-glucose
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-glucopyranoside + H2O
2-chloro-4-nitrophenol + D-glucose
-
-
-
?
2-hydroxy-1,4-benzoxazin-3-one-beta-D-glucoside + H2O
2-hydroxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2-hydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside + H2O
2-hydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2-nitrophenyl beta-1,4-D-galactopyranoside 6-phosphate + H2O
?
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside 6-phosphate + H2O
2-nitrophenol + beta-D-galactopyranose 6-phosphate
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-mannopyranoside + H2O
2-nitrophenol + D-mannopyranose
0.7% activity compared to 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylopyranose
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylose
-
-
-
?
2-nitrophenyl-alpha-L-arabinoside + H2O
2-nitrophenol + alpha-L-arabinose
-
very low activity
-
?
2-nitrophenyl-beta-D-fucoside + H2O
2-nitrophenol + beta-D-fucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
2-O-beta-D-glucopyranosylsalicylate + H2O
salicylic acid + beta-D-glucose
-
25% relative activity compared to hydrolysis of tuberonic acid beta-D-glucoside
-
-
?
2-phenylethanol + cellobiose
?
-
beta-glucosidase is capable of catalyzing transglycosylation reactions
-
-
?
2-phenylethyl-beta-D-glucopyranoside + H2O
2-phenylethanol + beta-D-glucose
-
51% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
3(2)-beta-D-glucosyl-D-cellobiose + H2O
beta-D-glucose + D-cellobiose
-
-
-
?
3,4-dinitrophenyl beta-D-glucopyranoside + H2O
3,4-dinitrophenol + beta-D-glucopyranose
-
-
-
-
?
3,4-dinitrophenyl beta-D-glucopyranoside + H2O
3,4-dinitrophenol + beta-D-glucose
-
-
-
-
?
3,5-dinitrophenyl beta-D-glucopyranoside + H2O
3,5-dinitrophenol + D-glucose
-
-
-
-
?
3-nitrophenyl beta-D-glucopyranoside + H2O
3-nitrophenol + D-glucose
-
-
-
-
?
3-O-alpha-D-glucopyranosyl-D-glucose + H2O
alpha-D-glucose + D-glucose
-
nigerose
-
?
3-O-beta-cellobiosyl-D-glucose + H2O
beta-D-glucose + D-cellobiose
-
-
-
?
3-O-beta-cellotriosyl-D-glucose + H2O
beta-D-glucose + D-cellotriose
-
-
-
?
3-O-[beta-D-glucopyranosyl-(1-2)-beta-D-glucopyranosyl]-20-O-[beta-D-glucopyranosyl-(1-6)-beta-D-glucopyranosyl]-20(S)-protopanaxadiol + 2 H2O
20-O-[beta-D-glucopyranosyl-(1-6)-beta-D-glucopyranosyl]-20(S)-protopanaxadiol + 2 D-glucose
-
Conversion of ginsenoside Rb1 to gypenoside LXXV. BgpA catalyzes the hydrolysis of the two glucose moieties attached to the C-3 position of ginsenoside Rb1, and the outer glucose attached to the C-20 position. Cleavages occur in a defined order, with the outer glucose of C-3 cleaved first, followed by the inner glucose of C-3, and finally the outer glucose of C-20. BgpA selectively and sequentially converts ginsenoside Rb1 to the rare ginsenosides gypenoside XVII, gypenoside LXXV, and then C-K
-
-
?
3-O-[beta-D-glucopyranosyl-(1-2)-beta-D-glucopyranosyl]-20-O-[beta-D-glucopyranosyl-(1-6)-beta-D-glucopyranosyl]-20(S)-protopanaxadiol + 3 H2O
20-O-(beta-D-glucopyranosyl)-20(S)-protopanaxadiol + 3 D-glucose
-
Conversion of ginsenoside Rb1 to C-K. BgpA catalyzes the hydrolysis of the two glucose moieties attached to the C-3 position of ginsenoside Rb1, and the outer glucose attached to the C-20 position. Cleavages occur in a defined order, with the outer glucose of C-3 cleaved first, followed by the inner glucose of C-3, and finally the outer glucose of C-20. BgpA selectively and sequentially converts ginsenoside Rb1 to the rare ginsenosides gypenoside XVII, gypenoside LXXV, and then C-K
-
-
?
3-O-[beta-D-glucopyranosyl-(1-2)-beta-D-glucopyranosyl]-20-O-[beta-D-glucopyranosyl-(1-6)-beta-D-glucopyranosyl]-20(S)-protopanaxadiol + H2O
3-O-beta-D-glucopyranosyl-20-O-[beta-D-glucopyranosyl-(1-6)-beta-D-glucopyranosyl]-20(S)-protopanaxadiol + D-glucose
-
Conversion of ginsenoside Rb1 to gypenoside XVII. BgpA catalyzes the hydrolysis of the two glucose moieties attached to the C-3 position of ginsenoside Rb1, and the outer glucose attached to the C-20 position. Cleavages occur in a defined order, with the outer glucose of C-3 is cleaved first, followed by the inner glucose of C-3, and finally the outer glucose of C-20. BgpA selectively and sequentially converts ginsenoside Rb1 to the rare ginsenosides gypenoside XVII, gypenoside LXXV, and then C-K
-
-
?
4-bromophenyl-beta-D-glucopyranoside + H2O
4-bromophenol + beta-D-glucose
-
-
-
-
?
4-methylumbeliferyl beta-D-glucoside + H2O
4-methylumbelliferol + D-glucose
-
-
-
?
4-methylumbelliferyl alpha-L-arabinoside + H2O
4-methylumbelliferone + alpha-L-arabinose
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
?
4-methylumbelliferyl beta-D-fucoside + H2O
4-methylumbelliferone + beta-D-fucose
-
-
-
-
?
4-methylumbelliferyl beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactose
-
-
-
?
4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside + H2O
4-methylumbelliferone + 2-acetamido-2-deoxy-beta-D-glucopyranose
0.09% of activity with 4-methylumbelliferyl-beta-D-glucopyranoside
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
0.1% of activity with 4-methylumbelliferyl-beta-D-glucopyranoside
-
-
?
4-methylumbelliferyl-alpha-L-arabinoside + H2O
4-methylumbelliferone + alpha-L-arabinose
-
-
-
?
4-methylumbelliferyl-beta-D-arabinopyranoside + H2O
4-methylumbelliferone + beta-D-arabinopyranose
-
-
-
?
4-methylumbelliferyl-beta-D-cellobiose + H2O
4-methylumbelliferyl-beta-D-glucopyranoside + beta-D-glucose
4-methylumbelliferyl-beta-D-cellobioside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactose
0.5% of activity with 4-methylumbelliferyl-beta-D-glucopyranoside
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucopyranose
163% relative activity
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-lactopyranoside + H2O
4-methylumbelliferone + beta-D-galactose + D-glucose
0.06% of activity with 4-methylumbelliferyl-beta-D-glucopyranoside
-
-
?
4-methylumbelliferyl-beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannose
0.075% of activity with 4-methylumbelliferyl-beta-D-glucopyranoside
-
-
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylose
7% of activity with 4-methylumbelliferyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl 1-thio-beta-D-glucopyranoside + H2O
4-nitrophenol + 1-thio-beta-D-glucopyranoside
-
1% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl alpha-D-fucopyranoside + H2O
4-nitrophenol + D-fucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
7.4% of the activity with 4-nitrophenyl beta-D-galactopyranoside
-
-
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
-
-
-
?
4-nitrophenyl beta-D-arabinopyranoside + H2O
4-nitrophenol + D-arabinose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + 2 H2O
4-nitrophenol + 2 D-glucose
-
-
glucosyl residues are removed from the non-reducing end of substrate
-
?
4-nitrophenyl beta-D-cellotrioside + H2O
4-nitrophenol + D-cellotriose
-
-
-
?
4-nitrophenyl beta-D-fucoside + 2-phenylethanol
2-phenylethyl-beta-D-fucoside + 4-nitrophenol
-
best substrate for transglycolsylation reaction
-
r
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + D-fucose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenyl + D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + 2-phenylethanol
2-phenylethyl beta-D-galactoside + 4-nitrophenol
-
transglycosylation reaction
-
r
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl beta-D-glucose + H2O
4-nitrophenyl + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + 2-phenylethanol
2-phenylethyl-beta-D-glucoside + 4-nitrophenol
-
transglycosylation reaction
-
r
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + beta-D-lactose
-
-
-
?
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + D-lactose
-
-
-
?
4-nitrophenyl N,N'-diacetyl-beta-chitobioside + H2O
?
-
-
-
?
4-nitrophenyl-1-thio-beta-D-glucopyranoside + H2O
4-nitrophenol + 1-thio-beta-D-glucose
-
31% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl-alpha-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinopyranose
-
4.9% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-O-beta-D-xylopyranosyl-D-xylose + H2O
beta-D-xylose + D-xylose
-
-
-
?
5-bromo-4-chloro-3-indolyl-beta-D-glucopyranoside + H2O
5-bromo-4-chloro-3-indolol + beta-D-glucose
-
-
-
-
?
5-bromo-4-chloro-3-indolyl-beta-D-glucopyranoside + H2O
? + beta-D-glucopyranose
-
-
-
?
6-bromo-2-naphthyl-beta-D-glucopyranoside + H2O
6-bromo-2-naphthol + beta-D-glucopyranose
-
-
-
-
?
6-bromo-2-naphthyl-beta-D-glucopyranoside + H2O
6-bromo-2-naphthol + beta-D-glucose
Thermochaetoides thermophila
-
-
-
-
?
6-bromo-2-naphthyl-beta-D-glucoside + H2O
6-bromo-2-naphthol + beta-D-glucose
-
substrate for direct screening for beta-glucosidase producing strains
-
?
6-bromonaphthyl beta-D-glucopyranoside + H2O
6-bromonaphthol + D-glucose
-
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucose + H2O
alpha-D-glucose + D-glucose
-
isomaltose
-
?
6-O-methyl-N-deacetylipecoside + H2O
?
90.5% of the efficiency with N-deacetylipecoside
-
-
?
alpha-L-arabinofuranose + H2O
alpha-L-arabinofuranose + ?
-
low activity
-
?
alpha-L-rhamnopyranoside + H2O
alpha-L-rhamnopyranose + ?
-
-
-
?
apigenin-7-O-beta-D-glucoside + H2O
apigenin + beta-D-glucose
high activity
-
-
?
benzyl-beta-D-glucopyranoside + H2O
benzyl alcohol + beta-D-glucopyranose
-
-
-
?
beta-D-fructofuranosyl-alpha-D-glucopyranoside + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
biochanin A 7-O-beta-D-glucopyranoside + H2O
biochanin A + beta-D-glucose
-
-
-
-
?
butyl beta-D-glucopyranoside + H2O
?
-
39% activity compared to ginsenoside Rg3
-
-
?
carboxymethylcellulose + H2O
beta-D-glucose + 2-(hydroxymethyl)phenol
-
-
-
-
?
cellobiose + methanol
methyl-beta-D-glucopyranoside + beta-D-glucose
-
25% methanol, transglycosylation activity
-
-
?
cellobiose [beta-(1-4)-linked] + H2O
?
beta-(1-4)-linked cellobiose
-
-
?
cellohexanose + H2O
beta-D-glucose + ?
-
85% activity compared to cellobiose
-
-
?
cellopentose + H2O
beta-D-glucose + ?
-
125% activity compared to cellobiose
-
-
?
cellotetraose + H2O
D-glucose + ?
-
64% of the activity with laminaribiose
-
?
cellotriose + H2O
beta-D-glucose + ?
-
124% activity compared to cellobiose
-
-
?
cellotriose + H2O
D-glucose + ?
-
67% of the activity with laminaribiose
-
?
citronellyl-beta-D-glucopyranoside + H2O
citronellol + beta-D-glucose
-
61.4% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
cyanoglucosides + H2O
HCN + beta-D-glucose
-
-
HCN acts as a deterrent to grazing animals
?
cyclopentyl beta-D-glucopyranoside + H2O
?
-
65.9% activity compared to ginsenoside Rg3
-
-
?
D-(+)-cellobiose + H2O
beta-D-glucose
-
12.9% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
daidzein 7'-O-(6''-O-beta-D-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
daidzein 7-O-(6-O-acetyl-beta-D-glucoside) + H2O
daidzein + 6-O-acetyl-beta-D-glucose
-
-
-
?
daidzein 7-O-(6-O-malonyl)beta-D-glucopyranoside + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
the specific activity of a recombinant enzyme for isoflavones in order of decreasing activity: daidzin, glycitin, genistin, malonyl genistin, malonyl daidzin, malonyl glycitin
-
-
?
daidzein 7-O-(6-O-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
daidzein-7-O-glucosyl-6''-O-malonate + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
-
-
-
?
dalcochinin-8'-O-beta-D-glucoside + H2O
dalcochinin + beta-D-glucose
-
-
-
-
?
dhurrin + H2O
4-hydroxy-(S)-mandelonitrile + beta-D-glucose
-
i.e. 4-hydroxy-(S)-mandelonitrile-beta-D-glucoside, Dhr1 is strictly specific for this substrate
-
-
?
dhurrin + H2O
4-hydroxybenzaldehyde + hydrogen cyanide + D-glucose
-
-
-
-
?
dhurrin + H2O
HCN + beta-D-glucose + 4-hydroxybenzaldehyde
-
low activity for PGI
-
?
digitoxigenin cellobioside + 2 H2O
digitoxigenin + 2 beta-D-glucose
-
38% of activity with glucoevatromonoside
-
-
?
dodecyl-beta-D-glucopyranoside + H2O
dodecanol + beta-D-glucose
-
15-30% of activity with p-nitrophenyl-beta-d-glucopyranoside
-
-
?
epipodophyllotoxin-4-O-beta-D-glucopyranoside + H2O
epipodophyllotoxin + beta-D-glucose
-
85% of activity with podophyllotoxin-4-O-beta-D-glucopyranoside
-
-
?
eriodicytol-7-beta-D-glucopyranoside + H2O
eriodicytol + beta-D-glucose
-
-
-
-
?
esculin hydrate + H2O
?
-
31.7% activity compared to ginsenoside Rg3
-
-
?
estrone-3-beta-D-glucoside + H2O
beta-D-glucose + estrone
-
poor activity
-
?
ethyl beta-D-glucopyranoside + H2O
?
-
14.6% activity compared to ginsenoside Rg3
-
-
?
geniposide + H2O
geniposide aglycone + D-glucose
-
-
-
?
genistein 7-beta-D-glucopyranoside + H2O
genistein + D-glucose
-
-
-
?
genistein 7-O-(6''-O-malonyl-beta-D-glucoside) + H2O
genistein + 6-O-malonyl-beta-D-glucose
preferred substrate
-
-
?
genistein 7-O-(6-O-malonyl)beta-D-glucopyranoside + H2O
beta-D-glucose + genistein
-
the specific activity of a recombinant enzyme for isoflavones in order of decreasing activity: daidzin, glycitin, genistin, malonyl genistin, malonyl daidzin, malonyl glycitin
-
-
?
genistein 7-O-beta-D-glucoside + H2O
genistein + beta-D-glucose
low activity
-
-
?
genistein-7-O-beta-D-glucosyl-6''-O-acetate + H2O
genistein + 6-O-acetyl-beta-D-glucose
-
-
-
?
genistein-7-O-beta-D-glucosyl-6''-O-malonate + H2O
genistein + 6-O-malonyl-beta-D-glucose
-
-
-
-
?
genistein-7-O-glucosyl-6''-O-malonate + H2O
genistein + beta-D-glucose-6-O-malonate
-
-
-
-
?
gentibiose + H2O
2 beta-D-glucose
-
54% activity compared to cellobiose
-
-
?
gentiopentaose + 4 H2O
5 D-glucose
-
specific for beta-1,6-linkages, activity decreases with number of glucose residues
-
?
ginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
-
ginsenoside Rg1 i.e. 6alpha,20-bis(beta-D-glucopyranosyl)oxy-dammar-24-en-3beta,12beta-diol
-
?
ginsenoside Rb1 + 3 H2O
(3beta,5xi,6alpha,12beta,13xi)-3,6,12-trihydroxydammar-24-en-20-yl beta-D-glucopyranoside + 3 beta-D-glucose
ginsenoside Rb1 + H2O
? + beta-D-glucose
-
63% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
ginsenoside Rb2 + 2 H2O
(3beta,5xi,6alpha,12beta,13xi)-3,6,12-trihydroxydammar-24-en-20-yl 6-O-alpha-L-arabinopyranosyl-beta-D-glucopyranoside + 2 beta-D-glucose
-
-
i.e. compound Y
-
?
ginsenoside Rb3 + H2O
20-O-beta -D-xylopyranosyl-1,6-beta-D-glucopyranosyl-20(S)-protopanaxadiol + beta-D-glucose
-
-
i.e. compound Mx
-
?
ginsenoside Rc + H2O
(3beta,5xi,6alpha,12beta,13xi)-3,6,12-trihydroxydammar-24-en-20-yl 6-O-beta-D-xylopyranosyl-beta-D-glucopyranoside + beta-D-glucose
-
-
i.e. compound Mc
-
?
ginsenoside Re + H2O
ginsenoside Rg1 + L-rhamnose
ginsenoside Re i.e. 20-(beta-D-glucopyranosyl)oxy-6alpha-[alpha-L-rhamnopyranosyl-(1->2)-beta-D-glucopyranosyloxy]dammar-24-en-3beta,12beta-diol
ginsenoside Rg1 i.e. 6alpha,20-bis(beta-D-glucopyranosyl)oxy-dammar-24-en-3beta,12beta-diol
-
?
ginsenoside Rg3 + H2O
ginsenoside Rh2 + D-glucose
-
100% activity, the enzyme hydrolyzes the 3-C, beta-(1-2)-glucoside of ginsenoside Rg3 to produce ginsenoside Rh2, but does not sequentially hydrolyze the beta-D-glucosidic bond of ginsenoside Rh2
-
-
?
Glc3Man9GlcNAc2 + H2O
Glc2Man9GlcNAc2 + beta-D-glucose
-
important in processing of oligosaccharides after their transfer from dolichyl diphosphate to proteins during glycoprotein synthesis
-
?
glucogitoroside + H2O
gitoroside + beta-D-glucose
-
38% of activity with glucoevatromonoside
-
-
?
glucoquinovosidodigitoxigenin + H2O
quinovosidodigitoxigenin + beta-D-glucose
-
38% of activity with glucoevatromonoside
-
-
?
glucosyl ceramide + H2O
sphingosine + fatty acid + beta-D-glucose
-
involved in normal catabolism of glucosyl ceramides
-
?
glycitein 7-O-(6-O-malonyl)beta-D-glucopyranoside + H2O
beta-D-glucose + glycitein
-
the specific activity of a recombinant enzyme for isoflavones in order of decreasing activity: daidzin, glycitin, genistin, malonyl genistin, malonyl daidzin, malonyl glycitin
-
-
?
glycitein 7-O-beta-D-glucopyranoside + H2O
glycitein + D-glucose
-
-
-
?
glycitein-7-O-beta-D-glucopyranoside + H2O
glycitein + beta-D-glucose
-
-
-
?
glycitein-7-O-beta-D-glucosyl-6''-O-acetate + H2O
glycitein + 6-O-acetyl-beta-D-glucose
-
-
-
?
hesperetin 7-O-beta-glucopyranoside + H2O
hesperetin + beta-D-glucose
-
199% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
hesperitin-dihydrochalcon 7-O-beta-D-glucopyranoside + H2O
hesperitin-dihydrochalcon + beta-D-glucose
-
91% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
hexyl beta-D-glucopyranoside + H2O
?
-
53.7% activity compared to ginsenoside Rg3
-
-
?
hexyl-beta-D-glucopyranoside + H2O
hexanol + beta-D-glucose
-
15% of activity with p-nitrophenyl-beta-d-glucopyranoside
-
-
?
insoluble cellooligosaccharaide + H2O
beta-D-glucose + ?
-
beta-glucosidase 3 less active
-
?
ipecoside + H2O
?
586% of the efficiency with N-deacetylipecoside
-
-
?
isopropyl beta-D-glucopyranoside + H2O
?
-
9.8% activity compared to ginsenoside Rg3
-
-
?
lactose + H2O
beta-D-glucose + D-galactose
-
34% activity compared to cellobiose
-
-
?
lactose + N,N'-diacetylchitobiose
Gal-beta-(1->4)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc + H2O
laminaran + H2O
D-glucose + ?
Littorina kurila
-
-
single product, enzyme retains the anomeric center configuration
-
?
laminaran + H2O
D-glucose + gentiobiose + gentiotriose
67% of the activity with laminaribiose
-
-
?
laminaribiose + H2O
?
beta-(1-3)-linked laminaribose, 55.7% activity compared to n-octyl beta-D-glucopyranoside
-
-
?
laminaribiose + H2O
beta-D-glucose + ?
-
very low activity with cellobiose, cellotriose, cellotetraose, cellopentaose and gentibiose
-
-
?
laminaripentaose + H2O
laminaritetraose + D-glucose
-
-
-
?
laminaritriose + H2O
?
7.43% activity compared to n-octyl beta-D-glucopyranoside
-
-
?
laminaritriose + H2O
D-glucose + ?
-
97% of the activity with laminaribiose
-
?
linalool-beta-D-glucopyranoside + H2O
linalool + beta-D-glucose
-
-
-
-
?
linamarin + H2O
alpha-hydroxyisobutyronitrile + D-glucose
-
34% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
lotaustralin + H2O
(2R)-2-hydroxy-2-methylbutanenitrile + D-glucose
-
-
-
-
?
lucumin + H2O
HCN + ?
-
low activity for PGI, very low activity for PGII
-
?
luteolin-3',7-dibeta-D-glucopyranoside + H2O
luteolin + beta-D-glucose
-
-
-
-
?
luteolin-beta-D-glucoside + H2O
luteolin + beta-D-glucose
-
weak activity
-
-
?
mandelonitrile-beta-D-glucopyranoside + H2O
mandelonitrile + beta-D-glucose
-
trivial name prunasin, 309% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
methyl tuberonic acid beta-D-glucoside + H2O
methyl tuberonic acid + beta-D-glucose
-
i.e. 12-hydroxyjasmonic acid beta-d-glucosid methyl ester, 80% relative activity compared to hydrolysis of tuberonic acid beta-D-glucoside
-
-
?
methyl-beta-D-glucopyranoside + H2O
methanol + beta-D-glucopyranose
-
-
-
-
?
methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + beta-D-glucose
-
-
-
?
N,N'-diacetyl-beta-chitobiose + H2O
N-acetyl-D-glucosamine
-
-
-
?
N-acetyl-D-glucosamine + lactose
4-O-beta-D-galactopyranosyl-N-acetyl-D-glucosamine + D-glucose
-
transgalactosylation reaction
-
?
N-acetylglucosamine + lactose
Gal-beta-(1->4)-GlcNAc + D-glucose
-
transgalactosylation reaction
-
?
n-decyl beta-D-glucoside + H2O
beta-D-glucose + n-decanol
-
6fold higher activity than with methyl-beta-D-glucoside
-
?
n-decyl-beta-D-glucopyranoside + H2O
n-decanol + beta-D-glucopyranose
11% relative activity
-
-
?
n-dodecyl-beta-D-glucopyranoside + H2O
n-dodecanol + D-Glucose
-
26% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
n-heptyl-beta-D-glucopyranoside + H2O
n-heptanol + beta-D-glucopyranose
17% relative activity
-
-
?
n-heptyl-beta-D-glucoside + H2O
?
29.5% activity compared to n-octyl beta-D-glucopyranoside
-
-
?
n-octyl-beta-D-glucopyranoside + H2O
n-octanol + beta-D-glucopyranose
7% relative activity
-
-
?
n-octyl-beta-D-glucopyranoside + H2O
n-octanol + beta-D-glucose
-
-
-
-
?
o-nitrophenyl-beta-D-fucopyranoside + H2O
o-nitrophenol + beta-D-fucopyranose
117% relative activity
-
-
?
o-nitrophenyl-beta-D-galactopyranoside + H2O
o-nitrophenol + beta-D-galactopyranose
17% relative activity
-
-
?
o-nitrophenyl-beta-D-glucopyranose + H2O
o-nitrophenol + beta-D-glucose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucose
-
-
-
?
p-nitrophenyl-alpha-D-arabinofuranoside + H2O
p-nitrophenol + alpha-D-arabinose
-
3.7% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-galactopyranoside + H2O
p-nitrophenol + alpha-D-galactose
-
-
-
-
?
p-nitrophenyl-alpha-D-rhamnopyranoside + H2O
p-nitrophenol + alpha-D-rhamnose
-
1.9% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-L-arabinopyranoside + H2O
p-nitrophenol + alpha-L-arabinose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobiose + H2O
p-nitrophenyl-beta-D-glucopyranoside + beta-D-glucose
-
-
-
?
p-nitrophenyl-beta-D-fucoopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
-
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucopyranose
71% relative activity
-
-
?
p-nitrophenyl-beta-D-glucopyranose + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucosamine
p-nitrophenyl-beta-D-glucopyranoside + beta-D-glucosamine
p-nitrophenyl-beta-D-mannopyranoside + H2O
p-nitrophenol + beta-D-mannose
-
-
-
-
?
p-nitrophenyl-beta-L-arabinopyranoside + H2O
p-nitrophenol + beta-L-arabinose
-
-
-
-
?
phenyl-beta-D-glucopyranoside + H2O
phenol + beta-D-glucose
-
-
-
-
?
phenylethyl-beta-D-galactoside + H2O
phenylethanol + beta-D-galactose
-
very poor substrate
-
?
phloridzin + H2O
phloridzin aglycone + D-glucose
-
-
-
?
podophyllotoxin-4-O-beta-D-glucopyranoside + H2O
podophyllotoxin + beta-D-glucose
-
-
-
-
?
propenyl beta-D-glucopyranoside + H2O
?
-
26.8% activity compared to ginsenoside Rg3
-
-
?
propyl beta-D-glucopyranoside + H2O
?
-
31.7% activity compared to ginsenoside Rg3
-
-
?
pyridoxine + D-galactose
7-O-(alpha-D-galactopyranosyl)pyridoxine + 7-O-(beta-D-galactopyranosyl)pyridoxine + 6-O-(alpha-D-galactopyranosyl)pyridoxine
-
-
yield 40%, with 27% 7-O-(alpha-D-galactopyranosyl)pyridoxine, 26% 7-O-(beta-D-galactopyranosyl)pyridoxine, and 47% 6-O-(alpha-D-galactopyranosyl)pyridoxine
-
?
pyridoxine + D-glucose
7-O-(alpha-D-glucopyranosyl)pyridoxine + 7-O-(beta-D-glucopyranosyl)pyridoxine + 6-O-(alpha-D-glucopyranosyl)pyridoxine
-
-
yield 36%, with 39% 7-O-(alpha-D-glucopyranosyl)pyridoxine, 41% 7-O-(beta-D-glucopyranosyl)pyridoxine and 20% 6-O-(alpha-D-glucopyranosyl)pyridoxine
-
?
pyridoxine + D-mannose
7-O-(alpha-D-mannopyranosyl)pyridoxine + 7-O-(beta-D-mannopyranosyl)pyridoxine + 6-O-(alpha-D-mannopyranosyl)pyridoxine
-
-
yield 23%, with 34% 7-O-(alpha-D-mannopyranosyl)pyridoxine, 42% 7-O-(beta-D-mannopyranosyl)pyridoxine, and 24% 6-O-(alpha-D-mannopyranosyl)pyridoxine
-
?
quercetin 3,4'-O-di-beta-D-glucopyranoside + H2O
quercetin + 2 beta-D-glucose
-
-
-
-
?
rhodiocyanoside A + H2O
(Z)-4-hydroxy-2-methyl-2-butenenitrile + D-glucose
-
-
-
-
?
saccharose + H2O
D-glucose + D-fructose
-
-
5% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
?
salicin + H2O
salicyl alcohol + D-glucose
-
at 70% of the rate with cellobiose
-
-
?
salicylic acid-beta-D-glucoside + H2O
beta-D-glucose + salicylate
-
low activity
-
?
samibunigrin + H2O
HCN + ?
-
best substrate for PGI and PGII
-
?
scopolin + H2O
scopoletin + beta-D-glucose
-
-
-
?
sinigrin + H2O
beta-D-glucose + ?
-
325% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
sophorose + H2O
?
beta-(1-2)-linked sophorose, 31.9% activity compared to n-octyl beta-D-glucopyranoside
-
-
?
stevioside + H2O
rubusoside + D-glucose
-
i.e. 13-O-beta-glucosyl-19-O-beta-D-glucosyl-steviol, the optimum rubusoside synthesis yield is 86% at 200 g/l with 1200 units lactase
-
?
strictosidine + H2O
?
12.6% of the efficiency with N-deacetylipecoside
-
-
?
taxiphyllin + H2O
4-hydroxybenzaldehyde + hydrogen cyanide + D-glucose
-
-
-
-
?
vincoside + H2O
?
25.1% of the efficiency with N-deacetylipecoside
-
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
lower activity for beta-glucosidase 3
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
lower activity for beta-glucosidase 3
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
-
-
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
thermophilic anaerobic bacterium
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
thermophilic anaerobic bacterium
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
lower activity for beta-glucosidase II
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
low activity
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
salicin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
product 4-hydroxyphenol toxic to invading pathogens
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
contribution to cyanide toxicity in ruminants
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
product 4-hydroxyphenol toxic to invading pathogens
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
low activity
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
arbutin
-
?
(4-hydroxyphenyl)-beta-D-glucopyranoside + H2O
4-hydroxyphenol + beta-D-glucopyranose
-
lower activity for beta-glucosidase II
-
?
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
HCN + ?
-
amygdalin
-
?
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
HCN + ?
-
amygdalin
-
?
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
HCN + ?
-
amygdalin
-
?
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
HCN + ?
-
amygdalin
-
?
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
HCN + ?
-
amygdalin
-
?
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
HCN + ?
-
less active
-
?
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
HCN + ?
-
amygdalin
-
?
(R)-alpha-[(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]benzeneacetonitrile + H2O
HCN + ?
-
amygdalin
-
?
2,4-dihydroxy-1,4-benzoxazin-3-one glucoside + H2O
?
-
-
-
?
2,4-dihydroxy-1,4-benzoxazin-3-one glucoside + H2O
?
best substrate for isoform GLU1
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
very low activity
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
35% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
low activity
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
thermophilic anaerobic bacterium
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
low activity
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
2% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside 6-phosphate + H2O
2-nitrophenol + beta-D-galactopyranose 6-phosphate
-
-
?
2-nitrophenyl beta-D-galactopyranoside 6-phosphate + H2O
2-nitrophenol + beta-D-galactopyranose 6-phosphate
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
51% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
51% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
109% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
131% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
131% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
best substrate
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
95% relative activity
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
83% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
retention of configuration
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
retention of configuration
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
thermophilic anaerobic bacterium
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
-
very low activity
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
Lenzites trabea
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
-
-
-
?
2-nitrophenyl cellobioside + H2O
beta-D-glucose + ?
-
-
-
?
2-nitrophenyl cellobioside + H2O
beta-D-glucose + ?
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-demethoxy-1,4-benzoxazin-3-one + beta-D-glucose
Ser464 and Leu465 are critical in the substrate specificity for the substrate of isozyme TaGlu1a
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one + beta-D-glucose
Ser464 and Leu465 are critical in the substrate specificity for the substrate of isozyme TaGlu1a
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
i.e. DIMBOA-glucoside
-
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
specific for beta-1,2-, -1,3- or -1,4-hydrolysis
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
lower activity for beta-glucosidase II
-
?
2-phenylethyl beta-D-glucopyranoside + H2O
2-phenylethanol + beta-D-glucose
-
-
2-phenylethanol is a flower sent compound
-
?
2-phenylethyl beta-D-glucopyranoside + H2O
2-phenylethanol + beta-D-glucose
-
best substrate, poor activity with 2-phenylethyl beta-D-galactopyranoside, no activity with 2-phenylethyl beta-D-xylopyranoside
-
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
r
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
high activity on short oligosaccharides, decreasing activity for higher oligosaccharides, transglycosylation reaction
-
r
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
not restricted to the beta-D-1,4-linkage
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
very low activity
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
very low activity
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
r
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
transglycoslation activity
-
r
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
preference for beta-1,3-bonds
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
lower activity for beta-glucosidase II
-
?
4-chlorophenyl beta-D-glucopyranoside + H2O
?
-
227% activity compared to ginsenoside Rg3
-
-
?
4-chlorophenyl beta-D-glucopyranoside + H2O
?
-
227% activity compared to ginsenoside Rg3
-
-
?
4-hydroxybenzyl beta-D-glucopyranoside + H2O
?
-
551% activity compared to ginsenoside Rg3
-
-
?
4-hydroxybenzyl beta-D-glucopyranoside + H2O
?
-
551% activity compared to ginsenoside Rg3
-
-
?
4-methoxybenzyl beta-D-glucopyranoside + H2O
?
-
73.2% activity compared to ginsenoside Rg3
-
-
?
4-methoxybenzyl beta-D-glucopyranoside + H2O
?
-
73.2% activity compared to ginsenoside Rg3
-
-
?
4-methylumbelliferyl beta-D-cellobioside + 2 H2O
4-methylumbelliferol + 2 D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + 2 H2O
4-methylumbelliferol + 2 D-glucose
native beta-glucosidase substrate, 14.9% relative activity compared to 4-nitrophenyl-beta-D-glucopyranoside as substrate
-
-
?
4-methylumbelliferyl beta-D-cellobioside + 2 H2O
4-methylumbelliferol + 2 D-glucose
native beta-glucosidase substrate, 14.9% relative activity compared to 4-nitrophenyl beta-D-glucopyranoside as substrate
-
-
?
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + beta-D-glucose
-
63% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-methylumbelliferyl-beta-D-cellobiose + H2O
4-methylumbelliferyl-beta-D-glucopyranoside + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellobiose + H2O
4-methylumbelliferyl-beta-D-glucopyranoside + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
high activity
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
hydrolysis of glucose residues from both ends in an exo-fashion
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
presence of sphingolipid binding site, possible role in glycosphingolipid metabolism
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
-
-
-
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
7% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
6% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
2.7% of the activity with 4-nitrophenyl alpha-D-glucopyranoside
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
almost no activity
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
[Humicola] grisea var. thermoidea IFO 9854
-
-
-
-
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
3.9% of the activity with 4-nitrophenyl alpha-D-glucopyranoside
-
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
low activity
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
very low activity
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
-
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
Lenzites trabea
-
-
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
-
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
cleaves beta-glucosidic linkages one by one at the non-reducing end only
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
-
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 D-glucose
-
-
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 D-glucose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
Melanocarpus sp.
-
low activity
-
-
?
4-nitrophenyl beta-D-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
low activity
-
-
?
4-nitrophenyl beta-D-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
13% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
11.6% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
Thermotoga petrophila DSM 13996
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
low activity
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + D-cellobiose
about 10% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
-
455% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
Lenzites trabea
-
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
415% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
relative activity of 125% as compared to 4-nitrophenyl beta-D-glucopyranoside. Maximum hydrolytic activity for beta-D-fucopyranoside followed by 4-nitrophenyl beta-D-glucopyranoside and 4-nitrophenyl beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
75% of the activity with 4-nitrophenyl beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
-
best synthetic substrate
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
high activity
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + D-fucopyranose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + D-fucopyranose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + D-fucopyranose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
transferase activity for the beta-D-fucosyl group, not for a beta-D-glucosyl group, fucosidase activity specific for intestinal flora
-
r
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
low activity
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
41% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
maximum hydrolytic activity for beta-D-fucopyranoside followed by 4-nitrophenyl beta-D-glucopyranoside and 4-nitrophenyl beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
8.4% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
8.4% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
Bacillus sp. ZJ1308
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
0.1% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
low activity
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
Thermotoga petrophila DSM 13996
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
8.3% relative activity compared to 4-nitrophenyl-beta-D-glucopyranoside as substrate
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
29.4% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
Jeotgalibacillus malaysiensis DSM 28777T
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
best substrate for isoform GLU4
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
maximum hydrolytic activity for beta-D-fucopyranoside followed by 4-nitrophenyl beta-D-glucopyranoside and 4-nitrophenyl beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
71% of the activity with 4-nitrophenyl beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
hydrolysis of beta-linkages
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
Bacillus sp. ZJ1308
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
Bacillus subtilis RA10
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
the enzyme catalysed both hydrolysis and transglycosylation
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
aryl beta-glucosidase activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
high activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
Littorina kurila
-
1000% of the activity with laminaran
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
Melanocarpus sp.
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
best substrate
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
best substrate
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
best substrate
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
Paecilomyces sp. (in: Eurotiomycetes) 220 Bainier
-
best substrate
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
best substrate
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
hydrolysis of beta-linkages
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
poor activity with 4-nitrophenyl-beta-D-galactopyranoside, no activity with 4-nitrophenyl-beta-D-xylopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
hydrolysis of beta-linkages
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
hydrolysis of beta-linkages
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
when the enzyme iss incubated with 4-nitrophenyl-beta-D-glucopyranoside in the presence of ethanol and propanol, the glucose moiety is transferred to acceptor alcohols
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
when the enzyme iss incubated with 4-nitrophenyl-beta-D-glucopyranoside in the presence of ethanol and propanol, the glucose moiety is transferred to acceptor alcohols
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
implicated in beta-glucan degradation through synergistic action with beta-glucanases
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
100% relative activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
100% activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
best substrate
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
high activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
less active than on cellobiose
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
one of two cloned genes are only active on this substrate
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
very low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
very low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
100% activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Halalkalibacterium halodurans
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Lenzites trabea
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
100% activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Mucor psychrophilus
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
highest activity against aryl-beta-1,4-glucosides
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
100% activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
activity measured in total fly homogenates, substrate concentration of 60 mM in citrate buffer
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
best substrate
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
higher activity than on cellobiose
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
temperature directed substrate specificity for aryl beta-1,4-linkage
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
substrate with highest affinity
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Sporotrichum pulverulentum
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
single active centre, containing one catalytic site and one saccharide-binding site, major binding determinant is the aglycone moiety, that influences the binding of the carbohydrate moiety
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
100% activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
100% activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
one of the two best substrates
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
the enzyme had higher specific activity against 4-nitrophenyl beta-D-glucopyranoside than cellobiose
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
the enzyme had higher specific activity against 4-nitrophenyl beta-D-glucopyranoside than cellobiose
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Thermochaetoides thermophila
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
quite specific for beta-1,4-linkages
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
best substrate
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
thermophilic anaerobic bacterium
-
best substrate
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Thermotoga petrophila DSM 13996
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
specific for beta-configuration of sugars
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
relatively specific for aryl-beta-D-linked glucopyranoside substrates
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
highest specific activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
EU918770
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
EU918770
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
100% relative activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
nitrophenol + D-glucose
H0HC94
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
nitrophenol + D-glucose
H0HC94
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
178% relative activity compared to hydrolysis of tuberonic acid beta-D-glucoside
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
the enzyme catalyses both hydrolysis and transglycosylation
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
the enzyme catalysed both hydrolysis and transglycosylation
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
very low activity
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Lenzites trabea
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
low activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
11% of the activity with 4-nitrophenyl beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
lowest specific activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
very low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
46% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
low activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
low activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
thermophilic anaerobic bacterium
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
highly active
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
highly active
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
Thermotoga petrophila DSM 13996
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
-
-
-
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl beta-L-arabinopyranoside + H2O
4-nitrophenol + beta-L-arabinopyranose
-
low activity
-
-
?
4-nitrophenyl beta-L-arabinopyranoside + H2O
4-nitrophenol + beta-L-arabinopyranose
-
-
-
?
4-nitrophenyl-alpha-D-glucoside
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl-alpha-D-glucoside
4-nitrophenol + alpha-D-glucose
-
less, but significant hydrolysis
-
?
4-nitrophenyl-alpha-D-glucoside
4-nitrophenol + alpha-D-glucose
-
less, but significant hydrolysis
-
?
4-nitrophenyl-alpha-D-glucoside
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl-alpha-D-glucoside
4-nitrophenol + alpha-D-glucose
-
less, but significant hydrolysis
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
-
-
-
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
-
-
-
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
-
-
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
-
-
-
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
?
4-nitrophenyl-beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl-beta-D-glucoside + H2O
4-nitrophenol + D-glucose
Listeria innocua Clip11262 ATCC BAA-680
-
-
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
maltose
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
maltose
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
maltose
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
only beta-glucosidase II
-
?
4-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
2 D-mannose
-
-
-
?
4-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
2 D-mannose
-
-
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
low activity
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
low activity
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
thermophilic anaerobic bacterium
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
low activity
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
high activity on short oligosaccharides, decreasing activity for higher oligosaccharides
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity for beta-glucosidase 3
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity for beta-glucosidase 3
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
additional product: cellotetraose as the product of transglycosylation
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
hydrophobic-driven binding of the glucose residue at subsite 2 of 2 main binding-modes of beta-glucosidase
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
synergistic action of Trichoderma reesei and Aspergillus wentii cellulases for cellulose hydrolysis
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
only one of two cloned genes is active on cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycolsylation reaction, yielding alcohol-beta-glucosides in the presence of alcohols
-
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
complete hydrolsis of barley endosperm cell wall through synergistic action of endo(1-3,1-4)-beta-glucanase and beta-glucosidase
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
Lenzites trabea
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
cellobiose
-
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
additional product: cellotriose by transglycosylation activity
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
transglycosylation activity through a third sub-site, ability to accommodate substrates longer than cellobiose
-
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
less active
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
additional product: cellotriose by transglycosylation activity
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
activity 60fold less than for 4-nitrophenyl-beta-D-glucopyranoside
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
additional product: cellotetraose as the product of transglycosylation
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
promoting action of 1,4-beta-cellobiohydrolase
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
Sporotrichum pulverulentum
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
one of the two best substrates
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cloned enzyme show greater activity against cellobiose than against aryl-beta-D-glucosides
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
Thermochaetoides thermophila
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
Thermochaetoides thermophila
-
no activity for aryl-beta-D-glucosidases
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
cellobiose
additional product: cellotriose by transglycosylation activity
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
transglycolsylation reaction, yielding alcohol-beta-glucosides in the presence of alcohols
additional product: cellotriose by transglycosylation activity
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycosylation reaction
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycosylation reaction
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycosylation reaction
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycosylation reaction
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
amygdalin + 2 H2O
mandelonitrile + 2 beta-D-glucose
-
22% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
amygdalin + 2 H2O
mandelonitrile + 2 beta-D-glucose
-
68% of activity with gentiobiose
-
-
?
amygdalin + 2 H2O
mandelonitrile + 2 beta-D-glucose
-
80% of activity with gentiobiose
-
-
?
amygdalin + 2 H2O
mandelonitrile + 2 beta-D-glucose
-
19% of the activity with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
amygdalin + H2O
?
-
11.3% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
amygdalin + H2O
?
-
11.3% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
apigenin-7-beta-D-glucopyranoside + H2O
apigenin + beta-D-glucose
-
-
-
-
?
arbutin + H2O
4-hydroxyphenol + beta-D-glucose
-
104% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
arbutin + H2O
hydroquinol + beta-D-glucose
-
10% of activity with gentiobiose
-
-
?
arbutin + H2O
hydroquinol + beta-D-glucose
-
8% of activity with gentiobiose
-
-
?
avenacoside + H2O
C26-desgluco-avenacosides + beta-D-glucose
-
the enzyme hydrolyzes the avenacosides to combat fungal attack
-
-
?
Avicel + H2O
beta-D-glucose + ?
0.9% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
Avicel + H2O
beta-D-glucose + ?
0.9% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
Avicel + H2O
beta-D-glucose + ?
-
acid-swollen, low activity
-
?
benzyl-beta-D-glucopyranoside + H2O
benzyl alcohol + beta-D-glucose
-
17% of activity with p-nitrophenyl-beta-d-glucopyranoside
-
-
?
benzyl-beta-D-glucopyranoside + H2O
benzyl alcohol + beta-D-glucose
-
-
-
-
?
beta-D-fructofuranosyl-alpha-D-glucopyranoside + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
-
low activity
-
?
beta-D-fructofuranosyl-alpha-D-glucopyranoside + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
-
-
-
?
beta-gentiobiose + H2O
2 D-glucose
-
6.2% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
carboxymethyl-cellulose + H2O
beta-D-glucose + ?
-
low activity
-
?
carboxymethyl-cellulose + H2O
beta-D-glucose + ?
-
low activity
-
?
carboxymethyl-cellulose + H2O
beta-D-glucose + ?
-
low activity
-
?
cellobiose + H2O
2 beta-D-glucose
-
15-30% of activity with p-nitrophenyl-beta-d-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
the specific activity towards cellobiose is higher than towards 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
Bgs also has transglucosidic activity
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
interaction between the sugar rings and aromatic ring of W293 at the entrance of the catalytic pocket enhances the substrate recognition of beta-glucosidase
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
609% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
3.6% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
-
22% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
?
cellobiose + H2O
2 beta-D-glucose
BglA is highly specific for cellobiose, BglB acts as an exo-beta-glucosidase hydrolyzing cellobiose and cellodextrins of higher degree of polymerization
-
-
?
cellobiose + H2O
2 beta-D-glucose
BGL has significant lower affinity for cellobiose compared with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
BGL has significant lower affinity for cellobiose compared with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
28% of activity with gentiobiose
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
74% of activity with gentiobiose
-
-
?
cellobiose + H2O
2 beta-D-glucose
substrate of isozyme BGL1B, but not of isozyme BGL1A
-
-
?
cellobiose + H2O
2 beta-D-glucose
49.4% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
49.4% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
low activity, the specific activity towards cellobiose is lower than towards 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
Thermochaetoides thermophila
-
0.5% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
89% of activity with p-nitrophenyl-beta-D-glucose
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
89% of activity with p-nitrophenyl-beta-D-glucose
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
low activity, the specific activity towards cellobiose is lower than towards 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
best natural substrate
-
-
?
cellobiose + H2O
2 D-glucose
17.5% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 D-glucose
17.5% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 D-glucose
-
62% of the activity with laminaribiose
-
?
cellobiose + H2O
2 D-glucose
-
100% of the activity with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 D-glucose
the highest activity with cellobiose as the substrate approaches 1.7 U/g, native enzyme and enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde
-
-
?
cellobiose + H2O
2 D-glucose
the highest activity with cellobiose as the substrate approaches 1.7 U/g, native enzyme and enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde
-
-
?
cellobiose + H2O
2 D-glucose
native beta-glucosidase substrate, 26.4% relative activity compared to 4-nitrophenyl-beta-D-glucopyranoside as substrate
-
-
?
cellobiose + H2O
?
highest specific activity
-
-
?
cellobiose + H2O
beta-D-glucose + alpha-D-glucose
-
low activity
-
-
?
cellobiose + H2O
beta-D-glucose + alpha-D-glucose
Paecilomyces sp. (in: Eurotiomycetes) 220 Bainier
-
low activity
-
-
?
cellobiose + H2O
beta-D-glucose + alpha-D-glucose
-
low activity
-
-
?
cellohexaose + 5 H2O
6 D-glucose
-
marked increase of relative activity for chimeric enzymes
-
?
cellohexaose + 5 H2O
6 D-glucose
-
low activity for beta-glucosidase 3
-
?
cellohexaose + 5 H2O
6 D-glucose
-
marked increase of relative activity for chimeric enzymes
-
?
cellopentaose + 4 H2O
5 D-glucose
-
marked increase of relative activity for chimeric enzyme
-
?
cellopentaose + 4 H2O
5 D-glucose
-
low activity for beta-glucosidase 3
-
?
cellopentaose + 4 H2O
5 D-glucose
-
marked increase of relative activity for chimeric enzyme
-
?
cellopentaose + 4 H2O
5 D-glucose
7.8% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellotetraose + 3 H2O
4 beta-D-glucose
substrate binding site and structure, overview
-
-
?
cellotetraose + 3 H2O
4 D-glucose
-
marked increase of relative activity for chimeric activity
-
?
cellotetraose + 3 H2O
4 D-glucose
-
low activity for beta-glucosidase 3
-
?
cellotetraose + 3 H2O
4 D-glucose
-
marked increase of relative activity for chimeric activity
-
?
cellotetraose + 3 H2O
4 D-glucose
11% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellotetraose + H2O
beta-D-glucose + ?
-
125% activity compared to cellobiose
-
-
?
cellotetraose + H2O
beta-D-glucose + ?
Jeotgalibacillus malaysiensis DSM 28777T
-
125% activity compared to cellobiose
-
-
?
cellotriose + 2 H2O
3 D-glucose
-
low activity for beta-glucosidase 3
-
?
cellotriose + 2 H2O
3 D-glucose
12.7% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellulose + H2O
beta-D-glucose + ?
-
cellulose MN 300
-
?
cyanidin-3-O-beta-D-glucoside + H2O
cyanidin + beta-D-glucose
-
the enzyme is involved in anthocyanin metabolism, overview
-
-
?
D-cellobiono-1,5-lactone + H2O
D-glucose + D-glucono-1,5-lactone
-
-
-
?
D-cellobiono-1,5-lactone + H2O
D-glucose + D-glucono-1,5-lactone
substrate of isozyme BGL1B, but not of isozyme BGL1A
-
-
?
daidzein 7'-O-(6''-O-beta-D-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
-
-
-
?
daidzein 7'-O-(6''-O-beta-D-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
-
-
?
daidzein 7-O-(6-O-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
-
-
-
?
daidzein 7-O-(6-O-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
-
-
?
daidzein 7-O-(6-O-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
-
-
-
?
daidzein 7-O-(6-O-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
-
-
-
?
daidzein 7-O-(6-O-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
-
-
-
?
daidzein 7-O-beta-D-glucopyranoside + H2O
daidzein + beta-D-glucose
-
-
-
?
daidzein-7-O-beta-D-glucopyranoside + H2O
daidzein + beta-D-glucose
-
-
-
?
daidzein-7-O-beta-D-glucopyranoside + H2O
daidzein + beta-D-glucose
-
-
-
-
?
daidzein-7-O-beta-D-glucopyranoside + H2O
daidzein + beta-D-glucose
-
-
-
-
?
daidzein-7-O-beta-D-glucopyranoside + H2O
daidzein + D-glucose
-
-
-
?
daidzein-7-O-beta-D-glucopyranoside + H2O
daidzein + D-glucose
-
-
-
?
daidzin + H2O
beta-D-glucose + daidzein
-
-
-
?
daidzin + H2O
beta-D-glucose + daidzein
-
-
-
?
daidzin + H2O
beta-D-glucose + daidzein
-
the specific activity of a recombinant enzyme for isoflavones in order of decreasing activity: daidzin, glycitin, genistin, malonyl genistin, malonyl daidzin, malonyl glycitin
-
-
?
daidzin + H2O
daidzein + D-glucose
-
-
-
?
deltoside + H2O
?
-
specific degradation, oligofurostanoside-specific beta-glucosidase
-
-
?
dhurrin + H2O
(2S)-hydroxy(4-hydroxyphenyl)ethanenitrile + beta-D-glucose
-
-
-
-
?
dhurrin + H2O
(2S)-hydroxy(4-hydroxyphenyl)ethanenitrile + beta-D-glucose
-
-
-
?
dhurrin + H2O
(S)-4-hydroxymandelonitrile + D-glucose
-
-
-
?
dhurrin + H2O
(S)-4-hydroxymandelonitrile + D-glucose
best substrate for isoform GLU2
-
-
?
esculin + H2O
beta-D-glucose + 6,7-dihydroxycoumarin
thermophilic anaerobic bacterium
-
-
-
?
esculin + H2O
beta-D-glucose + esculetin
-
87% of activity with p-nitrophenyl-beta-D-glucose
-
-
?
esculin + H2O
beta-D-glucose + esculetin
-
87% of activity with p-nitrophenyl-beta-D-glucose
-
-
?
esculin + H2O
beta-D-glucose + esculetin
-
92% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
esculin + H2O
beta-D-glucose + esculetin
-
92% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
esculin + H2O
esculetin + beta-D-glucose
-
100% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
genistein-7-O-beta-D-glucopyranoside + H2O
genistein + beta-D-glucose
-
-
-
?
genistein-7-O-beta-D-glucopyranoside + H2O
genistein + beta-D-glucose
-
-
-
-
?
genistin + H2O
beta-D-glucose + genistein
-
-
-
?
genistin + H2O
beta-D-glucose + genistein
-
the specific activity of a recombinant enzyme for isoflavones in order of decreasing activity: daidzin, glycitin, genistin, malonyl genistin, malonyl daidzin, malonyl glycitin
-
-
?
genistin + H2O
beta-D-glucose + genistein
genistin solubilized in 10-40% dimethylsulfoxide is hydrolyzed to genistein with nearly 99% conversion, indicating that high concentrations of the water-insoluble isoflavone glycoside can be treated by the enzyme
-
-
?
genistin + H2O
beta-D-glucose + genistein
genistin solubilized in 10-40% dimethylsulfoxide is hydrolyzed to genistein with nearly 99% conversion, indicating that high concentrations of the water-insoluble isoflavone glycoside can be treated by the enzyme
-
-
?
genistin + H2O
genistein + D-glucose
-
-
-
?
gentiobiose + H2O
2 beta-D-glucose
-
91% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
gentiobiose + H2O
2 beta-D-glucose
-
483% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
gentiobiose + H2O
2 beta-D-glucose
-
2.5% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
gentobiose + H2O
2 D-glucose
-
52% of the activity with laminaribiose
-
?
geranyl-beta-D-glucopyranoside + H2O
geraniol + beta-D-glucose
-
62.7% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
geranyl-beta-D-glucopyranoside + H2O
geraniol + beta-D-glucose
-
-
-
-
?
ginsenoside Rb1 + 3 H2O
(3beta,5xi,6alpha,12beta,13xi)-3,6,12-trihydroxydammar-24-en-20-yl beta-D-glucopyranoside + 3 beta-D-glucose
-
-
-
-
?
ginsenoside Rb1 + 3 H2O
(3beta,5xi,6alpha,12beta,13xi)-3,6,12-trihydroxydammar-24-en-20-yl beta-D-glucopyranoside + 3 beta-D-glucose
-
-
i.e. compound K
-
?
glucovanillin + H2O
vanillin + beta-D-glucose
-
22% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
glucovanillin + H2O
vanillin + beta-D-glucose
-
22% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
glycitin + H2O
beta-D-glucose + glycitein
-
-
-
?
glycitin + H2O
beta-D-glucose + glycitein
-
the specific activity of a recombinant enzyme for isoflavones in order of decreasing activity: daidzin, glycitin, genistin, malonyl genistin, malonyl daidzin, malonyl glycitin
-
-
?
lactose + H2O
D-glucose + D-galactose
preparation of lactose-free pasteurized milk with a recombinant thermostable beta-glucosidase
-
-
?
lactose + N,N'-diacetylchitobiose
Gal-beta-(1->4)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc + H2O
-
-
-
?
lactose + N,N'-diacetylchitobiose
Gal-beta-(1->4)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc + H2O
-
-
-
?
laminaribiose + H2O
2 beta-D-glucose
-
67% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
laminaribiose + H2O
2 beta-D-glucose
-
519% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
laminarin + H2O
beta-D-glucose
-
39% of activity with gentiobiose
-
-
?
laminarin + H2O
beta-D-glucose
-
54% of activity with gentiobiose
-
-
?
laminarin + H2O
beta-D-glucose + ?
-
involvement in autolysis
-
?
laminarin + H2O
beta-D-glucose + ?
-
highest specific activity
-
-
?
laminarin + H2O
beta-D-glucose + ?
thermophilic anaerobic bacterium
-
low activity
-
?
laminarin + H2O
laminarioligosaccharides + D-glucose
-
100times lower activity than with cellobiose
-
-
?
laminarin + H2O
laminarioligosaccharides + D-glucose
-
-
-
?
laminarin + H2O
laminarioligosaccharides + D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
80% of the activity with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
-
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
low activity for beta-glucosidase 3
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
low activity
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
low activity
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
very low activity
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
-
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
low activity
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
low activity
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
-
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
very low activity
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
very low activity
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
beta-glucosidase II
-
-
?
methyl-beta-D-glucoside + H2O
beta-D-glucose + methanol
-
very low activity
-
?
n-octyl-beta-D-glucopyranoside + H2O
n-octanol + D-glucose
-
28% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
n-octyl-beta-D-glucopyranoside + H2O
n-octanol + D-glucose
-
28% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
n-octyl-beta-D-glucopyranoside + H2O
n-octanol + D-glucose
-
at 75% of the rate with cellobiose
-
-
?
naringenin-7-beta-glucopyranoside + H2O
naringenin + beta-D-glucose
-
138% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
o-nitrophenyl-beta-D-glucopyranoside + H2O
o-nitrophenol + beta-D-glucose
-
-
-
-
?
o-nitrophenyl-beta-D-glucopyranoside + H2O
o-nitrophenol + beta-D-glucose
-
-
-
-
?
o-nitrophenyl-beta-D-glucopyranoside + H2O
o-nitrophenol + beta-D-glucose
-
-
-
-
?
o-nitrophenyl-beta-D-glucopyranoside + H2O
o-nitrophenol + beta-D-glucose
-
-
-
-
?
octyl-beta-D-glucopyranoside + H2O
octanol + beta-D-glucose
-
15% of activity with p-nitrophenyl-beta-d-glucopyranoside
-
-
?
oligofurostanosides + H2O
?
-
the specific degradation of the oligofurostanosides helps to maintain their furostanol structure of steroid glycosides is necessary for their transport within the leaf and from the leaf to the rhizome
-
-
?
oligofurostanosides + H2O
?
-
specific degradation by the oligofurostanoside-specific beta-glucosidase
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannose
-
1.1% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannose
-
-
-
-
?
p-nitrophenyl-beta-D-arabinopyranoside + H2O
p-nitrophenol + beta-D-arabinose
-
-
-
-
?
p-nitrophenyl-beta-D-arabinopyranoside + H2O
p-nitrophenol + beta-D-arabinose
-
2% of activity with o-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-cellobioside
p-nitrophenyl-beta-D-glucopyranoside + beta-D-glucose
-
8% of activity with p-nitrophenyl-beta-D-glucose
-
-
?
p-nitrophenyl-beta-D-cellobioside
p-nitrophenyl-beta-D-glucopyranoside + beta-D-glucose
-
8% of activity with p-nitrophenyl-beta-D-glucose
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + beta-D-glucose
-
17% of activity with p-nitrophenyl-beta-d-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + beta-D-glucose
-
22% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
13.5% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
-
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
42% of activity with o-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
-
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
weak activity
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
215% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
215% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
54% of activity with o-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
weak activity
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
61% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
assay at pH 5.0, 37°C, reaction stopped by adding sodium carbonate
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
54% of activity with o-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
substrate specificity in descending order, arylglucosides, alkylglucosides and disaccharides
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
beta-Glu x also has transglucosylation activity
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
Thermochaetoides thermophila
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-glucosamine
p-nitrophenyl-beta-D-glucopyranoside + beta-D-glucosamine
-
27% of activity with p-nitrophenyl-beta-D-glucose
-
-
?
p-nitrophenyl-beta-D-glucosamine
p-nitrophenyl-beta-D-glucopyranoside + beta-D-glucosamine
-
27% of activity with p-nitrophenyl-beta-D-glucose
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
1.9% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
-
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
13% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
14% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
1% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
% of activity with o-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
-
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
-
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
weak activity
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
5% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
-
-
-
?
phenyl-beta-D-glucoside + H2O
phenol + beta-D-glucose
-
low activity
-
?
phenyl-beta-D-glucoside + H2O
phenol + beta-D-glucose
-
low activity
-
?
phenyl-beta-D-glucoside + H2O
phenol + beta-D-glucose
-
low activity
-
?
phenyl-beta-D-glucoside + H2O
phenol + beta-D-glucose
thermophilic anaerobic bacterium
-
low activity
-
?
piceid + H2O
resveratrol + beta-D-glucose
-
specific for, high activity
-
-
?
plumieride coumarate beta-D-glucoside + H2O
13-O-coumarylplumieride + beta-D-glucose
-
an iridoid beta-glucoside from Plumeria obtusa, i.e. white frangipani, flower, the Plumeria obtusa beta-glucosidase shows high specificity for its natural substrate, plumieride coumarate glucoside
-
-
?
plumieride coumarate beta-D-glucoside + H2O
13-O-coumarylplumieride + beta-D-glucose
-
an iridoid beta-glucoside from Plumeria obtusa, i.e. white frangipani, flower, substrate and product identification and structure determination by NMR, overview
-
-
?
prunasin + H2O
D-mandelonitrile + beta-D-glucose
39% relative activity
-
-
?
prunasin + H2O
D-mandelonitrile + beta-D-glucose
-
27% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
prunasin + H2O
D-mandelonitrile + beta-D-glucose
-
27% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
prunasin + H2O
D-mandelonitrile + beta-D-glucose
-
57% of activity with o-nitrophenyl-beta-D-glucopyranoside
-
-
?
prunasin + H2O
D-mandelonitrile + beta-D-glucose
-
300% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
prunasin + H2O
D-mandelonitrile + beta-D-glucose
-
300% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
quercetin 3,4'-O-di-beta-D-glucopyranoside + 2 H2O
quercetin + 2 D-glucose
-
-
-
?
quercetin 3,4'-O-di-beta-D-glucopyranoside + 2 H2O
quercetin + 2 D-glucose
-
-
-
?
quercetin 3-O-beta-D-glucopyranoside + H2O
quercetin + D-glucose
-
-
-
?
quercetin 3-O-beta-D-glucopyranoside + H2O
quercetin + D-glucose
-
-
-
?
quercetin 4'-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
-
-
-
-
?
quercetin 4'-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
best substrate, homology modelling revealed that hydrophobic interactions dominate the binding of the aglycone moiety, Val168, Trp345, Phe225, Phe179, Phe334 and Phe433 are especially important in determining substrate specificity
-
-
?
quercetin 7-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
-
-
-
-
?
quercetin 7-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
high activity
-
-
?
rice bran hemicellulose + H2O
?
the enzyme is involved in degradation
-
-
?
rice bran hemicellulose + H2O
?
the enzyme is involved in degradation
-
-
?
salicin + H2O
beta-D-glucose + 2-(hydroxymethyl)phenol
-
-
-
-
?
salicin + H2O
beta-D-glucose + 2-(hydroxymethyl)phenol
-
-
-
?
salicin + H2O
beta-D-glucose + ?
-
390% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
salicin + H2O
beta-D-glucose + ?
-
118% activity compared to cellobiose
-
-
?
salicin + H2O
beta-D-glucose + ?
Jeotgalibacillus malaysiensis DSM 28777T
-
118% activity compared to cellobiose
-
-
?
salicin + H2O
beta-D-glucose + salicylic alcohol
-
4% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
salicin + H2O
D-glucose + salicyl alcohol
-
6% of the activity with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
salicin + H2O
salicyl alcohol + beta-D-glucose
-
36% of activity with gentiobiose
-
-
?
salicin + H2O
salicyl alcohol + beta-D-glucose
-
81% of activity with gentiobiose
-
-
?
salicin + H2O
saligenin + D-glucose
-
10.4% of the activity with 4-nitrophenyl beta-D-glucopyranoside
-
-
?
sophorose + H2O
2 beta-D-glucose
-
15-30% of activity with p-nitrophenyl-beta-d-glucopyranoside
-
-
?
sophorose + H2O
2 beta-D-glucose
-
430% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
sophorose + H2O
2 beta-D-glucose
-
144% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
sophorose + H2O
2 beta-D-glucose
Paecilomyces sp. (in: Eurotiomycetes) 220 Bainier
-
low activity
-
-
?
sophorose + H2O
2 beta-D-glucose
-
low activity
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?
additional information
?
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-
substrate specificity of wild-type and chimeric mutant enzymes, overview
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?
additional information
?
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substrate specificity of wild-type and chimeric mutant enzymes, overview
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?
additional information
?
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necessity of the nucleophilic glutamic acid residue, located in the motif YITENG, for the substrate hydrolysis. The mutated recombinant beta-glucosidase isoenzyme shows no activity with p-nitrophenyl 1-thio-beta-D-glucopyranoside, p-nitrophenyl beta-D-mannopyranoside, p-nitrophenyl beta-D-galactopyranoside and arbutin
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?
additional information
?
-
-
necessity of the nucleophilic glutamic acid residue, located in the motif YITENG, for the substrate hydrolysis. The mutated recombinant beta-glucosidase isoenzyme shows no activity with p-nitrophenyl 1-thio-beta-D-glucopyranoside, p-nitrophenyl beta-D-mannopyranoside, p-nitrophenyl beta-D-galactopyranoside and arbutin
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?
additional information
?
-
-
the enzyme does not hydrolyze 4-nitrophenyl-beta-D-galactoside, cellobiose, D-salicin, and galacturonic acid
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?
additional information
?
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no substrates: beta-glucans, laminarin, and 4-nitrophenyl-beta-D-xilopyranoside
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?
additional information
?
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no activity towards carboxymethylcellulose
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?
additional information
?
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the enzyme shows transglucosylation activity involving Trp49, overview
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?
additional information
?
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no marked activity with conjugates of lactose, mannose and xylose
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?
additional information
?
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no activity with 4-nitrophenyl-alpha-L-arabinoside and 4-nitrophenyl-alpha-L-rhamnoside
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?
additional information
?
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low substrate specificity for isoflavones
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?
additional information
?
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low substrate specificity for isoflavones
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?
additional information
?
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low substrate specificity for isoflavones
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?
additional information
?
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no activity with 4-nitrophenyl-alpha-L-arabinoside and 4-nitrophenyl-alpha-L-rhamnoside
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?
additional information
?
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the enzyme is active with a broad range of beta-linked glucosides, but not with alpha-linked saccharides, the enzyme hydrolyses some isoflavones to aglycone and beta-D-glucose, but shows no hydrolysis of isoflavones with 6''-O-acetyl and 6''-O-malonyl glucosides
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?
additional information
?
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the enzyme is active with a broad range of beta-linked glucosides, but not with alpha-linked saccharides, the enzyme hydrolyses some isoflavones to aglycone and beta-D-glucose, but shows no hydrolysis of isoflavones with 6''-O-acetyl and 6''-O-malonyl glucosides
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?
additional information
?
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an important enzyme of the cellulolytic complex necessary for the complete degrading of cellulose
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?
additional information
?
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an important enzyme of the cellulolytic complex necessary for the complete degrading of cellulose
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?
additional information
?
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no activity of the recombinant enzyme with salicin
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?
additional information
?
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no activity of the recombinant enzyme with salicin
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?
additional information
?
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cello-oligosaccharides from n equal 2 to 5 as substrates using 4 mM each sugar and 3 units/mg of enzyme are completely hydrolyzed to beta-D-glucose at 70°C within 16 h
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?
additional information
?
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cello-oligosaccharides from n equal 2 to 5 as substrates using 4 mM each sugar and 3 units/mg of enzyme are completely hydrolyzed to beta-D-glucose at 70°C within 16 h
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?
additional information
?
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the enzyme does not hydrolyze 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-beta-D-maltopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, and 4-nitrophenyl-beta-L-arabinopyranoside
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-
?
additional information
?
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the enzyme does not hydrolyze 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-beta-D-maltopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, and 4-nitrophenyl-beta-L-arabinopyranoside
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-
?
additional information
?
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the selectivity hexanol vs. water increases with increasing water activity in the reaction medium. It seems that the ideal condition for the transglycosylation reaction is a water activity close to 1.0
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?
additional information
?
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no activity with 4-nitrophenyl beta-D-xylopyranoside
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?
additional information
?
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isoform IpeGlu1 preferentially hydrolyzes glucosidic Ipecac alkaloids except for their lactams, but shows poor or no activity toward other substrates, including terpenoid-indole alkaloid glucosides. IpeGlu1 activity is extremely poor toward 7-O-methyl and 6,7-O,O-dimethyl derivatives. 6-O-methyl derivatives are hydrolyzed as efficiently as non-methylated substrates. IpeGlu1 lacks stereospecificity for its substrates. 1(R)-epimers are preferred to 1(S)-epimers
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?
additional information
?
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substrate binding of enzymes from wild-type strain and mutant strain 51 SMr
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?
additional information
?
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the enzyme does not degrade beta-glucans with modified ends, whereas it hydrolyzes various beta-glucans with free ends and related oligosaccharides with beta-1,3-, beta-1,4- or beta-1,6-linkages. It shows glycosyltransferase activity, preferably transfering 1 glucose residue from the donor oligosaccharides to the acceptor oligosaccharides, yielding laminario-(n1) oligosaccharides and laminario-(n+1) oligosaccharides
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?
additional information
?
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the enzyme does not degrade beta-glucans with modified ends, whereas it hydrolyzes various beta-glucans with free ends and related oligosaccharides with beta-1,3-, beta-1,4- or beta-1,6-linkages. It shows glycosyltransferase activity, preferably transfering 1 glucose residue from the donor oligosaccharides to the acceptor oligosaccharides, yielding laminario-(n1) oligosaccharides and laminario-(n+1) oligosaccharides
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?
additional information
?
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substrate specificity, overview, the enzyme catalyzes the hydrolysis of beta-glucosidic linkages, such as those in alkyl- or aryl-beta-glucosides as well as diglucosides and oligosaccharides, no activity with lactose, sucrose, Avicel, or 2-nitrophenyl-beta-D-galactopyranoside
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?
additional information
?
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the plant contains the oligofurostanoside-specific beta-glucosidase and an aryl beta-glucosidase
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?
additional information
?
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very little or no activity against 4-nitrophenyl-beta-lactoside, 4-nitrophenyl-beta-xyloside, 4-nitrophenyl-alpha-arabinofuranoside, xylan, and carboxymethyl cellulose
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?
additional information
?
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the purified enzyme exhibits almost no activity towards cellobiose and 4-nitrophenyl-beta-D-galactopyranoside, the enzyme does not hydrolyze 4-bromophenyl beta-D-glucopyranoside and ginsenoside Rh2 after incubation at 50°C for 24 h
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?
additional information
?
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the purified enzyme exhibits almost no activity towards cellobiose and 4-nitrophenyl-beta-D-galactopyranoside, the enzyme does not hydrolyze 4-bromophenyl beta-D-glucopyranoside and ginsenoside Rh2 after incubation at 50°C for 24 h
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?
additional information
?
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the enzyme is important in flavonoid-mediated interactions of legumes with microbes
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?
additional information
?
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the enzyme is important in flavonoid-mediated interactions of legumes with microbes
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?
additional information
?
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enzyme possesses strict specificity toward glucosyl isoflavones but not malonylglucosidic conjugates of isoflavones of soybean
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?
additional information
?
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enzyme deficiency causes the Gaucher's disease, the enzyme participates in degradation of glycosphingolipids
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?
additional information
?
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enzyme deficiency causes the Gaucher's disease, the enzyme participates in degradation of glycosphingolipids
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?
additional information
?
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the human cytosolic beta-glucosidase is a xenobiotic-metabolizing enzyme that hydrolyses certain flavonoid glucosides, with specificity depending on the aglycone moiety, the type of sugar and the linkage between them, substrate specificity, overview
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?
additional information
?
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the human cytosolic beta-glucosidase is a xenobiotic-metabolizing enzyme that hydrolyses certain flavonoid glucosides, with specificity depending on the aglycone moiety, the type of sugar and the linkage between them, substrate specificity, overview
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?
additional information
?
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no activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-beta-D-furanoside, lactose, maltose, trehalose, and sucrose, and poor activity with carboxymethyl cellulose, and Avicel, substrate specificity, overview
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?
additional information
?
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broad substrate specificity, specific for substrates having beta-glycosidic linkages, with strong preference for glucose, followed by galactose, at the non-reducing end. No activity with sucrose, maltose and trehalose, carboxymethyl cellulose and avicel
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?
additional information
?
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no activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-beta-D-furanoside, lactose, maltose, trehalose, and sucrose, and poor activity with carboxymethyl cellulose, and Avicel, substrate specificity, overview
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?
additional information
?
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broad substrate specificity, specific for substrates having beta-glycosidic linkages, with strong preference for glucose, followed by galactose, at the non-reducing end. No activity with sucrose, maltose and trehalose, carboxymethyl cellulose and avicel
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?
additional information
?
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not active towards sucrose and maltose as well as polysaccharides such as Avicel, carboxymethyl cellulose, Sigmacell cellulose 101, alpha-cellulose and xylan
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?
additional information
?
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Jeotgalibacillus malaysiensis DSM 28777T
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not active towards sucrose and maltose as well as polysaccharides such as Avicel, carboxymethyl cellulose, Sigmacell cellulose 101, alpha-cellulose and xylan
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?
additional information
?
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4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
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4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
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4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, geniposide, genistin, and trans-zeatin-O-glucoside are no substrates
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?
additional information
?
-
4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, geniposide, genistin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, geniposide, genistin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, geniposide, genistin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
-
4-nitrophenyl beta-D-mannopyranoside, harpagide, arbutin, geniposide, genistin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
4-nitrophenyl beta-D-mannopyranoside, harpagide, geniposide, arbutin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
4-nitrophenyl beta-D-mannopyranoside, harpagide, geniposide, arbutin, and trans-zeatin-O-glucoside are no substrates
-
-
?
additional information
?
-
4-nitrophenyl beta-D-mannopyranoside, harpagide, geniposide, arbutin, and trans-zeatin-O-glucoside are no substrates
-
-
?
additional information
?
-
4-nitrophenyl beta-D-mannopyranoside, harpagide, geniposide, arbutin, and trans-zeatin-O-glucoside are no substrates
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-
?
additional information
?
-
-
4-nitrophenyl beta-D-mannopyranoside, harpagide, geniposide, arbutin, and trans-zeatin-O-glucoside are no substrates
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?
additional information
?
-
-
the pure glucosidase from Lactobacillus brevis has also side activities of xylosidase, arabinosidase, and cellobiosidase
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?
additional information
?
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-
no hydrolysis of 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-rhamnopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-alpha-D-mannopyranoside, and 4-nitrophenyl-alpha-D-galactopyranoside
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-
?
additional information
?
-
-
substrate specificity with various 4-nitrophenol glycosides, overview, poor activity with lactose, sucrose, trehalose, and ginsenoside Rd, the enzyme can cleave both beta-1,2-glucosidic linkage at 3-C and beta-1,6-glucosidic linkage at 20-C of ginsenosides and can hydrolyze ginsenosides Rb1, Rb2, Rb3 and Rc into their active metabolites, compound K, compound Y, Mx, and Mc, respectively
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-
?
additional information
?
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no substrates: cellobiose, gentiobiose
-
-
-
additional information
?
-
Listeria innocua Clip11262 ATCC BAA-680
no substrates: cellobiose, gentiobiose
-
-
-
additional information
?
-
Littorina kurila
-
isoform G-II, exhibits exo-glucanase and beta-D-glucosidase activities as well as transglycosylation activity
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?
additional information
?
-
Melanocarpus sp.
-
the enzyme exhibits transglycosylation activity with methanol as acceptor
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?
additional information
?
-
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the enzyme exhibits transglycosylation activity with methanol as acceptor
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?
additional information
?
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enzyme is active against (1-4)beta and (1-2)beta glycosidic linkages
-
-
?
additional information
?
-
substrate specificity of the recombinant His-tagged enzyme, gentiobiose, lactose, and salicin are poor substrates, melibiose, palatinose, sophorose, and cellulose are no substrates, overview
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?
additional information
?
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enzyme is able to catalyze formation of lacto-N-neotetraose, i.e. Gal-beta-(1->4)-GlcNAc-beta-(1->3)-Gal-beta (1->4)-Glc, from lactose and N,N'-diacetylchitobiose and of N-acetyllactosamine, i.e Gal-beta-(1->4)-GlcNAc from N-acetylglucosamine and lactose. When compared with beta-glycosidase BglT from Thermus thermophilus, and beta-glycosidase CelB from Pyrococcus furiosus, BgaD is the most potent transgalactosidase, but both BglT and CelB can catalyze formation of LNnT and LacNAc, with BglT giving higher yields than CelB
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?
additional information
?
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-
demethyloleuropein derivatives, important in defense mechanisms, might be influenced by beta-glucosidase activity to improve the quality of the olive products with the best dialdehyde nutraceutical content
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?
additional information
?
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-
the beta-glucosidases involved in the enzymatic degradation of oleuropein, a bitter defence phenol glucoside in olive fruits, overview
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?
additional information
?
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-
does not hydrolyze the cell wall of Orobanche minor or cellohexaose
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?
additional information
?
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the enzyme is not able to hydrolyze n-octyl beta-D-thioglucopyranoside, amygdalin, dalcochinin glucoside, gossypin, linamarin, naringin, phlorizin, prunasin, pyridoxine-5-O-beta-D-glucoside, and quercitin 3-beta-D-glucoside. Negligible hydrolysis of 4-nitrophenyl-alpha-L-arabinoside, 4-nitrophenyl-beta-D-cellobioside, 4-nitrophenyl-beta-D-xyloside, 4-nitrophenyl-beta-D-mannoside, 4-nitrophenyl-beta-D-glucuronide, and 4-nitrophenyl-alpha-D-glucoside, cellotriose, cellotetraose, cellopentaose, cellohexaose, laminaritetraose, laminaripentaose, apigenin 7-glucoside, glycitin, diadzin, genistin, esculin, arbutin, coumaryl alcohol beta-D-glucoside, coniferin, and salicin
-
-
?
additional information
?
-
-
the enzyme is not able to hydrolyze n-octyl beta-D-thioglucopyranoside, amygdalin, dalcochinin glucoside, gossypin, linamarin, naringin, phlorizin, prunasin, pyridoxine-5-O-beta-D-glucoside, and quercitin 3-beta-D-glucoside. Negligible hydrolysis of 4-nitrophenyl-alpha-L-arabinoside, 4-nitrophenyl-beta-D-cellobioside, 4-nitrophenyl-beta-D-xyloside, 4-nitrophenyl-beta-D-mannoside, 4-nitrophenyl-beta-D-glucuronide, and 4-nitrophenyl-alpha-D-glucoside, cellotriose, cellotetraose, cellopentaose, cellohexaose, laminaritetraose, laminaripentaose, apigenin 7-glucoside, glycitin, diadzin, genistin, esculin, arbutin, coumaryl alcohol beta-D-glucoside, coniferin, and salicin
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?
additional information
?
-
-
jasmonic acid beta-D-glucosyl ester + H2O, product: jasmonic acid + beta-D-glucose, 51% relative activity compared to hydrolysis of tuberonic acid beta-D-glucoside
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-
?
additional information
?
-
-
no or negligible hydrolyzing activity with zeatin-O-glucoside, linamarin, or 4-nitrophenyl-beta-D-mannoside, 4-nitrophenyl-beta-D-galactoside, 4-nitrophenyl-beta-D-cellobioside, and 4-nitrophenyl-alpha-D-glucoside
-
-
?
additional information
?
-
-
the extracellular enzyme exhibits a broad substrate specificity, shows also exoglucanase and transglycosylation activities, overview
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-
?
additional information
?
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-
the extracellular enzyme exhibits a broad substrate specificity, shows also exoglucanase and transglycosylation activities, overview
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-
?
additional information
?
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-
maltose is a poor substrate, no activity with ginsenoside Rg3, Rb2, and Rb3, and with 4-nitrophenyl-alpha-D-glucopyranoside and 4-nitrophenyl-beta-D-xylopyranoside
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-
?
additional information
?
-
Paecilomyces sp. (in: Eurotiomycetes) 220 Bainier
-
maltose is a poor substrate, no activity with ginsenoside Rg3, Rb2, and Rb3, and with 4-nitrophenyl-alpha-D-glucopyranoside and 4-nitrophenyl-beta-D-xylopyranoside
-
-
?
additional information
?
-
-
maltose is a poor substrate, no activity with ginsenoside Rg3, Rb2, and Rb3, and with 4-nitrophenyl-alpha-D-glucopyranoside and 4-nitrophenyl-beta-D-xylopyranoside
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-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
in presence of high concentrations of glucose, both isoforms show trans-glycosidase activity
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-
?
additional information
?
-
enzyme is able to hydrolyze rice straw into simple sugars
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-
?
additional information
?
-
-
enzyme is able to hydrolyze rice straw into simple sugars
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-
?
additional information
?
-
exo-type glycoside hydrolase that cleaves beta-glucosidic bonds from the non-reducing ends of their substrates
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-
?
additional information
?
-
-
exo-type glycoside hydrolase that cleaves beta-glucosidic bonds from the non-reducing ends of their substrates
-
-
?
additional information
?
-
substrate specificity of isozyme BGL1A, overview
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-
?
additional information
?
-
substrate specificity of isozyme BGL1A, overview
-
-
?
additional information
?
-
-
substrate specificity of isozyme BGL1A, overview
-
-
?
additional information
?
-
substrate specificity of isozyme BGL1B, no activity with 4-nitrophenyl-beta-D-xylopyranoside, overview
-
-
?
additional information
?
-
substrate specificity of isozyme BGL1B, no activity with 4-nitrophenyl-beta-D-xylopyranoside, overview
-
-
?
additional information
?
-
-
substrate specificity of isozyme BGL1B, no activity with 4-nitrophenyl-beta-D-xylopyranoside, overview
-
-
?
additional information
?
-
substrate specificity of isozyme BGL1B, no activity with 4-nitrophenyl-beta-D-xylopyranoside, overview
-
-
?
additional information
?
-
substrate specificity of isozyme BGL1B, no activity with 4-nitrophenyl-beta-D-xylopyranoside, overview
-
-
?
additional information
?
-
substrate specificity of isozyme BGL1A, overview
-
-
?
additional information
?
-
substrate specificity of isozyme BGL1A, overview
-
-
?
additional information
?
-
-
no activity with caroxymethyl cellulose, xylan, Avicel, and laminarin, poor activity with 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
additional information
?
-
-
no activity with caroxymethyl cellulose, xylan, Avicel, and laminarin, poor activity with 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
additional information
?
-
-
substrate specificity, overview, poor hydrolysis of dalcochinin-8'-O-beta-glucoside, 4-methylumbelliferyl-beta-glucoside, and esculin, and no hydrolysis of alkyl-beta-glucosides, glucobioses, cyanogenic-beta-glucosides, steroid beta-glucosides, nor other iridoid beta-glucosides, including gonocaryoside A, or its derivative kingiside
-
-
?
additional information
?
-
-
the selectivity hexanol vs. water increases with increasing water activity in the reaction medium. It seems that the ideal condition for the transglycosylation reaction is a water activity close to 1.0
-
-
?
additional information
?
-
the gelatin-immobilized enzyme also catalyzes the transfer of beta-D-glucose from cellobiose to 5-phenylpentanol forming 5-phenylpentyl beta-D-glucopyranoside
-
-
?
additional information
?
-
-
the gelatin-immobilized enzyme also catalyzes the transfer of beta-D-glucose from cellobiose to 5-phenylpentanol forming 5-phenylpentyl beta-D-glucopyranoside
-
-
?
additional information
?
-
the enzyme hydrolyzes the outer glycoside at the C-6 position in protopanaxatriol-type ginsenosides whereas the enzyme does not hydrolyze the inner glucoside at the C-6 position and the glucoside at the C-20 position
-
-
?
additional information
?
-
-
the selectivity hexanol vs. water increases with increasing water activity in the reaction medium. It seems that the ideal condition for the transglycosylation reaction is a water activity close to 1.0
-
-
?
additional information
?
-
substrate specificity, barley glucan and 4-nitrophenyl beta-cellobioside are poor substrates, no activity with lactose, carboxy methyl cellulose, xyloglucan, and lichenan, the enzyme is a specific beta-glucosidase and does not show beta-galactosidase activity, but it shows additional glucosyl transferase activity producing cellobiose from D-glucose and cellotetrose from cellobiose
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-
?
additional information
?
-
-
substrate specificity, barley glucan and 4-nitrophenyl beta-cellobioside are poor substrates, no activity with lactose, carboxy methyl cellulose, xyloglucan, and lichenan, the enzyme is a specific beta-glucosidase and does not show beta-galactosidase activity, but it shows additional glucosyl transferase activity producing cellobiose from D-glucose and cellotetrose from cellobiose
-
-
?
additional information
?
-
enzyme shows a preference for disaccharide substrates over longer glucooligosaccharides
-
-
?
additional information
?
-
-
enzyme shows a preference for disaccharide substrates over longer glucooligosaccharides
-
-
?
additional information
?
-
substrate specificity, barley glucan and 4-nitrophenyl beta-cellobioside are poor substrates, no activity with lactose, carboxy methyl cellulose, xyloglucan, and lichenan, the enzyme is a specific beta-glucosidase and does not show beta-galactosidase activity, but it shows additional glucosyl transferase activity producing cellobiose from D-glucose and cellotetrose from cellobiose
-
-
?
additional information
?
-
-
the termite egg-recognition pheromone consists of beta-glucosidase and lysozyme. Both enzymes are major salivary compounds and also produced in eggs
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-
?
additional information
?
-
-
the termite egg-recognition pheromone consists of beta-glucosidase and lysozyme. Both enzymes are major salivary compounds and also produced in eggs
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-
?
additional information
?
-
isoform Bglu3B exhibits a broad range of substrate specificity, catalyzing the cleavage of beta-1,2, beta-1,3, beta-1,4 and beta-1,6 linkages, in various oligosaccharides, to liberate glucose, e.g. reaction of EC 3.2.1.58. Bglu3B shows relatively high activity toward laminaran and transglycosylation activity, enabling gentiobiose production. No substrates: 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, lactose, barley beta-glucan, Avicel, carboxymethyl cellulose, lichenan, birchwood xylan and chitin
-
-
?
additional information
?
-
-
beta-glucosidase requires strictly beta-gluco configuration for activity, it cleaves glucose-glucose beta-(1-4) linkages better than beta-(1-2), and beta-(1-6) linkages
-
-
?
additional information
?
-
-
the enzyme is highly specificic for beta-D-glucopyranosides, no activity with alpha-D-glucopyranosides
-
-
?
additional information
?
-
-
the enzyme shows highest activity with mono-beta-D-glycosides
-
-
?
additional information
?
-
-
the enzyme shows highest activity with mono-beta-D-glycosides
-
-
?
additional information
?
-
-
BGL1 is a non-cellulolytic yeast enzyme, substrate specifiicty with beta-1,4 linkage-specific cellulosic substrates, overview
-
-
?
additional information
?
-
-
the enzyme shows broad substrate specificity hydrolyzing beta-linked gluco-disaccharides and oligosaccharides, and transglycosylation activity forming beta-linked di- and oligosaccharides
-
-
?
additional information
?
-
-
the enzyme has the capacity to synthesize short oligosaccharides from cellobiose as the substrate concentration reaches 30% with a recovery of 40%, involvement of a transglucosylation to synthesize cellotetraose by a sequential addition of glucose to cellotriose, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with 4-methylumbelliferyl-beta-D-cellobioside, the enzyme has the capacity to synthesize short oligosaccharides from cellobiose as the substrate concentration reaches 30% with a recovery of 40%, overview
-
-
?
additional information
?
-
no activity towards 4-nitrophenyl-alpha-D-galactopyranoside, carboxymethylcellulose, and xylan (2% w/v)
-
-
?
additional information
?
-
-
no activity towards 4-nitrophenyl-alpha-D-galactopyranoside, carboxymethylcellulose, and xylan (2% w/v)
-
-
?
additional information
?
-
no activity towards 4-nitrophenyl-alpha-D-galactopyranoside, carboxymethylcellulose, and xylan (2% w/v)
-
-
?
additional information
?
-
-
no activity towards carboxymethylcellulose
-
-
?
additional information
?
-
-
does not hydrolyze 2-nitrophenyl alpha-D-galactopyranoside, methyl beta-D-glucopyranoside, carboxymethylcellulose, methyl alpha-D-galactopyranoside, maltose, and trehalose
-
-
?
additional information
?
-
-
the purified enzyme shows substrate specificity only towards substrates with beta-1,4 linkages and displays no hydrolytic activity towards 2-nitrophenyl apha-D-galactopyranoside, methyl alpha-D-galactopyranoside, melibiose, carboxymethyl cellulose, and starch
-
-
?
additional information
?
-
-
the purified enzyme shows substrate specificity only towards substrates with beta-1,4 linkages and displays no hydrolytic activity towards 2-nitrophenyl apha-D-galactopyranoside, methyl alpha-D-galactopyranoside, melibiose, carboxymethyl cellulose, and starch
-
-
?
additional information
?
-
-
an important enzyme of the cellulolytic complex necessary for the complete degrading of cellulose
-
-
?
additional information
?
-
the recombinant enzyme BGLII has both beta-glucosidase and beta-xylosidase activity and shows transglycosylation activity with 4-nitrophenyl-beta-D-glucopyranoside as a donor and with various alcohols as acceptors, overview, no activity with carboxymethylcellulose
-
-
?
additional information
?
-
-
the recombinant enzyme BGLII has both beta-glucosidase and beta-xylosidase activity and shows transglycosylation activity with 4-nitrophenyl-beta-D-glucopyranoside as a donor and with various alcohols as acceptors, overview, no activity with carboxymethylcellulose
-
-
?
additional information
?
-
-
enzyme hydrolyses aryl and alkyl beta-D-glucosides and cello-oligosaccharides, and is specific for substrates with a beta-glycosidic linkage. The hydroxy groups at positions 2, 4 and 6 of a glucose residue at the non-reducing end of a disaccharide are essential for catalysis. Enzyme releases one glucose unit at a time from the non-reducing end of cello-oligosaccharides, and the rate of hydrolysis decreases with an increase in chain length. The enzyme catalyses the synthesis of methyl, ethyl and propyl beta-D-glucosides in the presence of methanol, ethanol and propan-2-ol respectively with either glucose or cellobiose, cellobiose is preferred
-
-
?
additional information
?
-
-
an important enzyme of the cellulolytic complex necessary for the complete degrading of cellulose
-
-
?
additional information
?
-
the recombinant enzyme BGLII has both beta-glucosidase and beta-xylosidase activity and shows transglycosylation activity with 4-nitrophenyl-beta-D-glucopyranoside as a donor and with various alcohols as acceptors, overview, no activity with carboxymethylcellulose
-
-
?
additional information
?
-
-
the recombinant enzyme BGLII has both beta-glucosidase and beta-xylosidase activity and shows transglycosylation activity with 4-nitrophenyl-beta-D-glucopyranoside as a donor and with various alcohols as acceptors, overview, no activity with carboxymethylcellulose
-
-
?
additional information
?
-
-
enzyme hydrolyses aryl and alkyl beta-D-glucosides and cello-oligosaccharides, and is specific for substrates with a beta-glycosidic linkage. The hydroxy groups at positions 2, 4 and 6 of a glucose residue at the non-reducing end of a disaccharide are essential for catalysis. Enzyme releases one glucose unit at a time from the non-reducing end of cello-oligosaccharides, and the rate of hydrolysis decreases with an increase in chain length. The enzyme catalyses the synthesis of methyl, ethyl and propyl beta-D-glucosides in the presence of methanol, ethanol and propan-2-ol respectively with either glucose or cellobiose, cellobiose is preferred
-
-
?
additional information
?
-
-
the enzyme shows significant transglucosylation activity, resulting in formation of e.g. galactooligosaccharides with lactose as acceptor, and is active with galactosides, overview
-
-
?
additional information
?
-
-
enzyme hydrolyzes a variety of aryl/alkyl-beta-glucosides and disaccharides as well as (1->6) and (1->4)-beta-glucosidic linkages and alpha-glycosidic substrates
-
-
?
additional information
?
-
-
the enzyme shows significant transglucosylation activity, resulting in formation of e.g. galactooligosaccharides with lactose as acceptor, and is active with galactosides, overview
-
-
?
additional information
?
-
-
the enzyme is capable of hydrolysing larchwood xylan, xylobiose and 4-nitrophenyl-beta-D-xyloside, though to a lesser extent. The enzyme was specific for the beta-configuration and glucose moiety in the substrate
-
-
?
additional information
?
-
-
enzyme requires glucoside substrates containing a terminal, non-reducing beta-D-glucose residue. Enzyme exhibited little, but significant alpha-D-glucosidase activity and is capable of hydrolysing beta-1,6-linked diglucosides and gentiobiose
-
-
?
additional information
?
-
-
enzyme requires glucoside substrates containing a terminal, non-reducing beta-D-glucose residue. Enzyme exhibited little, but significant alpha-D-glucosidase activity and is capable of hydrolysing beta-1,6-linked diglucosides and gentiobiose
-
-
?
additional information
?
-
no activity is detected for 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-beta-L-arabinopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, and 4-nitrophenyl-alpha-L-arabinopyranoside
-
-
?
additional information
?
-
-
above 1 mM substrate concentration, enzyme catalyses a parallel transglycosylation reaction. No substrate: beta-1,4-glucan
-
-
?
additional information
?
-
enzyme hydrolyzes low molecular weight substrates and polysaccharides containing beta-glucosidic residues, and efficiently synthesizes methyl-D-glucoside in the presence of methanol due to its transglycosylation activity. It shows no detectable activity towards 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, carboxymethyl cellulose, wheat and birchwood xylans and avicel
-
-
?
additional information
?
-
-
enzyme hydrolyzes low molecular weight substrates and polysaccharides containing beta-glucosidic residues, and efficiently synthesizes methyl-D-glucoside in the presence of methanol due to its transglycosylation activity. It shows no detectable activity towards 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, carboxymethyl cellulose, wheat and birchwood xylans and avicel
-
-
?
additional information
?
-
enzyme hydrolyzes low molecular weight substrates and polysaccharides containing beta-glucosidic residues, and efficiently synthesizes methyl-D-glucoside in the presence of methanol due to its transglycosylation activity. It shows no detectable activity towards 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, carboxymethyl cellulose, wheat and birchwood xylans and avicel
-
-
?
additional information
?
-
-
substrate specificity of wild-type and chimeric mutant enzymes, overview
-
-
?
additional information
?
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
substrate specificity of wild-type and chimeric mutant enzymes, overview
-
-
?
additional information
?
-
-
the enzyme also shows glycosyl tranferase activity with arbutin and cellobiose as acceptor and donor, respectively, resulting in three distinct transfer products, where glucose is transferred from cellobiose to C3, C4, and C5 of arbutin, product analysis by mass spectrometry
-
-
?
additional information
?
-
-
the enzyme plays a role in the carbohydrate metabolism of many organisms by acting on the beta-glycosidic linkages of cellooligosaccharides containing beta-D-1,4-glycosidic bonds, glycosyl hydrolase family 3 enzymes are retaining enzymes that utilize a double-displacement mechanism with retention of configuration at the anomeric carbon of the sugar ring and often display transglycosylation abilities
-
-
?
additional information
?
-
enzyme is able to catalyze formation of lacto-N-neotetraose, i.e. Gal-beta(1,4)-GlcNAc-beta(1,3)-Gal-beta(1,4)-Glc, from lactose and N,N'-diacetylchitobiose and of N-acetyllactosamine, i.e Gal-beta(1,4)-GlcNAc from N-acetylglucosamine and lactose. When compared with truncated beta-galactosidase BgaD-D from Bacillus circulans, and beta-glycosidase CelB from Pyrococcus furiosus, BgaD is the most potent transgalactosidase, but both BglT and CelB can catalyze formation of LNnT and LacNAc, with BglT giving higher yields than CelB
-
-
?
additional information
?
-
-
the enzyme shows transglycosylase activities, the enzyme catalyze the transfer of beta-D-glucosyl and beta-D-fucosyl from the corresponding 4-nitrophenyl-beta-D-glycopyranosides to a hydroxyl group of glucose in the synthesis of beta-D-glucosyl-D-glucopyranoses and beta-Dfucosyl-D-glucopyranoses. The yields in disaccharides produced under conditions of non-initial velocity are very attractive and the formation of the beta(1-3) linked disaccharides is largely favored
-
-
?
additional information
?
-
-
no activity towards carboxymethylcellulose
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, the aromatic side chain at position 378 of isozyme TaGlu1a, which is located at the entrance to the catalytic center, plays an important role in substrate binding, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, the aromatic side chain at position 378 of isozyme TaGlu1a, which is located at the entrance to the catalytic center, plays an important role in substrate binding, overview
-
-
?
additional information
?
-
the wheat beta-D-glucosidases hydrolyze hydroxamic acid-glucose conjugates, the aromatic side chain at position 378 of isozyme TaGlu1a, which is located at the entrance to the catalytic center, plays an important role in substrate binding, overview
-
-
?
additional information
?
-
no hydrolysis of xylan, cellopentaose, cellohexaose, and carboxymethylcellulose
-
-
?
additional information
?
-
no activity using 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, or sucrose as substrates
-
-
?
additional information
?
-
-
enzyme exhibits weak activities toward 4-nitrophenyl beta-D-galactopyranoside and 4-nitrophenyl beta-D-xylopyranoside, but no detectable activity toward 4-nitrophenyl beta-D-cellobioside
-
-
?
additional information
?
-
no activity with oat spelt xylan, 4-nitrophenyl-alpha-D-arabinofuranoside, and 4-nitrophenyl-beta-D-xylanopyranoside
-
-
?
additional information
?
-
-
no activity with oat spelt xylan, 4-nitrophenyl-alpha-D-arabinofuranoside, and 4-nitrophenyl-beta-D-xylanopyranoside
-
-
?
additional information
?
-
no activity with oat spelt xylan, 4-nitrophenyl-alpha-D-arabinofuranoside, and 4-nitrophenyl-beta-D-xylanopyranoside
-
-
?
additional information
?
-
-
no activity with oat spelt xylan, 4-nitrophenyl-alpha-D-arabinofuranoside, and 4-nitrophenyl-beta-D-xylanopyranoside
-
-
?
additional information
?
-
Glu1 shows broad substrate specificity in vitro
-
-
?
additional information
?
-
-
does not hydrolyze 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, avicel carboxymethyl cellulose , xylan, starch, and pectin
-
-
?
additional information
?
-
-
beta-glucosidases show poor activity on 4-nitrophenyl beta-D-cellobioside or cellooligosaccharides
-
-
?
additional information
?
-
[Humicola] grisea var. thermoidea IFO 9854
-
beta-glucosidases show poor activity on 4-nitrophenyl beta-D-cellobioside or cellooligosaccharides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1-4)-beta-D-glucosyl-D-mannobiose + H2O
beta-D-glucose + D-mannobiose
-
-
-
?
(1-4)-beta-D-glucosyl-D-mannose + H2O
beta-D-glucose + D-mannose
-
-
-
?
2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one + H2O
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
-
-
-
?
2-phenylethyl beta-D-glucopyranoside + H2O
2-phenylethanol + beta-D-glucose
-
-
2-phenylethanol is a flower sent compound
-
?
3(2)-beta-D-glucosyl-D-cellobiose + H2O
beta-D-glucose + D-cellobiose
-
-
-
?
3-O-alpha-D-glucopyranosyl-D-glucose + H2O
alpha-D-glucose + D-glucose
-
nigerose
-
?
3-O-beta-cellobiosyl-D-glucose + H2O
beta-D-glucose + D-cellobiose
-
-
-
?
3-O-beta-cellotriosyl-D-glucose + H2O
beta-D-glucose + D-cellotriose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + 2 H2O
4-methylumbelliferol + 2 D-glucose
native beta-glucosidase substrate, 14.9% relative activity compared to 4-nitrophenyl-beta-D-glucopyranoside as substrate
-
-
?
4-O-beta-D-xylopyranosyl-D-xylose + H2O
beta-D-xylose + D-xylose
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucose + H2O
alpha-D-glucose + D-glucose
-
isomaltose
-
?
alpha-L-arabinofuranose + H2O
alpha-L-arabinofuranose + ?
-
low activity
-
?
alpha-L-rhamnopyranoside + H2O
alpha-L-rhamnopyranose + ?
-
-
-
?
arbutin + H2O
4-hydroxyphenol + beta-D-glucose
-
104% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
avenacoside + H2O
C26-desgluco-avenacosides + beta-D-glucose
-
the enzyme hydrolyzes the avenacosides to combat fungal attack
-
-
?
beta-D-fructofuranosyl-alpha-D-glucopyranoside + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
cyanidin-3-O-beta-D-glucoside + H2O
cyanidin + beta-D-glucose
-
the enzyme is involved in anthocyanin metabolism, overview
-
-
?
cyanoglucosides + H2O
HCN + beta-D-glucose
-
-
HCN acts as a deterrent to grazing animals
?
D-cellobiono-1,5-lactone + H2O
D-glucose + D-glucono-1,5-lactone
-
-
-
?
dhurrin + H2O
4-hydroxy-(S)-mandelonitrile + beta-D-glucose
-
i.e. 4-hydroxy-(S)-mandelonitrile-beta-D-glucoside, Dhr1 is strictly specific for this substrate
-
-
?
digitoxigenin cellobioside + 2 H2O
digitoxigenin + 2 beta-D-glucose
-
38% of activity with glucoevatromonoside
-
-
?
eriodicytol-7-beta-D-glucopyranoside + H2O
eriodicytol + beta-D-glucose
-
-
-
-
?
gentiobiose + H2O
2 beta-D-glucose
-
483% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
gentiopentaose + 4 H2O
5 D-glucose
-
specific for beta-1,6-linkages, activity decreases with number of glucose residues
-
?
ginsenoside Rb1 + 3 H2O
(3beta,5xi,6alpha,12beta,13xi)-3,6,12-trihydroxydammar-24-en-20-yl beta-D-glucopyranoside + 3 beta-D-glucose
-
-
-
-
?
ginsenoside Rb2 + 2 H2O
(3beta,5xi,6alpha,12beta,13xi)-3,6,12-trihydroxydammar-24-en-20-yl 6-O-alpha-L-arabinopyranosyl-beta-D-glucopyranoside + 2 beta-D-glucose
-
-
-
-
?
ginsenoside Rb3 + H2O
20-O-beta -D-xylopyranosyl-1,6-beta-D-glucopyranosyl-20(S)-protopanaxadiol + beta-D-glucose
-
-
-
-
?
ginsenoside Rc + H2O
(3beta,5xi,6alpha,12beta,13xi)-3,6,12-trihydroxydammar-24-en-20-yl 6-O-beta-D-xylopyranosyl-beta-D-glucopyranoside + beta-D-glucose
-
-
-
-
?
Glc3Man9GlcNAc2 + H2O
Glc2Man9GlcNAc2 + beta-D-glucose
-
important in processing of oligosaccharides after their transfer from dolichyl diphosphate to proteins during glycoprotein synthesis
-
?
glucogitoroside + H2O
gitoroside + beta-D-glucose
-
38% of activity with glucoevatromonoside
-
-
?
glucoquinovosidodigitoxigenin + H2O
quinovosidodigitoxigenin + beta-D-glucose
-
38% of activity with glucoevatromonoside
-
-
?
glucosyl ceramide + H2O
sphingosine + fatty acid + beta-D-glucose
-
involved in normal catabolism of glucosyl ceramides
-
?
hesperetin 7-O-beta-glucopyranoside + H2O
hesperetin + beta-D-glucose
-
199% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
hesperitin-dihydrochalcon 7-O-beta-D-glucopyranoside + H2O
hesperitin-dihydrochalcon + beta-D-glucose
-
91% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
insoluble cellooligosaccharaide + H2O
beta-D-glucose + ?
-
beta-glucosidase 3 less active
-
?
laminaribiose + H2O
2 beta-D-glucose
-
519% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
mandelonitrile-beta-D-glucopyranoside + H2O
mandelonitrile + beta-D-glucose
-
trivial name prunasin, 309% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
n-decyl beta-D-glucoside + H2O
beta-D-glucose + n-decanol
-
6fold higher activity than with methyl-beta-D-glucoside
-
?
oligofurostanosides + H2O
?
-
the specific degradation of the oligofurostanosides helps to maintain their furostanol structure of steroid glycosides is necessary for their transport within the leaf and from the leaf to the rhizome
-
-
?
plumieride coumarate beta-D-glucoside + H2O
13-O-coumarylplumieride + beta-D-glucose
-
an iridoid beta-glucoside from Plumeria obtusa, i.e. white frangipani, flower, the Plumeria obtusa beta-glucosidase shows high specificity for its natural substrate, plumieride coumarate glucoside
-
-
?
podophyllotoxin-4-O-beta-D-glucopyranoside + H2O
podophyllotoxin + beta-D-glucose
-
-
-
-
?
quercetin 4'-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
-
-
-
-
?
salicin + H2O
beta-D-glucose + ?
-
390% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
scopolin + H2O
scopoletin + beta-D-glucose
-
-
-
?
sinigrin + H2O
beta-D-glucose + ?
-
325% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
sophorose + H2O
2 beta-D-glucose
-
430% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
specific for beta-1,2-, -1,3- or -1,4-hydrolysis
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
lower activity for beta-glucosidase II
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
r
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
high activity on short oligosaccharides, decreasing activity for higher oligosaccharides, transglycosylation reaction
-
r
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
not restricted to the beta-D-1,4-linkage
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
very low activity
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
very low activity
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
r
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
transglycoslation activity
-
r
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
preference for beta-1,3-bonds
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
lower activity for beta-glucosidase II
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
maltose
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
maltose
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
maltose
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
only beta-glucosidase II
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
low activity
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
low activity
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
thermophilic anaerobic bacterium
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
low activity
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
high activity on short oligosaccharides, decreasing activity for higher oligosaccharides
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity for beta-glucosidase 3
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity for beta-glucosidase 3
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
additional product: cellotetraose as the product of transglycosylation
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
hydrophobic-driven binding of the glucose residue at subsite 2 of 2 main binding-modes of beta-glucosidase
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
synergistic action of Trichoderma reesei and Aspergillus wentii cellulases for cellulose hydrolysis
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
only one of two cloned genes is active on cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycolsylation reaction, yielding alcohol-beta-glucosides in the presence of alcohols
-
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
complete hydrolsis of barley endosperm cell wall through synergistic action of endo(1-3,1-4)-beta-glucanase and beta-glucosidase
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
Lenzites trabea
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
cellobiose
-
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
additional product: cellotriose by transglycosylation activity
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
transglycosylation activity through a third sub-site, ability to accommodate substrates longer than cellobiose
-
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
less active
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
additional product: cellotriose by transglycosylation activity
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
activity 60fold less than for 4-nitrophenyl-beta-D-glucopyranoside
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
additional product: cellotetraose as the product of transglycosylation
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
promoting action of 1,4-beta-cellobiohydrolase
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
Sporotrichum pulverulentum
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
one of the two best substrates
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cloned enzyme show greater activity against cellobiose than against aryl-beta-D-glucosides
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
Thermochaetoides thermophila
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
Thermochaetoides thermophila
-
no activity for aryl-beta-D-glucosidases
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
cellobiose
additional product: cellotriose by transglycosylation activity
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
transglycolsylation reaction, yielding alcohol-beta-glucosides in the presence of alcohols
additional product: cellotriose by transglycosylation activity
r
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycosylation reaction
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycosylation reaction
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycosylation reaction
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
transglycosylation reaction
-
r
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
thermophilic anaerobic bacterium
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
beta-D-fructofuranosyl-alpha-D-glucopyranoside + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
-
low activity
-
?
beta-D-fructofuranosyl-alpha-D-glucopyranoside + H2O
beta-D-fructofuranose + alpha-D-glucopyranose
-
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
609% of activity with p-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
2 beta-D-glucose
-
best natural substrate
-
-
?
cellobiose + H2O
2 D-glucose
native beta-glucosidase substrate, 26.4% relative activity compared to 4-nitrophenyl-beta-D-glucopyranoside as substrate
-
-
?
cellohexaose + 5 H2O
6 D-glucose
-
marked increase of relative activity for chimeric enzymes
-
?
cellohexaose + 5 H2O
6 D-glucose
-
low activity for beta-glucosidase 3
-
?
cellohexaose + 5 H2O
6 D-glucose
-
marked increase of relative activity for chimeric enzymes
-
?
cellopentaose + 4 H2O
5 D-glucose
-
marked increase of relative activity for chimeric enzyme
-
?
cellopentaose + 4 H2O
5 D-glucose
-
low activity for beta-glucosidase 3
-
?
cellopentaose + 4 H2O
5 D-glucose
-
marked increase of relative activity for chimeric enzyme
-
?
cellotetraose + 3 H2O
4 D-glucose
-
marked increase of relative activity for chimeric activity
-
?
cellotetraose + 3 H2O
4 D-glucose
-
low activity for beta-glucosidase 3
-
?
cellotetraose + 3 H2O
4 D-glucose
-
marked increase of relative activity for chimeric activity
-
?
cellotriose + 2 H2O
3 D-glucose
-
low activity for beta-glucosidase 3
-
?
cellulose + H2O
beta-D-glucose + ?
-
cellulose MN 300
-
?
laminarin + H2O
beta-D-glucose + ?
-
involvement in autolysis
-
?
laminarin + H2O
beta-D-glucose + ?
thermophilic anaerobic bacterium
-
low activity
-
?
rice bran hemicellulose + H2O
?
the enzyme is involved in degradation
-
-
?
rice bran hemicellulose + H2O
?
the enzyme is involved in degradation
-
-
?
additional information
?
-
-
an important enzyme of the cellulolytic complex necessary for the complete degrading of cellulose
-
-
?
additional information
?
-
-
an important enzyme of the cellulolytic complex necessary for the complete degrading of cellulose
-
-
?
additional information
?
-
the enzyme is important in flavonoid-mediated interactions of legumes with microbes
-
-
?
additional information
?
-
-
the enzyme is important in flavonoid-mediated interactions of legumes with microbes
-
-
?
additional information
?
-
-
enzyme deficiency causes the Gaucher's disease, the enzyme participates in degradation of glycosphingolipids
-
-
?
additional information
?
-
-
enzyme deficiency causes the Gaucher's disease, the enzyme participates in degradation of glycosphingolipids
-
-
?
additional information
?
-
-
the pure glucosidase from Lactobacillus brevis has also side activities of xylosidase, arabinosidase, and cellobiosidase
-
-
?
additional information
?
-
-
demethyloleuropein derivatives, important in defense mechanisms, might be influenced by beta-glucosidase activity to improve the quality of the olive products with the best dialdehyde nutraceutical content
-
-
?
additional information
?
-
-
the beta-glucosidases involved in the enzymatic degradation of oleuropein, a bitter defence phenol glucoside in olive fruits, overview
-
-
?
additional information
?
-
-
the termite egg-recognition pheromone consists of beta-glucosidase and lysozyme. Both enzymes are major salivary compounds and also produced in eggs
-
-
?
additional information
?
-
-
the termite egg-recognition pheromone consists of beta-glucosidase and lysozyme. Both enzymes are major salivary compounds and also produced in eggs
-
-
?
additional information
?
-
-
the enzyme has the capacity to synthesize short oligosaccharides from cellobiose as the substrate concentration reaches 30% with a recovery of 40%, involvement of a transglucosylation to synthesize cellotetraose by a sequential addition of glucose to cellotriose, overview
-
-
?
additional information
?
-
-
an important enzyme of the cellulolytic complex necessary for the complete degrading of cellulose
-
-
?
additional information
?
-
-
an important enzyme of the cellulolytic complex necessary for the complete degrading of cellulose
-
-
?
additional information
?
-
-
the enzyme plays a role in the carbohydrate metabolism of many organisms by acting on the beta-glycosidic linkages of cellooligosaccharides containing beta-D-1,4-glycosidic bonds, glycosyl hydrolase family 3 enzymes are retaining enzymes that utilize a double-displacement mechanism with retention of configuration at the anomeric carbon of the sugar ring and often display transglycosylation abilities
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Cu2+
EDTA
Fe2+
Fe3+
Hg2+
K+
Mg2+
Mn2+
Na+
NaCl
Ni2+
Pb2+
1 mM, native enzyme is activated to 109.3% of control, recombinant enzyme is activated to 110.6% of control, beta-glucosidase activity
Zn2+
additional information
Ba2+
1 mM, native enzyme is activated to 111.6% of control, recombinant enzyme is activated to 109.1% of control, beta-glucosidase activity
Ca2+
-
233.33% relative activity of the enzyme from midgut at 40 mM Ca2+, 193.31% relative activity of the enzyme from salivary gland at 40 mM Ca2+
Ca2+
-
121% activity at 5 mM. The activity and stability are increased when CaCl2 is supplemented to the enzyme
Fe2+
1 mM, native enzyme is activated to 130.0% of control, recombinant enzyme is activated to 127.3% of control, beta-glucosidase activity
Mg2+
-
200% relative activity of the enzyme from midgut at 40 mM Mg2+, 169.49% relative activity of the enzyme from salivary gland at 40 mM Mg2+
Mn2+
1 mM, native enzyme is activated to 102.3% of control, recombinant enzyme is activated to 106.4% of control, beta-glucosidase activity
Na+
-
198.57% relative activity of the enzyme from midgut at 40 mM Na+, 163.63% relative activity of the enzyme from salivary gland at 40 mM Na+
Zn2+
2 mM Zn2+ increases the relative activity of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde to 192% and 199% with cellobiose and 4-nitrophenyl beta-D-glucopyranoside as substrates, respectively
additional information
-
no effect on piceid-beta-D-glucosidase by Ca2+, Mg2+, and Zn2+ ions
additional information
-
the enzyme is not apparently affected by heavy metal salts, such as Cu2+ and Fe3+
additional information
-
no effect on enzyme activity by Ca2+, Sr2+, Co2+, Zn2+, Ni2+, Mg2+, and Mn2+ at up to 5 mM and by Fe2+ and Cr3+ at 1 mM, no metalloenzyme
additional information
no remarkable activation or inhibition by 5 mM Mg2+, 5 mM Zn2+, 5 mM Ca2+, 5 mM Cu2+, 5 mM Co2+, 5 mM Cr2+, 5 mM Ni2+, 5 mM Pb2+, 5 mM EDTA, 5 mM 2-mercaptoethanol
additional information
no remarkable activation or inhibition by 5 mM Mg2+, 5 mM Zn2+, 5 mM Ca2+, 5 mM Cu2+, 5 mM Co2+, 5 mM Cr2+, 5 mM Ni2+, 5 mM Pb2+, 5 mM EDTA, 5 mM 2-mercaptoethanol
additional information
no remarkable activation or inhibition by 5 mM Mg2+, 5 mM Zn2+, 5 mM Ca2+, 5 mM Cu2+, 5 mM Co2+, 5 mM Cr2+, 5 mM Ni2+, 5 mM Pb2+, 5 mM EDTA, 5 mM 2-mercaptoethanol
additional information
-
no remarkable activation or inhibition by 5 mM Mg2+, 5 mM Zn2+, 5 mM Ca2+, 5 mM Cu2+, 5 mM Co2+, 5 mM Cr2+, 5 mM Ni2+, 5 mM Pb2+, 5 mM EDTA, 5 mM 2-mercaptoethanol
additional information
-
no metalloprotein, not affected by Al3+ at 1.0 mM
additional information
-
Ca2+, Co2+, Mg2+, Mn2+, and Zn2+ have no inhibitory effects at 5 mM. Addition of beta-mercaptoethanol or cysteine does not significantly alter activity
additional information
-
the enzyme is not affected by Ca2+, Co2+, Mg2+, K+, Na+, and Zn2+
additional information
-
no effect by Co2+, optimal activity is obtained with 100 mM phosphate buffer and, the activity decreased at 150 and 200 mM but not dramatically
additional information
the enzyme is not activated by the presence of monovalent or divalent cations
additional information
the enzyme is unaffected by Mn2+, Mg2+, and Co2+
additional information
-
the enzyme is unaffected by Mn2+, Mg2+, and Co2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S,5S)-3-methylidene-6,8-bis[(1S)-1-phenylethyl]-6,8-diazabicyclo[3.2.2]nonane-7,9-dione
-
-
(2R,3R,4R,5S)-1-butyl-2-(hydroxymethyl)piperidine-3,4,5-triol
-
(2S,5S)-2-benzyl-3,11-bis[(1S)-1-phenylethyl]-2,3,5,6-tetrahydro-5,2-(epiminomethano)-3-benzazocine-4,12(1H)-dione
-
-
(2S,5S)-2-methyl-3,11-bis[(1S)-1-phenylethyl]-2,3,5,6-tetrahydro-5,2-(epiminomethano)-3-benzazocine-4,12(1H)-dione
-
-
(2S,5S)-3,11-bis[(1S)-1-phenylethyl]-2,3,5,6-tetrahydro-5,2-(epiminomethano)-3-benzazocine-4,12(1H)-dione
-
-
1-O-methyl-beta-D-glucose
-
competitive inhibition, Ki: 17.5 mM
2,4-dinitrophenyl-2-fluoro-2-deoxy-beta-D-glucopyranoside
-
0.001 mM, 64% inhibition after 30 min incubation
2-butanol
-
highest decrease of activity in comparison to ethanol and 2-propanol
2-nitrophenyl-beta-D-fucopyranoside
-
competitively versus substrate 4-nitrophenyl beta-D-glucopyranoside
4-chloromercuribenzoate
-
63.1% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 0.5 mM
4-hydroxybenzoic acid
-
97.5% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside as substrate
4-nitrophenol
the gelatin-immobilized enzyme is less sensitive than the native enzyme
4-nitrophenyl-beta-D-fucopyranoside
-
competitively versus substrate 4-nitrophenyl beta-D-glucopyranoside
4-[4-(cyanomethoxy)phenyl]-4-oxo-N-{3-[(2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl]propyl}butanamide
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
8.67% inhibitory effect at 1 mM
acetone
-
68.3% and 62% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
dimethyl sulfoxide
30% 25% inhibition. 40% 47% inhibition. 50% 68% inhibition
ferulic acid
-
97.4% and 99.1% residual activity at 0.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
gallic acid
-
91.1% and 75.3% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
Guanidine HCl
10 mM, 8% loss of activity of native enzyme, 10% loss of activity of recombinant enzyme, beta-glucosidase activity
guanidine hydrochloride
-
83.3-45.5% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 1-2 M
imidazole
-
competitive inhibition with laminarin, non-competitive inhibition with 4-nitrophenyl-beta-D-glucopyranoside
Isopropanol
-
66.5-70.1% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
jacalin-related lectin
-
isoform Pyk10 is localized in ER bodies and has beta-D-glucosidase and beta-D-fucosidase activities. Jacalin-related lectins regulate the size of the active Pyk10 complexes, with two types of lectins working antagonistically
-
N-Bromoacetyl-beta-D-galactosylamine
-
inhibition of the glucosidase- and galactosidase-activities only above pH 8.0
N-bromosuccinamide
2 mM, 92% loss of activity of native enzyme, 94% loss of activity of recombinant enzyme, beta-glucosidase activity
N-ethyl-5-phenylisoxazolium-3'-sulfonate
-
nearly complete inhibition at 2 mM
p-coumaric acid
-
70.5% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside as substrate
p-nitrophenyl-1-thio-beta-D-glucopyranoside
competitively inhibits with p-nitrophenyl-beta-D-glucopyranoside, o-nitrophenyl-beta-D-glucopyranoside, and 4-methylumbelliferyl-beta-D-glucopyranoside as substrates
PEG 8000
-
67.6% and 58.5% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
-
phenol
the gelatin-immobilized enzyme is not sensitive in contrast to the native enzyme
Phenylmercuriacetate
-
0.1 mM, 80% inhibition, 1 mM, complete inhibition, activity is restored by addition of 10 mM beta-mercaptoethanol
polyvinyl alcohol
-
71.2% and 56.8% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
propan-2-ol
-
inhibition above 50% concentration, 50% inhibition at 90%-100% propan-2-ol
syringaldehyde
-
92.8% and 96.4% residual activity at 0.25 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
syringic acid
-
95.2% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside as substrate
Tannic acid
-
complete inhibition at 0.0625 mM with 4-nitrophenyl beta-D-glucopyranoside as substrate
thiocellobiose
a substrate analogue-type inhibitor, competitive inhibition, binding structure and inhibition mechanism, overview
vanillic acid
-
87.6% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside as substrate
Vanillin
-
94% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside as substrate
2-deoxy-D-glucose
-
82.7% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 1 mg/ml
2-mercaptoethanol
1 mM, 9% loss of activity of native enzyme, 10% loss of activity of recombinant enzyme, beta-glucosidase activity
4-nitrophenyl-beta-D-glucopyranoside
-
inhibition of intracellular enzyme if higher than 0.4 mM
Ag+
-
1 mM, 65% inhibition, 10 mM, complete inhibition, 50% inhibition at 14 mM in the presence of 250 mM beta-mercaptoethanol
Ag+
5 mM, 72% inhibition; 5 mM, 76% inhibition; 5 mM, 89% inhibition
AgNO3
-
0.5 mM, 81% inhibition, reversible by the addition of 50 mM beta-mercaptoethanol
Al3+
-
83.5% and 43.7% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
Ba2+
-
76.7% residual activity at 2.5 mM with cellobiose as substrate
beta-D-glucose
-
5 mM, approx. 50% inhibition, 100 mM, almost complete inhibition
beta-D-glucose
Thermochaetoides thermophila
-
Ki for cellobiase activity: 91 mM, Ki for cell-bound aryl-beta-glucosidase activity: 0.53 mM, Ki for extracellular aryl-beta-glucosidase activity: 0.34 mM
beta-D-glucose
-
competitive inhibition, Ki for beta-glucosidase I: 0.62 mM
beta-mercaptoethanol
-
the mycelial extract shows 87.1% residual activity at 1% (v/v)
beta-mercaptoethanol
-
79-22% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 10-20 mM
Ca2+
-
the mycelial extract shows 59.5% residual activity at 20 mM, the purified enzyme shows 53.5% residual activity at 20 mM
cellobiose
Thermochaetoides thermophila
-
Ki for cellobiase activity: 0.31 mM, Ki for cell-bound aryl-beta-glucosidase activity: 0.72 mM, Ki for extracellular aryl-beta-glucosidase activity: 0.56 mM
cellobiose
Thermochaetoides thermophila
-
competitive vs. p-nitrophenyl-beta-D-glucopyranoside
conduritol-B-epoxide
-
bound as an ester of (+) chiro-inositol to aspartic acid
Cr3+
1 mM, 29% loss of activity of native enzyme, 30% loss of activity of recombinant enzyme, beta-glucosidase activity
Cu2+
-
stronger inhibition for linamarin than for amygdalin at 1 mM, both PGI and PGII
Cu2+
-
2 mM, significant inhibition, both isoforms beta-glu 2 and beta-glu 1
Cu2+
1 mM, 22% inhibition, not significantly stimulated or inhibited by other divalent cations
Cu2+
-
the mycelial extract shows 58.1% residual activity at 2 mM, the purified enzyme shows 44.4% residual activity at 2 mM
Cu2+
-
78.4% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 2.0 mM
D-glucono-1,5-lactone
-
complete inhibition at 1 mM for PGI and PGII
D-glucono-1,5-lactone
Sporotrichum pulverulentum
-
competitive inhibition, Ki: 0.0004 mM for enzyme A, Ki: 0.0015 mM for enzyme B, Ki: 0.12 mM for cell wall bound enzyme
D-glucono-1,5-lactone
-
competitive inhibition, Ki: 0.003 mM for 4-nitrophenyl-beta-D-glucopyranoside
D-glucono-1,5-lactone
-
beta-glucosidase 1, Ki: 1.8 mM, beta-glucosidase 2, Ki: 1.17 mM
D-gluconolactone
-
competitive inhibition of wild-type enzyme and mutant W49A
D-glucose
-
high tolerance towards D-glucose inhibition with 4-nitrophenyl beta-D-glucopyranoside as substrate
D-glucose
-
the enzyme is able to tolerate D-glucose concentration up to 2500 mM, retaining about 80% of its maximal activity
D-glucose
-
competitively versus substrate 4-nitrophenyl beta-D-glucopyranoside
D-glucose
-
enzyme is active and stable in presence of 5 g glucose per l. In presence of 100 g glucose per l, 25% residual activity
D-glucose
-
strong inhibitor, 15.7% residual activity at 10 mg/ml
D-glucose
-
1%, 17-26% inhibition of isoform A, 10-22% inhibition of isoform B
D-glucose
the gelatin-immobilized enzyme is less sensitive than the native enzyme
D-glucose
-
strong inhibitor, 14.7% residual activity at 10 mg/ml
D-glucose
-
14.6% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 20 mg/ml
D-glucose
when the glucose concentration is 400 mM, the native enzyme is completely inactivated, and the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde with 2mM Zn2+ maintains 63% of its initial activity, which is 19.5% higher than the activity of immobilized enzyme in the absence of Zn2+
delta-gluconolactone
-
competitive, both isoforms beta-glu 2 and beta-glu 1
delta-gluconolactone
5 mM, 85% loss of activity of native enzyme, 86% loss of activity of recombinant enzyme, beta-glucosidase activity
diethyldicarbonate
-
binds to the active site, 4-nitrophenyl beta-D-glucoside partially protects against inactivation
dithiothreitol
-
the mycelial extract shows 75.7% residual activity at 20 mM
dithiothreitol
-
82.5% residual activity and complete inhibition at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
DMSO
-
92.9% and 57% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
DTT
1 mM, 4% loss of activity of native enzyme, 5% loss of activity of recombinant enzyme, beta-glucosidase activity
EDTA
-
46.49% residual activity of the enzyme from midgut at 4 mM EDTA, 29.8% residual activity of the enzyme from salivary gland at 4 mM EDTA; 4 mmol/l, 46.49% relative enzyme activity in midgut, 29.8% relative enzyme activity in salivary glands
EDTA
-
the mycelial extract shows 64.3% residual activity at 20 mM, the purified enzyme shows 37.4% residual activity at 20 mM
EDTA
-
69.1% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 20 mM
ethanol
-
inhibition at concentration below 10%, inhibition of 40-60% at about 12-14% ethanol in wine solution of strain CBS314, depends on the yeast strain, overview
ethanol
10% v/v, 180% of initial activity, 20% v/v, 70% of initial activity
ethanol
-
10%, 16-24% inhibition of isoform A, 10-29% inhibition of isoform B
ethanol
-
70.6% and 55.6% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
Fe3+
5 mM, 5% inhibition; 5 mM, 6% inhibition; 5 mM, 7% inhibition
gluconolactone
competitively inhibits with p-nitrophenyl-beta-D-glucopyranoside, o-nitrophenyl-beta-D-glucopyranoside, and 4-methylumbelliferyl-beta-D-glucopyranoside as substrates
gluconolactone
-
competitively versus substrate 4-nitrophenyl beta-D-glucopyranoside
Hg2+
-
strong inactivation at 0.5 mM, reversal by addition of 10 mM beta-mercaptoethanol
Hg2+
-
2 mM, significant inhibition, both isoforms beta-glu 2 and beta-glu 1
Hg2+
1 mM, 55% loss of activity of native enzyme, 58% loss of activity of recombinant enzyme, beta-glucosidase activity
Hg2+
-
1 mM, complete inhibition, 73% reversion by addition of 10 mM dithiothreitol
Hg2+
-
the mycelial extract shows 26.8% residual activity at 20 mM, the purified enzyme shows 1.2% residual activity at 20 mM
Hg2+
-
40.9% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 2.0 mM
HgCl2
-
0.5 mM, 77% inhibition, reversible by the addition of 50 mM beta-mercaptoethanol
K+
-
58.03% residual activity of the enzyme from midgut at 40 mM K+, 45.95% residual activity of the enzyme from salivary gland at 40 mM K+
K+
-
the mycelial extract shows 70.9% residual activity at 20 mM, the purified enzyme shows 41.5% residual activity at 20 mM
K+
-
76.2% and 81.9% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
KCl
-
40 mmol/l, 58.03% relative enzyme activity in midgut, 45.95% relative enzyme activity in salivary glands
KCl
-
80.3% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 20 mM
Mg2+
1 mM, 7% loss of activity, native and recombinant enzyme, beta-glucosidase activity
Mg2+
-
the mycelial extract shows 62.1% residual activity at 20 mM, the purified enzyme shows 39.2% residual activity at 20 mM
Mg2+
-
62.7% residual activity at 2.5 mM with cellobiose as substrate
Mn2+
-
the mycelial extract shows 42.9% residual activity at 20 mM, the purified enzyme shows 26.3% residual activity at 20 mM
Mn2+
-
54.7% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 20 mM
Mn2+
-
49.6% and 67.1% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
N-ethylmaleimide
-
rapid loss of activity at 5 mM, reversal by addition of beta-mercaptoethanol
Na+
-
70.6% and 57.1% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
Ni2+
1 mM, 16% loss of activity of native enzyme, 18% loss of activity of recombinant enzyme, beta-glucosidase activity
p-chloromercuribenzene sulfonic acid
thermophilic anaerobic bacterium
-
nearly complete inhibition at 1 mM
p-chloromercuribenzoic acid
-
the mycelial extract shows 66.9% residual activity at 0.5 mM, the purified enzyme shows 36.9% residual activity at 0.5 mM
p-chloromercuribenzoic acid
Thermochaetoides thermophila
-
sensitivity only for cellobiase activity
p-nitrophenyl-beta-D-glucopyranoside
-
strong substrate inhibition above 0.5 mM
p-nitrophenyl-beta-D-glucopyranoside
-
minimal substrate inhibition above 1.5 mM
p-nitrophenyl-beta-D-glucopyranoside
-
minimal substrate inhibition above 1.5 mM
p-nitrophenyl-beta-D-glucopyranoside
-
substrate inhibition above 5 mM
SDS
-
61.32% residual activity of the enzyme from midgut at 8 mM SDS, 43.75% residual activity of the enzyme from salivary gland at 8 mM SDS; 8 mmol/l, 61.32% relative enzyme activity in midgut, 43.75% relative enzyme activity in salivary glands
SDS
5 mM, 55% inhibition; 5 mM, 62% inhibition; 5 mM, 95% inhibition
SDS
-
the mycelial extract shows no residual activity at 0.05% (v/v), purified enzyme shows 50% residual activity at 0.05% (v/v)
SDS
-
82.4% and 60.6% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
Sodium azide
-
the mycelial extract shows 67.6% residual activity at 20 mM, the purified enzyme shows 42.7% residual activity at 20 mM
Sodium azide
-
77.8% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 20 mM
Triton X-100
-
the mycelial extract shows 70.6% residual activity at 1% (v/v), the purified enzyme is not inhibited by 1% (v/v) Triton X-100
Triton X-100
-
57.5% and 45% residual activity at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
Urea
-
half-life of the wild-type enzyme at 4 M is 72 min, and of the mutant enzyme 126 min
Urea
-
53.8% residual activity of the enzyme from midgut at 4 M urea, 20.05% residual activity of the enzyme from salivary gland at 6 M urea; 6000 mmol/l, 56.41% relative enzyme activity in midgut, 20.05% relative enzyme activity in salivary glands
Urea
-
the mycelial extract shows 8% residual activity at 4 M, the purified enzyme shows 66% residual activity at 4 M
Urea
-
69% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 4 M
Zn2+
1 mM, 47% loss of activity of native enzyme, 52% loss of activity of recombinant enzyme, beta-glucosidase activity
Zn2+
-
the mycelial extract shows 38.6% residual activity at 20 mM, the purified enzyme shows 30.3% residual activity at 20 mM
Zn2+
-
67.5% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 2.0 mM
Zn2+
-
63% residual activity and complete inhibition at 2.5 mM with 4-nitrophenyl beta-D-glucopyranoside and cellobioside as substrate, respectively
additional information
the enzyme is very tolerant to glucose inhibition
-
additional information
-
the enzyme is very tolerant to glucose inhibition
-
additional information
-
the enzyme is D-glucose-resistant showing 92% activity retension at 250 mM D-glucose
-
additional information
not inhibitory: EDTA, 2-mercaptoethanol
-
additional information
no or poor effects by 0.1 mM of Co2+, Cu2+, Mg2+, Mn2+, Ni2+, Zn2+, or EDTA
-
additional information
-
no or poor effects by 0.1 mM of Co2+, Cu2+, Mg2+, Mn2+, Ni2+, Zn2+, or EDTA
-
additional information
-
no inhibition by EDTA and insensitive to fructose, ribose, galactose, and L-arabinose up to 50 mM
-
additional information
-
the enzyme is not inhibited by D-fructose
-
additional information
-
the enzyme is inhibited by metabolites in the aqueous ethanol extract of Fucus evanescens
-
additional information
-
not inhibitory: 2-mercaptoethanol, sodium dodecyl sulfate, EDTA
-
additional information
-
not inhibitory: D-glucose, enzyme retains 84% activity at glucose concentrations up to 140 mM
-
additional information
-
mannose, fructose, ribose, galactose, sorbose, arabinose, maltose and sucrose are without effect
-
additional information
-
fruit fly attacks in october reduce the enzyme activity in olive fruits, overview
-
additional information
-
no or poor inhibition by Ca2+ and DTT
-
additional information
no effect by EDTA, DTT, 2-mercaptoethanol, iodoacetc acid, glutathione, L-fucose, L-rhamnose, and D-xylose
-
additional information
-
inhibiting saccharides used at three concentrations, 10, 50, and 100 mM
-
additional information
-
not inhibited by 2-propyl 3-deoxy-4-S-(beta-D-xylopyranosyl)-4-thio-alpha-D-xylohexopyranoside and 2-propyl 3-deoxy-4-S-(beta-D-xylopyranosyl)-4-thio-alpha-D-xylo-hexopyranoside
-
additional information
significant resistant to D-glucose concentration up to 500 mM
-
additional information
-
the enzyme is not affected by Ba2+, Mg2+, Mn2+, Sr2+, and Ca2+
-
additional information
-
no inhibition by D-glucose and D-fructose
-
additional information
-
the enzyme is not affected by glycerol, EDTA, acetic acid, SDS, Triton X-100, D-glucose, and ethanol
-
additional information
-
optimal activity is obtained with 100 mM phosphate buffer and, the activity decreased at 150 and 200 mM but not dramatically
-
additional information
-
no inhibition by SDS and 2-mercaptoethanol as long as the enzyme is not preheated
-
additional information
the enzyme is not inhibited by glucose up to 5% w/v
-
additional information
not inhibitory: EDTA (10 mM), 1% of Urea, 2-mercaptoethanol, Triton X-100, and Tween-80
-
additional information
not inhibited by glucose up to 5% (w/v)
-
additional information
the enzyme is unaffected by EDTA and Tween 20
-
additional information
-
the enzyme is unaffected by EDTA and Tween 20
-
additional information
not inhibited by EDTA and phenylmethylsulfonyl fluoride
-
additional information
-
no inhibition by D-glucose and D-fructose
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-Methyl-1-pentanol
addition of 20% v/v n-octanol results in a higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview
2-methyl-2-pentanol
addition of 20% v/v n-octanol results in a higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview
3-methyl-1-pentanol
addition of 20% v/v n-octanol results in an over 40fold higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview
4-hydroxybenzoic acid
-
109.7% activity at 2.5 mM with cellobioside as substrate
4-Methyl-1-pentanol
addition of 20% v/v n-octanol results in a higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview
acetone
hydrolysis activity is enhanced in the presence of non-acceptor type organic solvents such as hexane, cyclohexane, diethylether, and acetone
CaCl2
-
40 mmol/l, 233.33% relative enzyme activity in midgut, 193.31% relative enzyme activity in salivary glands
Cyclohexane
hydrolysis activity is enhanced in the presence of non-acceptor type organic solvents such as hexane, cyclohexane, diethyl ether, and acetone
diethylether
hydrolysis activity is enhanced in the presence of non-acceptor type organic solvents such as hexane, cyclohexane, diethylether, and acetone
Gaucher spleen heat-stable factor
-
15fold increase for hydrolysis of 17beta-estradiol-17'-beta-D-glucoside
-
hexane
hydrolysis activity is enhanced in the presence of non-acceptor type organic solvents such as hexane, cyclohexane, diethyl ether, and acetone
Inositol
-
constant enzyme activation, values of relative activation about 40%
jacalin-related lectin
-
isoform Pyk10 is localized in ER bodies and has beta-D-glucosidase and beta-D-fucosidase activities. Jacalin-related lectins regulate the size of the active Pyk10 complexes, with two types of lectins working antagonistically
-
MgCl2
-
40 mmol/l, 200% relative enzyme activity in midgut, 169.49% relative enzyme activity in salivary glands
n-Heptanol
addition of 20% v/v n-octanol results in an over 40fold higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview
n-Hexanol
addition of 20% v/v n-octanol results in an over 40fold higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview
n-Octanol
addition of 20% v/v n-octanol results in a 54fold higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview
NaCl
-
40 mmol/l, 198.57% relative enzyme activity in midgut, 163.63% relative enzyme activity in salivary glands
p-coumaric acid
-
118% activity at 2.5 mM with cellobioside as substrate
protein PBPI
binding protein, interacts with beta-glucosidases and activates them
-
protein PBPII
binding protein, interacts with beta-glucosidases and activates them
-
SDS
1 mg/ml, native enzyme is activated to 118.3% of control, recombinant enzyme is activated to 115.6% of control, beta-glucosidase activity
syringic acid
-
111.4% activity at 2.5 mM with cellobioside as substrate
vanillic acid
-
125.1% activity at 2.5 mM with cellobioside as substrate
Vanillin
-
118% activity at 2.5 mM with cellobioside as substrate
Zn2+
presence of 2 mM Zn2+ increases the relative activity of the immobilized enzyme to 192% and 199% with cellobiose and 4-nitrophenyl-beta-D-glucopyranoside as substrates
2-mercaptoethanol
-
129.9% relative activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 1-2 mM
beta-mercaptoethanol
-
the purified enzyme shows 152.9% relative activity at 1% (v/v)
D-glucose
-
50 mM, 204% of initial activity, activating constant 36.7 mM
D-glucose
-
D-glucose (1% w/v) in the reaction medium stimulates beta-glucosidase activity by about 2fold in crude extracts from mycelia grown in sugarcane bagasse
D-xylose
-
50 mM, 191% of initial activity, activating constant 43.2 mM
D-xylose
-
xylose (1% w/v) in the reaction medium stimulates beta-glucosidase activity by about 2fold in crude extracts from mycelia grown in sugarcane bagasse
dithiothreitol
-
the purified enzyme shows 108.4% relative activity at 20 mM
DMSO
10% v/v, 106% of initial activity, 20% v/v, 112.6% of initial activity
DMSO
10% (v/v), native enzyme is activated to 102.3% of control, recombinant enzyme is activated to 106.4% of control, beta-glucosidase activity
EDTA
1 mM, native enzyme is activated to 110.7% of control, recombinant enzyme is activated to 108.2% of control, beta-glucosidase activity
ethanol
-
activation depends on the yeast strain, e.g. strain Y8 shows 5fold increased activity at 14% ethanol in wine solution, overview
ethanol
-
in the presence of 16% (v/v) ethanol the enzyme activity is increased more than 2fold
ethanol
10% v/v, 180% of initial activity, 20% v/v, 70% of initial activity
ethanol
10%, 127% of initial activity, 50%, 0.6% of initial activity
ethanol
-
strain AL41 shows increased activity at 14% ethanol in wine solution
methanol
-
in the presence of 16% (v/v) methanol the enzyme activity is increased more than 2fold
methanol
10%, 121% of initial activity, 50%, 1.3% of initial activity
propan-2-ol
10%, 107% of initial activity, 50%, 0.2% of initial activity
Triton X-100
10 mg/ml, native enzyme is activated to 113.4% of control, recombinant enzyme is activated to 111.7% of control, beta-glucosidase activity
additional information
-
poor activation by glycerol, dimethyl sulfoxide, and dithiothreitol
-
additional information
-
high concentrations (up to 0.2 M) of fructose, malate, lactate, mannitol and sorbitol have little or no effect on the enzyme activity
-
additional information
-
mannose, fructose, ribose, galactose, sorbose, arabinose, maltose and sucrose are without effect
-
additional information
the enzyme is induced by growth on rice bran hemicellulose, and slightly by pectin, xylan, and glucose, no effect by EDTA, L-fucose, G-glucuronic acid, D-mannose, L-rhamnose, and D-xylose
-
additional information
at -20 to 40 °C no significant enzymatic activity is detected in the absence of microwave irradiation. However, a greater than 4 orders of magnitude increase in enzymatic activity of Pfu CelB is achieved with 300 W of microwave irradiation
-
additional information
-
the enzyme is not affected by glycerol, EDTA, acetic acid, SDS, Triton X-100, D-glucose, and ethanol
-
additional information
-
the addition of vitamins such as thiamin hydrochloride, folic acid, pyridoxine hydrochloride, and riboflavin increases the enzyme activity. A 1.6fold increase in enzyme activity is observed when the culture medium is supplemented with 20 mg/l of inositol
-
additional information
the hydrophobic linker region in BGLII is required for activation by organic solvents
-
additional information
-
the hydrophobic linker region in BGLII is required for activation by organic solvents
-
additional information
the enzyme is unaffected by EDTA and Tween 20
-
additional information
-
the enzyme is unaffected by EDTA and Tween 20
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside
-
30°C, pH 5.5
0.32
2-hydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside
-
30°C, pH 5.5
0.14
3-O-[beta-D-glucopyranosyl-(1-2)-beta-D-glucopyranosyl]-20-O-[beta-D-glucopyranosyl-(1-6)-beta-D-glucopyranosyl]-20(S)-protopanaxadiol
-
pH 7.0, 37°C
2.1
4-hydroxyphenyl-beta-D-glucopyranoside
-
hydrophobicity of the aglycon takes a substantial role in the binding of the substrate at subsite 2 of the 2 main binding-modes
0.19
4-nitrophenyl-alpha-L-arabino-pyranoside
recombinant wild-type enzyme
3.5
benzyl-beta-D-glucopyranoside
-
hydrophobicity of the aglycon takes a substantial role in the binding of the substrate at subsite 2 of the 2 main binding-modes
2.5
2,4-dihydroxy-1,4-benzoxazin-3-one glucoside
isoform GLU1, at pH 5.5 and 30°C
0.015
2,4-dinitrophenyl beta-D-glucoside
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 6.0, at 40°C
0.1
2,4-dinitrophenyl beta-D-glucoside
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.26
2,4-dinitrophenyl beta-D-glucoside
-
wild type enzyme, in 0.1 M sodium acetate, pH 6.0, at 40°C
0.49
2,4-dinitrophenyl beta-D-glucoside
-
wild type enzyme, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.1
2-nitrophenyl beta-D-glucopyranoside
-
130000 Da form, pH 4.5, 37°C
0.11
2-nitrophenyl beta-D-glucopyranoside
-
230000 Da form, pH 4.5, 37°C
0.2
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C
0.38
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C, presence of 2 M formate
1.01
2-nitrophenyl beta-D-glucopyranoside
mutant E387G, pH 6.5, 65°C, presence of 2 M formate
1.02
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
1.02
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
1.23
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
1.23
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
1.36
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
1.36
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
1.39
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
1.39
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
1.4
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
1.4
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
1.9
2-nitrophenyl beta-D-glucopyranoside
-
in 50 mM sodium acetate, pH 5.5, at 37°C
2.8
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 6.0, 65°C
3.1
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 5.0, 65°C
3.3
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 4.0, 65°C
3.76
2-nitrophenyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
6.6
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 3.0, 65°C
6.8
2-nitrophenyl-beta-D-galactopyranoside
-
at 50°C, in 50 mM sodium phosphate buffer, pH 6.0
0.08
4-methylumbeliferyl beta-D-glucoside
mutant K201F, 30°C, pH 6.0
1.7
4-methylumbeliferyl beta-D-glucoside
mutant M453A, 30°C, pH 6.0
2.3
4-methylumbeliferyl beta-D-glucoside
wild-type, 30°C, pH 6.0
2.6
4-methylumbeliferyl beta-D-glucoside
mutant E194A, 30°C, pH 6.0
2.6
4-methylumbeliferyl beta-D-glucoside
mutant K201A, 30°C, pH 6.0
6.2
4-methylumbeliferyl beta-D-glucoside
mutant E190Q, 30°C, pH 6.0
6.3
4-methylumbeliferyl beta-D-glucoside
mutant E190A, 30°C, pH 6.0
0.33
4-methylumbelliferyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
0.76
4-methylumbelliferyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F466S/A467S
0.9
4-methylumbelliferyl beta-D-glucopyranoside
pH 4.0, 60°C
2.97
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant N370S/L444P, Gaucher's disease patient
3.64
4-methylumbelliferyl beta-D-glucoside
-
pH 5.4, 37°C, Gaucher's disease enzyme from leukocytes
4.13
4-methylumbelliferyl beta-D-glucoside
-
pH 5.4, 37°C, healthy human enzyme from leukocytes
6.18
4-methylumbelliferyl beta-D-glucoside
-
pH 5.4, 37°C, healthy human enzyme from fibroblasts
7.18
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant N370S, heterozygote
12.37
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant N370S/N370S, Gaucher's disease patient
12.4
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant L444P, heterozygote
18.43
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant N370S and deletion mutation, Gaucher's disease patient
37.2
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant D409H, heterozygote
0.1
4-methylumbelliferyl-beta-D-glucoside
-
beta-glucosidase C, pH 5, 30°C
0.12
4-nitrophenyl alpha-D-glucopyranoside
-
isoform beta-glucosidase 6, pH 5.0, 50°C
0.16
4-nitrophenyl alpha-D-glucopyranoside
-
isoform beta-glucosidase 1, pH 5.0, 50°C
0.22
4-nitrophenyl alpha-D-glucopyranoside
-
isoform beta-glucosidase 3, pH 5.0, 50°C
0.25
4-nitrophenyl alpha-D-glucopyranoside
-
isoform beta-glucosidase 2, pH 5.0, 50°C
0.34
4-nitrophenyl alpha-D-glucopyranoside
-
isoform beta-glucosidase 4, pH 5.0, 50°C
0.56
4-nitrophenyl alpha-D-glucopyranoside
-
isoform beta-glucosidase 5, pH 5.0, 50°C
2.01
4-nitrophenyl beta-D-cellobioside
pH not specified in the publication, temperature not specified in the publication
0.14
4-nitrophenyl beta-D-fucopyranoside
wild-type, pH 5.5, 75°C
0.39
4-nitrophenyl beta-D-fucopyranoside
mutant N223Y, pH 5.5, 75°C
0.46
4-nitrophenyl beta-D-fucopyranoside
pH 4.6, 37°C, native enzyme
0.47
4-nitrophenyl beta-D-fucopyranoside
pH not specified in the publication, temperature not specified in the publication
0.47
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, without additive
0.51
4-nitrophenyl beta-D-fucopyranoside
pH 4.6, 37°C, recombinant enzyme
0.65
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 250 mM D-galactose
0.94
4-nitrophenyl beta-D-fucopyranoside
80°C, pH is not specified in the publication, wild-type
0.98
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 25 mM cellobiose
1.29
4-nitrophenyl beta-D-fucopyranoside
80°C, pH is not specified in the publication, mutant enzyme D206N
1.3
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 250 mM D-xylose
3.93
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 250 mM D-glucose
5
4-nitrophenyl beta-D-fucopyranoside
mutant N223Q, pH 5.5, 75°C
0.64
4-nitrophenyl beta-D-galactopyranoside
pH 4.6, 37°C, native enzyme
0.65
4-nitrophenyl beta-D-galactopyranoside
pH not specified in the publication, temperature not specified in the publication
0.68
4-nitrophenyl beta-D-galactopyranoside
pH 4.6, 37°C, recombinant enzyme
0.71
4-nitrophenyl beta-D-galactopyranoside
mutant N223Y, pH 5.5, 75°C
3.61
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 5.5, 75°C
6.18
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 250 mM D-galactose
7.44
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 25 mM cellobiose
7.65
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, without additive
8.21
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 250 mM D-xylose
13.3
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 250 mM D-glucose
17.6
4-nitrophenyl beta-D-galactopyranoside
mutant N223Q, pH 5.5, 75°C
0.006
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.042
4-nitrophenyl beta-D-glucopyranoside
mutant D58A, pH 5.6, 90°C, 0.1 M NaN3
0.047
4-nitrophenyl beta-D-glucopyranoside
mutant E458G, pH 5.6, 90°C, 0.1 M NaN3
0.057
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.06
4-nitrophenyl beta-D-glucopyranoside
mutant D242G, pH 5.6, 90°C, 0.1 M NaN3
0.06
4-nitrophenyl beta-D-glucopyranoside
mutant E458G, pH 5.6, 90°C
0.06
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.6, 90°C
0.08
4-nitrophenyl beta-D-glucopyranoside
mutant D58A, pH 5.6, 90°C
0.09
4-nitrophenyl beta-D-glucopyranoside
mutant W243F, pH 5.6, 90°C
0.1
4-nitrophenyl beta-D-glucopyranoside
-
130000 Da form, pH 4.5, 37°C
0.117
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.13
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 72°C, recombinant enzyme
0.16
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.164
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, compared to KM-value: 0.03 mM for 4-nitrophenyl-beta-D-xylopyranoside of the beta-xylosidase activity, suggesting that RuBGX1 prefers 4-nitrophenyl-beta-D-xylopyranoside substrate
0.17
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.6, 90°C, 0.1 M NaN3
0.17
4-nitrophenyl beta-D-glucopyranoside
mutant F310L, pH 5.6, 80°C
0.18
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 72°C, recombinant enzyme
0.19
4-nitrophenyl beta-D-glucopyranoside
-
230000 Da form, pH 4.5, 37°C
0.19
4-nitrophenyl beta-D-glucopyranoside
mutant F310E, pH 5.6, 80°C
0.2
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 60°C
0.2
4-nitrophenyl beta-D-glucopyranoside
presence of D-glucose, pH 6.0, 50°C
0.21
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.5, 75°C
0.22
4-nitrophenyl beta-D-glucopyranoside
mutant W322A, pH 5.6, 80°C
0.24
4-nitrophenyl beta-D-glucopyranoside
mutant N221F, pH 5.6, 80°C
0.24
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.6, 80°C
0.25
4-nitrophenyl beta-D-glucopyranoside
pH 7.0, 40°C, recombinant enzyme
0.29
4-nitrophenyl beta-D-glucopyranoside
pH 7.0, 60°C
0.3
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.3
4-nitrophenyl beta-D-glucopyranoside
mutant N220F, pH 5.6, 80°C
0.31
4-nitrophenyl beta-D-glucopyranoside
mutant N220S, pH 5.6, 80°C
0.316
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.35
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
0.35
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
0.35
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
0.35
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
0.36
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
0.36
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
0.37
4-nitrophenyl beta-D-glucopyranoside
-
in 50 mM sodium acetate, pH 5.5, at 37°C
0.39
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
0.39
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
0.42
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
0.42
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
0.43
4-nitrophenyl beta-D-glucopyranoside
mutant N221S, pH 5.6, 80°C
0.49
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, without additive
0.5
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.52
4-nitrophenyl beta-D-glucopyranoside
pH not specified in the publication, temperature not specified in the publication
0.53
4-nitrophenyl beta-D-glucopyranoside
pH 4.6, 37°C, native enzyme
0.58
4-nitrophenyl beta-D-glucopyranoside
pH 4.6, 37°C, recombinant enzyme
0.64
4-nitrophenyl beta-D-glucopyranoside
mutant F224I, pH 5.6, 80°C
0.706
4-nitrophenyl beta-D-glucopyranoside
-
isoform BGL1, pH not specified in the publication, at 55°C
0.706
4-nitrophenyl beta-D-glucopyranoside
-
isoform BGL2, pH not specified in the publication, at 55°C
0.77
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 25 mM cellobiose
0.83
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 250 mM D-galactose
0.85
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.85
4-nitrophenyl beta-D-glucopyranoside
mutant N223Y, pH 5.5, 75°C
0.9
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 60°C, wild-type enzyme
0.94
4-nitrophenyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
1
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
1.1
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 72°C, recombinant enzyme
1.2
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
1.26
4-nitrophenyl beta-D-glucopyranoside
-
presence of D-glucose, pH 6.5, 60°C
1.33
4-nitrophenyl beta-D-glucopyranoside
-
presence of D-xylose, pH 6.5, 60°C
1.43
4-nitrophenyl beta-D-glucopyranoside
-
both isoforms beta-glu 2 and beta-glu 1
1.5 - 2
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
1.51
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, wild-type enzyme
1.9
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
1.99
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme I48W
2
4-nitrophenyl beta-D-glucopyranoside
pH not specified in the publication, temperature not specified in the publication
2.22
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 250 mM D-xylose
2.32
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, without Zn2+
2.37
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme T484Y
2.42
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme I278F
2.43
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 250 mM D-glucose
2.45
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 60°C, mutant enzyme Y509T
2.48
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme I48W/I278F/T484Y
2.5
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
2.61
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant C174V, pH not specified in the publication, temperature not specified in the publication
2.65
4-nitrophenyl beta-D-glucopyranoside
wild-type, presence of 500 mM D-glucose, pH 5.5, 75°C
2.67
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
2.7
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant H229S, pH not specified in the publication, temperature not specified in the publication
3.03
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, 2 mM Zn2+
3.1
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, pH not specified in the publication, temperature not specified in the publication
3.11
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
3.9
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.0, temperature not specified in the publication
3.99
4-nitrophenyl beta-D-glucopyranoside
mutant N223Y, presence of 500 mM D-glucose, pH 5.5, 75°C
4.6
4-nitrophenyl beta-D-glucopyranoside
80°C, pH is not specified in the publication, wild-type
5
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant L178A, pH not specified in the publication, temperature not specified in the publication
6.8
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant V176A, pH not specified in the publication, temperature not specified in the publication
7
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 0.5 M glucose, pH not specified in the publication, temperature not specified in the publication
7.69
4-nitrophenyl beta-D-glucopyranoside
mutant N223Q, pH 5.5, 75°C
8
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant L178E, pH not specified in the publication, temperature not specified in the publication
8.5
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 1 M glucose, pH not specified in the publication, temperature not specified in the publication
9.1
4-nitrophenyl beta-D-glucopyranoside
pH 7.0, 30°C, recombinant enzyme
9.23
4-nitrophenyl beta-D-glucopyranoside
80°C, pH is not specified in the publication, mutant enzyme D206N
10.14
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 0.25 M glucose, pH not specified in the publication, temperature not specified in the publication
13.3
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 0.1 M glucose, pH not specified in the publication, temperature not specified in the publication
19.6
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant W127F, pH not specified in the publication, temperature not specified in the publication
34.3
4-nitrophenyl beta-D-glucopyranoside
mutant N223Q, presence of 500 mM D-glucose, pH 5.5, 75°C
68
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.2
4-nitrophenyl beta-D-glucoside
pH 6.4, 50°C, recombinant enzyme
0.2
4-nitrophenyl beta-D-glucoside
-
immobilized enzyme, at pH 5.0 and 37°C
0.44
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D496A, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.54
4-nitrophenyl beta-D-glucoside
-
wild type enzyme, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.55
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D487A, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.61 - 0.71
4-nitrophenyl beta-D-glucoside
-
enzymes from several different strains
0.64
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D463A, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.97
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D501A, in 0.1 M sodium acetate, pH 4.0, at 40°C
6.09
4-nitrophenyl beta-D-glucoside
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.4
4-nitrophenyl beta-D-mannopyranoside
80°C, pH is not specified in the publication, mutant enzyme D206N
1.08
4-nitrophenyl beta-D-mannopyranoside
80°C, pH is not specified in the publication, wild-type
0.24
4-nitrophenyl-alpha-L-arabinopyranoside
-
pH 6.5, 30°C, wild-type enzyme
18.9
4-nitrophenyl-alpha-L-arabinopyranoside
-
pH 6.5, 30°C, wild-type enzyme
0.05
4-nitrophenyl-beta-D-fucopyranoside
-
at 50°C, in 50 mM sodium phosphate buffer, pH 6.0
0.08
4-nitrophenyl-beta-D-fucopyranoside
-
pH 6.5, 30°C, wild-type enzyme
0.2
4-nitrophenyl-beta-D-fucopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
0.44
4-nitrophenyl-beta-D-fucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
0.5
4-nitrophenyl-beta-D-fucopyranoside
in 100 mM sodium acetate, pH 5.0, at 30°C
42.7
4-nitrophenyl-beta-D-fucopyranoside
-
pH 6.5, 30°C, wild-type enzyme
0.57
4-nitrophenyl-beta-D-fucoside
-
pH 5.0, 30°C, recombinant enzyme
1.32
4-nitrophenyl-beta-D-galactopyranoside
-
at 50°C, in 50 mM sodium phosphate buffer, pH 6.0
1.5
4-nitrophenyl-beta-D-galactopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
1.93
4-nitrophenyl-beta-D-galactopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
4.02
4-nitrophenyl-beta-D-galactopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
6.06
4-nitrophenyl-beta-D-galactopyranoside
in 100 mM sodium acetate, pH 5.0, at 30°C
10.2
4-nitrophenyl-beta-D-galactopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
0.11
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme Q39N/E451S, at 30°C
0.22
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme Q39E/E451A, at 30°C
0.38
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme Q39E/E451S, at 30°C
0.002
4-nitrophenyl-beta-D-glucopyranoside
Sporotrichum pulverulentum
-
cell wall bound enzyme
0.0039
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.5, 30°C, wild-type enzyme
0.0039
4-nitrophenyl-beta-D-glucopyranoside
-
wild type enzyme, in 50 mM MOPS buffer (pH 6.5), at 30°C
0.0082
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.8, in 50 mM MOPS buffer (pH 6.5), at 30°C
0.0082
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.8, in 50 mM MOPS buffer (pH 6.5), at 30°C
0.012
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.5, 30°C, wild-type enzyme
0.012
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.6, in 50 mM MOPS buffer (pH 6.5), at 30°C
0.012
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.6, in 50 mM MOPS buffer (pH 6.5), at 30°C
0.02
4-nitrophenyl-beta-D-glucopyranoside
pH 5.0, 50°C, recombinant enzyme
0.032
4-nitrophenyl-beta-D-glucopyranoside
-
marked increase for chimeric enzyme
0.076
4-nitrophenyl-beta-D-glucopyranoside
Thermochaetoides thermophila
-
for extracellular aryl-beta-D-glucosidase
0.089
4-nitrophenyl-beta-D-glucopyranoside
Thermochaetoides thermophila
-
for cell-bound aryl-beta-D-glucosidase
0.09
4-nitrophenyl-beta-D-glucopyranoside
recombinant enzyme, in 50 mM sodium citrate buffer pH 4.8, at 22°C
0.111
4-nitrophenyl-beta-D-glucopyranoside
-
pH 3.5, 45°C
0.12
4-nitrophenyl-beta-D-glucopyranoside
-
at 50°C, in 50 mM sodium phosphate buffer, pH 6.0
0.187
4-nitrophenyl-beta-D-glucopyranoside
-
purified enzyme, in 0.1 M NaOAc buffer, pH 5.0, at 45°C
0.22
4-nitrophenyl-beta-D-glucopyranoside
-
in 0.2 mM citrate-phosphate buffer, pH 5.5, at 37°C
0.229
4-nitrophenyl-beta-D-glucopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
0.38
4-nitrophenyl-beta-D-glucopyranoside
-
in 50 mM citrate buffer, pH 4.8, at 50°C
0.39
4-nitrophenyl-beta-D-glucopyranoside
-
enzyme from salivary gland, in 100 mM universal buffer (pH 5.0) at 37°C
0.4
4-nitrophenyl-beta-D-glucopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
0.44
4-nitrophenyl-beta-D-glucopyranoside
-
wild type enzyme, in 50 mM MOPS buffer (pH 6.5), at 30°C
0.57
4-nitrophenyl-beta-D-glucopyranoside
-
hydrophobicity of the aglycon in the 4-position takes a substantial role in the binding of the substrate at subsite 2 of the 2 main binding-modes
0.57
4-nitrophenyl-beta-D-glucopyranoside
-
in 50 mM citrate buffer, pH 4.8, at 50°C
0.61
4-nitrophenyl-beta-D-glucopyranoside
-
enzyme from midgut, in 100 mM universal buffer (pH 5.0) at 37°C
0.619
4-nitrophenyl-beta-D-glucopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
0.67
4-nitrophenyl-beta-D-glucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
1.5
4-nitrophenyl-beta-D-glucopyranoside
-
pH 4.5, 25°C, recombinant wild-type enzyme
1.8
4-nitrophenyl-beta-D-glucopyranoside
-
marked decrease for chimeric enzymes
2.63
4-nitrophenyl-beta-D-glucopyranoside
-
large isozyme, pH 3.5, 60°C
4.5
4-nitrophenyl-beta-D-glucopyranoside
-
non-immobilized soluble enzyme
5
4-nitrophenyl-beta-D-glucopyranoside
-
immobilized enzyme to polyacrylamide gel
5.1
4-nitrophenyl-beta-D-glucopyranoside
in 100 mM sodium acetate buffer, pH 5.0, at 65°C
5.2
4-nitrophenyl-beta-D-glucopyranoside
-
immobilized enzyme to CNBr-Sepharose
5.25
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.2, 40°C, mutant enzyme
5.37
4-nitrophenyl-beta-D-glucopyranoside
-
pH 5.0, 30°C, native enzyme
5.78
4-nitrophenyl-beta-D-glucopyranoside
-
pH 5.0, 30°C, recombinant enzyme
6.3
4-nitrophenyl-beta-D-glucopyranoside
in 100 mM sodium acetate, pH 5.0, at 30°C
7.1
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.2, 40°C, wild-type enzyme
1.3
4-nitrophenyl-beta-D-mannopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
0.005
4-nitrophenyl-beta-D-xylopyranoside
-
pH 6.5, 30°C, wild-type enzyme
0.752
4-nitrophenyl-beta-D-xylopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
1.14
4-nitrophenyl-beta-D-xylopyranoside
-
in 0.2 mM citrate-phosphate buffer, pH 5.5, at 37°C
2.64
4-nitrophenyl-beta-D-xylopyranoside
-
pH 6.5, 30°C, wild-type enzyme
0.005
4-nitrophenyl-beta-D-xyloside
-
no change for chimeric enzymes
0.27
cellobiose
-
at 50°C, in 50 mM sodium phosphate buffer, pH 6.0
0.44
cellobiose
-
pH and temperature not specified in the publication
0.57
cellobiose
-
mutant enzyme D496A, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.77
cellobiose
pH not specified in the publication, temperature not specified in the publication
1
cellobiose
-
mutant enzyme D463A, in 0.1 M sodium acetate, pH 4.0, at 40°C
1.02
cellobiose
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 4.0, at 40°C
1.03
cellobiose
-
mutant enzyme D487A, in 0.1 M sodium acetate, pH 4.0, at 40°C
1.11
cellobiose
-
wild type enzyme, in 0.1 M sodium acetate, pH 4.0, at 40°C
1.36
cellobiose
-
mutant enzyme D501A, in 0.1 M sodium acetate, pH 4.0, at 40°C
1.58
cellobiose
recombinant enzyme, in 50 mM sodium citrate buffer pH 4.8, at 22°C
1.85
cellobiose
H0HC94
mutant C174V, pH not specified in the publication, temperature not specified in the publication
2.9
cellobiose
H0HC94
wild-type, pH not specified in the publication, temperature not specified in the publication
3.07 - 5.84
cellobiose
-
4 different isoforms, Km depends on pH-value, ionizing groups control binding of substrate
5.5
cellobiose
H0HC94
mutant H229S, pH not specified in the publication, temperature not specified in the publication
6.8
cellobiose
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
8.3
cellobiose
H0HC94
mutant L178A, pH not specified in the publication, temperature not specified in the publication
8.44
cellobiose
pH 5.5, 60°C, wild-type enzyme
10.1
cellobiose
H0HC94
mutant W127F, pH not specified in the publication, temperature not specified in the publication
12.5
cellobiose
H0HC94
mutant L178E, pH not specified in the publication, temperature not specified in the publication
15.3
cellobiose
beta-(1-4)-linked cellobiose,in 100 mM sodium acetate, pH 5.0, at 30°C
22.4
cellobiose
H0HC94
mutant V176A, pH not specified in the publication, temperature not specified in the publication
1.48
dalcochinin-8'-O-beta-D-glucoside
-
pH 5.0, 30°C, recombinant enzyme
1.68
dalcochinin-8'-O-beta-D-glucoside
-
pH 5.0, 30°C, native enzyme
0.04
Dhurrin
-
pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)
0.04
Dhurrin
-
pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)
0.076
Dhurrin
pH 5.8, 37°C, chimeric mutant (Chim21) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1
0.09
Dhurrin
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
0.09
Dhurrin
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
0.1
Dhurrin
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
0.1
Dhurrin
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
0.101
Dhurrin
pH 5.8, 37°C, chimeric mutant (Chim16) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1 (with an extra 22 amino acids substitution)
0.12
Dhurrin
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
0.12
Dhurrin
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
0.15
Dhurrin
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
0.15
Dhurrin
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
0.18
Dhurrin
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
0.18
Dhurrin
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
0.36
Dhurrin
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
0.36
Dhurrin
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
0.51
Dhurrin
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
0.51
Dhurrin
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
1.9
Dhurrin
isoform GLU1, at pH 5.5 and 30°C
14.9
gentiobiose
beta-(1-6)-linked gentiobiose,in 100 mM sodium acetate, pH 5.0, at 30°C
1.42
lactose
-
at 50°C, in 50 mM sodium phosphate buffer, pH 6.0
3.6
laminaribiose
beta-(1-3)-linked laminaribose,in 100 mM sodium acetate, pH 5.0, at 30°C
0.38
oleuropein
-
enzyme immobilized on polysulphone capillary membranes, at pH 6.5 and 25°C
4.1
oleuropein
isoform GLU1, at pH 5.5 and 30°C
11.3
p-nitrophenyl-beta-D-glucopyranoside
-
35°C, pH 5.0, beta-glucosidase purified from honey sac
12
p-nitrophenyl-beta-D-glucopyranoside
-
35°C, pH 5.0, beta-glucosidase purified from ventriculus
0.09
quercetin 3-O-beta-D-glucopyranoside
mutant N220S, pH 5.6, 80°C
0.09
quercetin 3-O-beta-D-glucopyranoside
mutant N221S, pH 5.6, 80°C
0.13
quercetin 3-O-beta-D-glucopyranoside
wild-type, pH 5.6, 80°C
0.15
quercetin 3-O-beta-D-glucopyranoside
mutant F224I, pH 5.6, 80°C
9.8
sophorose
beta-(1-2)-linked sophorose, in 100 mM sodium acetate, pH 5.0, at 30°C
additional information
additional information
-
kinetics and thermodynamics
-
additional information
additional information
-
kinetics and thermodynamics
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics of multimers of different size, overview, effects of active site modifcation by N-(dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride on kinetics, overview
-
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics, activation energy, and enthalpy and entropy of enzymes from wild-type strain and mutant strain 51 SMr
-
additional information
additional information
-
the enzyme does not follow Michaelis-Menten kinetics
-
additional information
additional information
-
thermodynamics and kinetics of wild-type and mutant enzymes, isothermal titration microcalorimetry
-
additional information
additional information
-
kinetics of hydrolytic activity of mutant enzymes and of transglucosylation activities of recombinant wild-type and mutant enzymes, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
211.1
2,4-dihydroxy-1,4-benzoxazin-3-one glucoside
isoform GLU1, at pH 5.5 and 30°C
1.88
4-nitrophenyl-alpha-L-arabino-pyranoside
recombinant wild-type enzyme
14
4-nitrophenyl-beta-D-mannopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
104.4
oleuropein
isoform GLU1, at pH 5.5 and 30°C
additional information
additional information
-
in the presence of 50 mM azide, the apparent kcat values of the E176Q and E176A mutants are nearly independent of the pH from pH 5-10, while those of the wild-type and E176D enzymes decrease 30 and 8fold, respectively, as the pH increases from 5 to 10
-
0.34
2,4-dinitrophenyl beta-D-glucoside
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 6.0, at 40°C
2.12
2,4-dinitrophenyl beta-D-glucoside
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 4.0, at 40°C
71
2,4-dinitrophenyl beta-D-glucoside
-
wild type enzyme, in 0.1 M sodium acetate, pH 6.0, at 40°C
422
2,4-dinitrophenyl beta-D-glucoside
-
wild type enzyme, in 0.1 M sodium acetate, pH 4.0, at 40°C
11.6
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 6.0, 65°C
19.1
2-nitrophenyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
31.19
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
31.19
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
37.05
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
37.05
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
45.65
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
45.65
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
53.9
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 5.0, 65°C
54.02
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
54.02
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
64.25
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
64.25
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
72.9
2-nitrophenyl beta-D-glucopyranoside
mutant E387G, pH 6.5, 65°C, presence of 2 M formate
305
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 4.0, 65°C
309
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C
439.8
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C, presence of 2 M formate
970
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 3.0, 65°C
0.02
4-methylumbeliferyl beta-D-glucoside
mutant E190A, 30°C, pH 6.0
0.032
4-methylumbeliferyl beta-D-glucoside
mutant K201A, 30°C, pH 6.0
0.114
4-methylumbeliferyl beta-D-glucoside
mutant E190Q, 30°C, pH 6.0
0.231
4-methylumbeliferyl beta-D-glucoside
wild-type, 30°C, pH 6.0
0.2674
4-methylumbeliferyl beta-D-glucoside
mutant E194A, 30°C, pH 6.0
0.62
4-methylumbeliferyl beta-D-glucoside
mutant M453A, 30°C, pH 6.0
1.32
4-methylumbeliferyl beta-D-glucoside
mutant K201F, 30°C, pH 6.0
1.7
4-methylumbelliferyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
8.8
4-methylumbelliferyl beta-D-glucopyranoside
pH 4.0, 60°C
87.2
4-methylumbelliferyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F466S/A467S
7.56
4-nitrophenyl beta-D-cellobioside
pH not specified in the publication, temperature not specified in the publication
12.71
4-nitrophenyl beta-D-fucopyranoside
pH 4.6, 37°C, recombinant enzyme
14.05
4-nitrophenyl beta-D-fucopyranoside
pH not specified in the publication, temperature not specified in the publication
14.77
4-nitrophenyl beta-D-fucopyranoside
pH 4.6, 37°C, native enzyme
16
4-nitrophenyl beta-D-fucopyranoside
wild-type, pH 5.5, 75°C
34.8
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, without additive
38.7
4-nitrophenyl beta-D-fucopyranoside
mutant N223Y, pH 5.5, 75°C
80.4
4-nitrophenyl beta-D-fucopyranoside
mutant N223Q, pH 5.5, 75°C
117
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 250 mM D-galactose
142
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 25 mM cellobiose
322.25
4-nitrophenyl beta-D-fucopyranoside
80°C, pH is not specified in the publication, wild-type
323.41
4-nitrophenyl beta-D-fucopyranoside
80°C, pH is not specified in the publication, mutant enzyme D206N
486
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 250 mM D-glucose
600
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 250 mM D-xylose
5.82
4-nitrophenyl beta-D-galactopyranoside
pH 4.6, 37°C, recombinant enzyme
7.39
4-nitrophenyl beta-D-galactopyranoside
pH 4.6, 37°C, native enzyme
7.95
4-nitrophenyl beta-D-galactopyranoside
pH not specified in the publication, temperature not specified in the publication
17.6
4-nitrophenyl beta-D-galactopyranoside
mutant N223Y, pH 5.5, 75°C
30.8
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 5.5, 75°C
32.3
4-nitrophenyl beta-D-galactopyranoside
mutant N223Q, pH 5.5, 75°C
95.6
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, without additive
128
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 250 mM D-galactose
129
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 25 mM cellobiose
187
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 250 mM D-glucose
197
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 250 mM D-xylose
0.058
4-nitrophenyl beta-D-galactoside
mutant K201A, 30°C, pH 6.0
0.072
4-nitrophenyl beta-D-galactoside
mutant E190A, 30°C, pH 6.0
0.153
4-nitrophenyl beta-D-galactoside
mutant E190Q, 30°C, pH 6.0
0.174
4-nitrophenyl beta-D-galactoside
mutant M453A, 30°C, pH 6.0
0.189
4-nitrophenyl beta-D-galactoside
mutant E194A, 30°C, pH 6.0
4.03
4-nitrophenyl beta-D-galactoside
mutant K201F, 30°C, pH 6.0
0.67
4-nitrophenyl beta-D-glucopyranoside
pH 5.8, 37°C, mutant F198V/F205L/P377A
3.1
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.0, temperature not specified in the publication
3.21
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme I48W
3.6
4-nitrophenyl beta-D-glucopyranoside
mutant E458G, pH 5.6, 90°C
4.24
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme I48W/I278F/T484Y
6.94
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.5, 75°C
7.1
4-nitrophenyl beta-D-glucopyranoside
mutant D58A, pH 5.6, 90°C
7.4
4-nitrophenyl beta-D-glucopyranoside
mutant D58A, pH 5.6, 90°C, 0.1 M NaN3
9.61
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme I278F
10.39
4-nitrophenyl beta-D-glucopyranoside
pH 4.6, 37°C, recombinant enzyme
11.7
4-nitrophenyl beta-D-glucopyranoside
pH not specified in the publication, temperature not specified in the publication
12
4-nitrophenyl beta-D-glucopyranoside
pH 4.6, 37°C, native enzyme
13
4-nitrophenyl beta-D-glucopyranoside
mutant E458G, pH 5.6, 90°C, 0.1 M NaN3
15.05
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme T484Y
22
4-nitrophenyl beta-D-glucopyranoside
mutant N221F, pH 5.6, 80°C
25.3
4-nitrophenyl beta-D-glucopyranoside
mutant D242G, pH 5.6, 90°C, 0.1 M NaN3
26.89
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, without Zn2+
31.2
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, without additive
33.9
4-nitrophenyl beta-D-glucopyranoside
presence of D-glucose, pH 6.0, 50°C
33.93
4-nitrophenyl beta-D-glucopyranoside
-
at pH 7.4 and 65°C
34.26
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
34.26
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
36.7
4-nitrophenyl beta-D-glucopyranoside
mutant N223Y, pH 5.5, 75°C
40.42
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, wild-type enzyme
42.5
4-nitrophenyl beta-D-glucopyranoside
mutant N223Q, pH 5.5, 75°C
51.43
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, 2 mM Zn2+
61
4-nitrophenyl beta-D-glucopyranoside
mutant W322A, pH 5.6, 80°C
68.16
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 60°C, mutant enzyme Y509T
68.9
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
68.9
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
69
4-nitrophenyl beta-D-glucopyranoside
wild-type, presence of 500 mM D-glucose, pH 5.5, 75°C
73.08
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 60°C, wild-type enzyme
78
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.6, 90°C, 0.1 M NaN3
82.8
4-nitrophenyl beta-D-glucopyranoside
mutant N223Q, presence of 500 mM D-glucose, pH 5.5, 75°C
87.24
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
87.24
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
89.6
4-nitrophenyl beta-D-glucopyranoside
mutant W243F, pH 5.6, 90°C
90.8
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
90.8
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
91.1
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 25 mM cellobiose
95
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant C174V, pH not specified in the publication, temperature not specified in the publication
107.9
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
107.9
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
108
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 250 mM D-galactose
110
4-nitrophenyl beta-D-glucopyranoside
-
130000 Da form, pH 4.5, 37°C
129
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.6, 90°C
131.5
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 1 M glucose, pH not specified in the publication, temperature not specified in the publication
145
4-nitrophenyl beta-D-glucopyranoside
mutant N223Y, presence of 500 mM D-glucose, pH 5.5, 75°C
163
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 0.5 M glucose, pH not specified in the publication, temperature not specified in the publication
193
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant H229S, pH not specified in the publication, temperature not specified in the publication
227.64
4-nitrophenyl beta-D-glucopyranoside
80°C, pH is not specified in the publication, wild-type
230
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 0.25 M glucose, pH not specified in the publication, temperature not specified in the publication
236
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 250 mM D-glucose
277
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, pH not specified in the publication, temperature not specified in the publication
282
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant V176A, pH not specified in the publication, temperature not specified in the publication
286
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 250 mM D-xylose
334.9
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 0.1 M glucose, pH not specified in the publication, temperature not specified in the publication
349.62
4-nitrophenyl beta-D-glucopyranoside
80°C, pH is not specified in the publication, mutant enzyme D206N
363
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant L178E, pH not specified in the publication, temperature not specified in the publication
371
4-nitrophenyl beta-D-glucopyranoside
mutant F310L, pH 5.6, 80°C
390
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant L178A, pH not specified in the publication, temperature not specified in the publication
485
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.6, 80°C
508
4-nitrophenyl beta-D-glucopyranoside
mutant F310E, pH 5.6, 80°C
559
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant W127F, pH not specified in the publication, temperature not specified in the publication
757
4-nitrophenyl beta-D-glucopyranoside
mutant N220S, pH 5.6, 80°C
803
4-nitrophenyl beta-D-glucopyranoside
mutant F224I, pH 5.6, 80°C
849
4-nitrophenyl beta-D-glucopyranoside
mutant N220F, pH 5.6, 80°C
1170
4-nitrophenyl beta-D-glucopyranoside
mutant N221S, pH 5.6, 80°C
2226
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 72°C, recombinant enzyme
4000
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 72°C, recombinant enzyme
8664
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 72°C, recombinant enzyme
0.32
4-nitrophenyl beta-D-glucoside
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 4.0, at 40°C
83.5
4-nitrophenyl beta-D-glucoside
-
free enzyme, at pH 5.0 and 37°C
104
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D501A, in 0.1 M sodium acetate, pH 4.0, at 40°C
116.6
4-nitrophenyl beta-D-glucoside
-
immobilized enzyme, at pH 5.0 and 37°C
141
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D496A, in 0.1 M sodium acetate, pH 4.0, at 40°C
141
4-nitrophenyl beta-D-glucoside
-
wild type enzyme, in 0.1 M sodium acetate, pH 4.0, at 40°C
160
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D463A, in 0.1 M sodium acetate, pH 4.0, at 40°C
163
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D487A, in 0.1 M sodium acetate, pH 4.0, at 40°C
20.69
4-nitrophenyl beta-D-mannopyranoside
80°C, pH is not specified in the publication, mutant enzyme D206N
50.99
4-nitrophenyl beta-D-mannopyranoside
80°C, pH is not specified in the publication, wild-type
0.00188
4-nitrophenyl beta-D-xyloside
mutant E190A, 30°C, pH 6.0
9
4-nitrophenyl-alpha-L-arabinopyranoside
-
pH 6.5, 30°C, wild-type enzyme
119
4-nitrophenyl-alpha-L-arabinopyranoside
-
pH 6.5, 30°C, wild-type enzyme
22.1
4-nitrophenyl-beta-D-fucopyranoside
-
pH 6.5, 30°C, wild-type enzyme
27.7
4-nitrophenyl-beta-D-fucopyranoside
-
pH 6.5, 30°C, wild-type enzyme
33.5
4-nitrophenyl-beta-D-fucopyranoside
in 100 mM sodium acetate, pH 5.0, at 30°C
182
4-nitrophenyl-beta-D-fucopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
516
4-nitrophenyl-beta-D-fucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
0.0004
4-nitrophenyl-beta-D-fucoside
-
mutant enzyme Q39N/E451S, at 30°C
0.0236
4-nitrophenyl-beta-D-fucoside
-
mutant enzyme Q39E/E451A, at 30°C
0.0342
4-nitrophenyl-beta-D-fucoside
-
mutant enzyme Q39E/E451S, at 30°C
0.04 - 1.97
4-nitrophenyl-beta-D-galactopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
0.9
4-nitrophenyl-beta-D-galactopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
9.15
4-nitrophenyl-beta-D-galactopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
9.8
4-nitrophenyl-beta-D-galactopyranoside
in 100 mM sodium acetate, pH 5.0, at 30°C
27
4-nitrophenyl-beta-D-galactopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
67.6
4-nitrophenyl-beta-D-galactopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
82
4-nitrophenyl-beta-D-galactopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
0.000285
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme E451A, at 30°C
0.0006
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme Q39N/E451S, at 30°C
0.00093
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme E451S, at 30°C
0.0036
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme Q39E/E451A, at 30°C
0.0065
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme Q39E/E451S, at 30°C
0.04 - 1.97
4-nitrophenyl-beta-D-glucopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
3.84
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.8, in 50 mM MOPS buffer (pH 6.5), at 30°C
3.84
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.8, in 50 mM MOPS buffer (pH 6.5), at 30°C
5.62
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.6, in 50 mM MOPS buffer (pH 6.5), at 30°C
5.62
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.6, in 50 mM MOPS buffer (pH 6.5), at 30°C
6.4
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.5, 30°C, wild-type enzyme
6.4
4-nitrophenyl-beta-D-glucopyranoside
-
wild type enzyme, in 50 mM MOPS buffer (pH 6.5), at 30°C
9.35
4-nitrophenyl-beta-D-glucopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
20.8
4-nitrophenyl-beta-D-glucopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
26.37
4-nitrophenyl-beta-D-glucopyranoside
-
in 50 mM citrate buffer, pH 4.8, at 50°C
38.9
4-nitrophenyl-beta-D-glucopyranoside
in 100 mM sodium acetate, pH 5.0, at 30°C
42.2
4-nitrophenyl-beta-D-glucopyranoside
-
wild type enzyme, in 50 mM MOPS buffer (pH 6.5), at 30°C
87.93
4-nitrophenyl-beta-D-glucopyranoside
-
in 50 mM citrate buffer, pH 4.8, at 50°C
89
4-nitrophenyl-beta-D-glucopyranoside
-
pH 4.5, 25°C, recombinant wild-type enzyme
95.4
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.5, 30°C, wild-type enzyme
118
4-nitrophenyl-beta-D-glucopyranoside
recombinant enzyme, in 50 mM sodium citrate buffer pH 4.8, at 22°C
141
4-nitrophenyl-beta-D-glucopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
387
4-nitrophenyl-beta-D-glucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
0.384
4-nitrophenyl-beta-D-xylopyranoside
pH 6.5, 30°C, recombinant His-tagged isozyme BGL1A
18.4
4-nitrophenyl-beta-D-xylopyranoside
-
pH 6.5, 30°C, wild-type enzyme
28.9
4-nitrophenyl-beta-D-xylopyranoside
-
pH 6.5, 30°C, wild-type enzyme
0.001
cellobiose
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.13
cellobiose
beta-(1-4)-linked cellobiose,in 100 mM sodium acetate, pH 5.0, at 30°C
7.88
cellobiose
pH not specified in the publication, temperature not specified in the publication
43
cellobiose
recombinant enzyme, in 50 mM sodium citrate buffer pH 4.8, at 22°C
47.3
cellobiose
-
mutant enzyme D501A, in 0.1 M sodium acetate, pH 4.0, at 40°C
67.4
cellobiose
-
wild type enzyme, in 0.1 M sodium acetate, pH 4.0, at 40°C
78.3
cellobiose
-
mutant enzyme D496A, in 0.1 M sodium acetate, pH 4.0, at 40°C
78.4
cellobiose
-
mutant enzyme D463A, in 0.1 M sodium acetate, pH 4.0, at 40°C
87.7
cellobiose
-
mutant enzyme D487A, in 0.1 M sodium acetate, pH 4.0, at 40°C
91
cellobiose
H0HC94
mutant C174V, pH not specified in the publication, temperature not specified in the publication
107
cellobiose
H0HC94
mutant W127F, pH not specified in the publication, temperature not specified in the publication
118
cellobiose
H0HC94
mutant H229S, pH not specified in the publication, temperature not specified in the publication
233
cellobiose
H0HC94
wild-type, pH not specified in the publication, temperature not specified in the publication
324
cellobiose
H0HC94
mutant V176A, pH not specified in the publication, temperature not specified in the publication
328
cellobiose
H0HC94
mutant L178A, pH not specified in the publication, temperature not specified in the publication
354
cellobiose
H0HC94
mutant L178E, pH not specified in the publication, temperature not specified in the publication
1.32
Dhurrin
pH 5.8, 37°C, chimeric mutant (Chim21) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1
2.23
Dhurrin
pH 5.8, 37°C, chimeric mutant (Chim16) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1 (with an extra 22 amino acids substitution)
13.46
Dhurrin
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
13.46
Dhurrin
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
18.68
Dhurrin
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
18.68
Dhurrin
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
22.7
Dhurrin
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
22.7
Dhurrin
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
23.41
Dhurrin
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
23.41
Dhurrin
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
27.17
Dhurrin
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
27.17
Dhurrin
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
31.83
Dhurrin
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
31.83
Dhurrin
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
46.02
Dhurrin
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
46.02
Dhurrin
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
53.96
Dhurrin
-
pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)
53.96
Dhurrin
-
pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)
112.5
Dhurrin
isoform GLU1, at pH 5.5 and 30°C
0.17
gentiobiose
beta-(1-6)-linked gentiobiose, in 100 mM sodium acetate, pH 5.0, at 30°C
6.17
laminaribiose
beta-(1-3)-linked laminaribose,in 100 mM sodium acetate, pH 5.0, at 30°C
13.6
quercetin 3-O-beta-D-glucopyranoside
wild-type, pH 5.6, 80°C
14.4
quercetin 3-O-beta-D-glucopyranoside
mutant F224I, pH 5.6, 80°C
39.8
quercetin 3-O-beta-D-glucopyranoside
mutant N220S, pH 5.6, 80°C
40.8
quercetin 3-O-beta-D-glucopyranoside
mutant N221S, pH 5.6, 80°C
9.8
sophorose
beta-(1-2)-linked sophorose, in 100 mM sodium acetate, pH 5.0, at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
81.6
2,4-dihydroxy-1,4-benzoxazin-3-one glucoside
isoform GLU1, at pH 5.5 and 30°C
9.9
4-methylumbelliferyl beta-D-glucopyranoside
pH 4.0, 60°C
11
4-nitrophenyl-beta-D-mannopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
25.5
oleuropein
isoform GLU1, at pH 5.5 and 30°C
21.2
2,4-dinitrophenyl beta-D-glucoside
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 4.0, at 40°C
22.6
2,4-dinitrophenyl beta-D-glucoside
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 6.0, at 40°C
273
2,4-dinitrophenyl beta-D-glucoside
-
wild type enzyme, in 0.1 M sodium acetate, pH 6.0, at 40°C
863
2,4-dinitrophenyl beta-D-glucoside
-
wild type enzyme, in 0.1 M sodium acetate, pH 4.0, at 40°C
22
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme E206Q
309
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, wild-type enzyme
310
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
435
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, recombinant enzyme
4.2
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 6.0, 65°C
17.2
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 5.0, 65°C
22.43
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
22.43
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
26.46
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
26.46
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
43.91
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
43.91
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
44.75
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
44.75
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
47.24
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
47.24
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
72.9
2-nitrophenyl beta-D-glucopyranoside
mutant E387G, pH 6.5, 65°C, presence of 2 M formate
91
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 4.0, 65°C
147.4
2-nitrophenyl beta-D-glucopyranoside
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, pH 3.0, 65°C
1164
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C, presence of 2 M formate
1575
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C
160
2-Nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
251
2-Nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, wild-type enzyme
3.76
4-nitrophenyl beta-D-cellobioside
pH not specified in the publication, temperature not specified in the publication
14.9
4-nitrophenyl beta-D-fucopyranoside
pH 4.6, 37°C, recombinant enzyme
16.1
4-nitrophenyl beta-D-fucopyranoside
mutant N223Q, pH 5.5, 75°C
29.9
4-nitrophenyl beta-D-fucopyranoside
pH not specified in the publication, temperature not specified in the publication
32.1
4-nitrophenyl beta-D-fucopyranoside
pH 4.6, 37°C, native enzyme
74.5
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, without additive
98.3
4-nitrophenyl beta-D-fucopyranoside
mutant N223Y, pH 5.5, 75°C
115
4-nitrophenyl beta-D-fucopyranoside
wild-type, pH 5.5, 75°C
124
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 250 mM D-glucose
144
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 25 mM cellobiose
181
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 250 mM D-galactose
250.7
4-nitrophenyl beta-D-fucopyranoside
80°C, pH is not specified in the publication, mutant enzyme D206N
342.81
4-nitrophenyl beta-D-fucopyranoside
80°C, pH is not specified in the publication, wild-type
463
4-nitrophenyl beta-D-fucopyranoside
pH 6.0, 60°C, additive: 250 mM D-xylose
382
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
584
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 65°C, wild-type enzyme
698
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 75°C, recombinant enzyme
772
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 75°C, wild-type enzyme
1.83
4-nitrophenyl beta-D-galactopyranoside
mutant N223Q, pH 5.5, 75°C
7
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme E206Q
8.52
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 5.5, 75°C
8.57
4-nitrophenyl beta-D-galactopyranoside
pH 4.6, 37°C, recombinant enzyme
11.5
4-nitrophenyl beta-D-galactopyranoside
pH 4.6, 37°C, native enzyme
12.2
4-nitrophenyl beta-D-galactopyranoside
pH not specified in the publication, temperature not specified in the publication
12.5
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, without additive
14
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 250 mM D-glucose
17.3
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 25 mM cellobiose
20.7
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 250 mM D-galactose
24
4-nitrophenyl beta-D-galactopyranoside
pH 6.0, 60°C, additive: 250 mM D-xylose
24.7
4-nitrophenyl beta-D-galactopyranoside
mutant N223Y, pH 5.5, 75°C
217
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, wild-type enzyme
234
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
299
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, recombinant enzyme
1.61
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme I48W
1.71
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme I48W/I278F/T484Y
2.41
4-nitrophenyl beta-D-glucopyranoside
mutant N223Q, presence of 500 mM D-glucose, pH 5.5, 75°C
3.98
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme I278F
5.53
4-nitrophenyl beta-D-glucopyranoside
mutant N223Q, pH 5.5, 75°C
6.36
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, mutant enzyme T484Y
11.6
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, without Zn2+
15.5
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 1 M glucose, pH not specified in the publication, temperature not specified in the publication
17.9
4-nitrophenyl beta-D-glucopyranoside
pH 4.6, 37°C, recombinant enzyme
22.6
4-nitrophenyl beta-D-glucopyranoside
pH not specified in the publication, temperature not specified in the publication
22.6
4-nitrophenyl beta-D-glucopyranoside
pH 4.6, 37°C, native enzyme
22.7
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 0.25 M glucose, pH not specified in the publication, temperature not specified in the publication
23.3
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 0.5 M glucose, pH not specified in the publication, temperature not specified in the publication
25.2
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, presence of 0.1 M glucose, pH not specified in the publication, temperature not specified in the publication
26.1
4-nitrophenyl beta-D-glucopyranoside
wild-type, presence of 500 mM D-glucose, pH 5.5, 75°C
26.77
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 50°C, wild-type enzyme
27.82
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 60°C, mutant enzyme Y509T
28.5
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant W127F, pH not specified in the publication, temperature not specified in the publication
32.3
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.5, 75°C
36.4
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant C174V, pH not specified in the publication, temperature not specified in the publication
36.4
4-nitrophenyl beta-D-glucopyranoside
mutant N223Y, presence of 500 mM D-glucose, pH 5.5, 75°C
36.9
4-nitrophenyl beta-D-glucopyranoside
80°C, pH is not specified in the publication, mutant enzyme D206N
41.6
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant V176A, pH not specified in the publication, temperature not specified in the publication
43.2
4-nitrophenyl beta-D-glucopyranoside
mutant N223Y, pH 5.5, 75°C
45.4
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant L178E, pH not specified in the publication, temperature not specified in the publication
49.48
4-nitrophenyl beta-D-glucopyranoside
80°C, pH is not specified in the publication, wild-type
61.6
4-nitrophenyl beta-D-glucopyranoside
mutant E458G, pH 5.6, 90°C
63.7
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, without additive
70.4
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant H229S, pH not specified in the publication, temperature not specified in the publication
78.2
4-nitrophenyl beta-D-glucopyranoside
H0HC94
mutant L178A, pH not specified in the publication, temperature not specified in the publication
81.6
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 60°C, wild-type enzyme
88
4-nitrophenyl beta-D-glucopyranoside
mutant D58A, pH 5.6, 90°C
89.9
4-nitrophenyl beta-D-glucopyranoside
H0HC94
wild-type, pH not specified in the publication, temperature not specified in the publication
93
4-nitrophenyl beta-D-glucopyranoside
mutant N221F, pH 5.6, 80°C
96.8
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 250 mM D-glucose
97.88
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
97.88
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
118
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 25 mM cellobiose
129
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 250 mM D-galactose
129
4-nitrophenyl beta-D-glucopyranoside
pH 6.0, 60°C, additive: 250 mM D-xylose
169
4-nitrophenyl beta-D-glucopyranoside
presence of D-glucose, pH 6.0, 50°C
173
4-nitrophenyl beta-D-glucopyranoside
mutant D58A, pH 5.6, 90°C, 0.1 M NaN3
196.4
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
196.4
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
216.4
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
216.4
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
242.6
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
242.6
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
273
4-nitrophenyl beta-D-glucopyranoside
mutant E458G, pH 5.6, 90°C, 0.1 M NaN3
276.7
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
276.7
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.8, 25°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
282
4-nitrophenyl beta-D-glucopyranoside
mutant W322A, pH 5.6, 80°C
435
4-nitrophenyl beta-D-glucopyranoside
mutant D242G, pH 5.6, 90°C, 0.1 M NaN3
446
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.6, 90°C, 0.1 M NaN3
996
4-nitrophenyl beta-D-glucopyranoside
mutant W243F, pH 5.6, 90°C
1247
4-nitrophenyl beta-D-glucopyranoside
mutant F224I, pH 5.6, 80°C
1557
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 60°C
2000
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.6, 80°C
2002
4-nitrophenyl beta-D-glucopyranoside
wild-type, pH 5.6, 90°C
2144
4-nitrophenyl beta-D-glucopyranoside
mutant F310L, pH 5.6, 80°C
2433
4-nitrophenyl beta-D-glucopyranoside
mutant N220S, pH 5.6, 80°C
2714
4-nitrophenyl beta-D-glucopyranoside
mutant F310E, pH 5.6, 80°C
2724
4-nitrophenyl beta-D-glucopyranoside
mutant N221S, pH 5.6, 80°C
2857
4-nitrophenyl beta-D-glucopyranoside
mutant N220F, pH 5.6, 80°C
0.03
4-nitrophenyl beta-D-glucoside
-
pH 5.0, 95°C, mutant enzyme M424K/F426Y
0.05
4-nitrophenyl beta-D-glucoside
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 4.0, at 40°C
87.5
4-nitrophenyl beta-D-glucoside
-
free enzyme, at pH 5.0 and 37°C
107
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D501A, in 0.1 M sodium acetate, pH 4.0, at 40°C
132
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
249
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D463A, in 0.1 M sodium acetate, pH 4.0, at 40°C
263
4-nitrophenyl beta-D-glucoside
-
wild type enzyme, in 0.1 M sodium acetate, pH 4.0, at 40°C
297
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D487A, in 0.1 M sodium acetate, pH 4.0, at 40°C
321
4-nitrophenyl beta-D-glucoside
-
mutant enzyme D496A, in 0.1 M sodium acetate, pH 4.0, at 40°C
566.3
4-nitrophenyl beta-D-glucoside
-
immobilized enzyme, at pH 5.0 and 37°C
830
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, wild-type enzyme
1004
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 75°C, recombinant enzyme
1084
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 75°C, wild-type enzyme
47.21
4-nitrophenyl beta-D-mannopyranoside
80°C, pH is not specified in the publication, wild-type
51.72
4-nitrophenyl beta-D-mannopyranoside
80°C, pH is not specified in the publication, mutant enzyme D206N
1446
4-nitrophenyl cellobioside
-
pH 6.5, 75°C, recombinant enzyme
67
4-nitrophenyl-beta-D-fucopyranoside
in 100 mM sodium acetate, pH 5.0, at 30°C
1068
4-nitrophenyl-beta-D-fucopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
1185
4-nitrophenyl-beta-D-fucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
0.00018
4-nitrophenyl-beta-D-fucoside
-
mutant enzyme Q39N/E451S, at 30°C
0.0087
4-nitrophenyl-beta-D-fucoside
-
mutant enzyme Q39E/E451A, at 30°C
0.014
4-nitrophenyl-beta-D-fucoside
-
mutant enzyme Q39E/E451S, at 30°C
1.6
4-nitrophenyl-beta-D-galactopyranoside
in 100 mM sodium acetate, pH 5.0, at 30°C
18
4-nitrophenyl-beta-D-galactopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
42
4-nitrophenyl-beta-D-galactopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
0.00053
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme E451S, at 30°C
0.00057
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme E451A, at 30°C
0.005
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme Q39N/E451S, at 30°C
0.016
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme Q39E/E451A, at 30°C
0.017
4-nitrophenyl-beta-D-galactoside
-
mutant enzyme Q39E/E451S, at 30°C
6.2
4-nitrophenyl-beta-D-glucopyranoside
in 100 mM sodium acetate, pH 5.0, at 30°C
95.9
4-nitrophenyl-beta-D-glucopyranoside
-
wild type enzyme, in 50 mM MOPS buffer (pH 6.5), at 30°C
381
4-nitrophenyl-beta-D-glucopyranoside
in 100 mM citrate/phosphate buffer, at pH 6.0 and 90°C
468
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.6, in 50 mM MOPS buffer (pH 6.5), at 30°C
468
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.6, in 50 mM MOPS buffer (pH 6.5), at 30°C
468
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.8, in 50 mM MOPS buffer (pH 6.5), at 30°C
468
4-nitrophenyl-beta-D-glucopyranoside
-
chimeric beta-glucosidase No.8, in 50 mM MOPS buffer (pH 6.5), at 30°C
579
4-nitrophenyl-beta-D-glucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
1640
4-nitrophenyl-beta-D-glucopyranoside
-
wild type enzyme, in 50 mM MOPS buffer (pH 6.5), at 30°C
240.5
4-nitrophenyl-beta-D-glucoside
-
in 100 mM acetate buffer, pH 5.0, at 37°C
0.001
cellobiose
-
mutant enzyme E490A, in 0.1 M sodium acetate, pH 4.0, at 40°C
0.0085
cellobiose
beta-(1-4)-linked cellobiose, in 100 mM sodium acetate, pH 5.0, at 30°C
10.2
cellobiose
pH not specified in the publication, temperature not specified in the publication
10.5
cellobiose
H0HC94
mutant W127F, pH not specified in the publication, temperature not specified in the publication
11.1
cellobiose
pH 5.5, 60°C, wild-type enzyme
14.5
cellobiose
H0HC94
mutant V176A, pH not specified in the publication, temperature not specified in the publication
21.4
cellobiose
H0HC94
mutant H229S, pH not specified in the publication, temperature not specified in the publication
28.3
cellobiose
H0HC94
mutant L178E, pH not specified in the publication, temperature not specified in the publication
34.7
cellobiose
-
mutant enzyme D501A, in 0.1 M sodium acetate, pH 4.0, at 40°C
39.7
cellobiose
H0HC94
mutant L178A, pH not specified in the publication, temperature not specified in the publication
49.4
cellobiose
H0HC94
mutant C174V, pH not specified in the publication, temperature not specified in the publication
60.6
cellobiose
-
wild type enzyme, in 0.1 M sodium acetate, pH 4.0, at 40°C
78.7
cellobiose
-
mutant enzyme D463A, in 0.1 M sodium acetate, pH 4.0, at 40°C
79.3
cellobiose
H0HC94
wild-type, pH not specified in the publication, temperature not specified in the publication
85.2
cellobiose
-
mutant enzyme D487A, in 0.1 M sodium acetate, pH 4.0, at 40°C
138
cellobiose
-
mutant enzyme D496A, in 0.1 M sodium acetate, pH 4.0, at 40°C
26.1
Dhurrin
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
26.1
Dhurrin
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
59
Dhurrin
isoform GLU1, at pH 5.5 and 30°C
62.4
Dhurrin
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
62.4
Dhurrin
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
124
Dhurrin
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
124
Dhurrin
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
150
Dhurrin
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
150
Dhurrin
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
195
Dhurrin
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
195
Dhurrin
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
303.1
Dhurrin
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
303.1
Dhurrin
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
494.8
Dhurrin
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
494.8
Dhurrin
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
1349
Dhurrin
-
pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)
1349
Dhurrin
-
pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)
0.011
gentiobiose
beta-(1-6)-linked gentiobiose, in 100 mM sodium acetate, pH 5.0, at 30°C
1.7
laminaribiose
beta-(1-3)-linked laminaribose, in 100 mM sodium acetate, pH 5.0, at 30°C
95
quercetin 3-O-beta-D-glucopyranoside
mutant F224I, pH 5.6, 80°C
101
quercetin 3-O-beta-D-glucopyranoside
wild-type, pH 5.6, 80°C
428
quercetin 3-O-beta-D-glucopyranoside
mutant N220S, pH 5.6, 80°C
446
quercetin 3-O-beta-D-glucopyranoside
mutant N221S, pH 5.6, 80°C
0.96
sophorose
beta-(1-2)-linked sophorose, in 100 mM sodium acetate, pH 5.0, at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
(1S,5S)-3-methylidene-6,8-bis[(1S)-1-phenylethyl]-6,8-diazabicyclo[3.2.2]nonane-7,9-dione
-
-
0.00515
(2R,3R,4R,5S)-1-butyl-2-(hydroxymethyl)piperidine-3,4,5-triol
pH 4.0, 60°C
0.58
(2S,5S)-2-benzyl-3,11-bis[(1S)-1-phenylethyl]-2,3,5,6-tetrahydro-5,2-(epiminomethano)-3-benzazocine-4,12(1H)-dione
-
-
2.2
(2S,5S)-2-methyl-3,11-bis[(1S)-1-phenylethyl]-2,3,5,6-tetrahydro-5,2-(epiminomethano)-3-benzazocine-4,12(1H)-dione
-
-
0.535
(2S,5S)-3,11-bis[(1S)-1-phenylethyl]-2,3,5,6-tetrahydro-5,2-(epiminomethano)-3-benzazocine-4,12(1H)-dione
-
-
0.41
2-nitrophenyl-beta-D-fucopyranoside
-
pH 7.3, 40°C, versus substrate 4-nitrophenyl beta-D-glucopyranoside
17.9
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.0064
4-[4-(cyanomethoxy)phenyl]-4-oxo-N-{3-[(2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl]propyl}butanamide
-
-
330
D-glucoheptose
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
130
D-glucuronamide
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
1.4
decyl-beta-D-glucopyranoside
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
0.004
deoxynojirimycin
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
5.9
heptyl-beta-D-glucopyranoside
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
9.8
hexyl-beta-D-glucopyranoside
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
440
myo-inositol
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
0.0013
N-{3-[4-(cyanomethoxy)benzoyl]benzoyl}propylamido-1-deoxynojirimycin
-
-
1.7
nonyl-beta-D-glucopyranoside
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
0.4
p-nitrophenyl-beta-D-glucopyranoside
-
vs. cellobiose, 30°C, pH 6.0
18
pentyl-beta-D-glucopyranoside
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
additional information
additional information
-
substrate inhibition kinetics of wild-type and mutant enzymes, overview
-
0.058
3,8-dibutylamino-7,8-dideoxy-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.223
3,8-dibutylamino-7,8-dideoxy-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.025
7,8-dideoxy-3,8-didodecylamino-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.367
7,8-dideoxy-3,8-didodecylamino-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.012
7,8-dideoxy-3,8-dioctylamino-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.441
7,8-dideoxy-3,8-dioctylamino-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.0096
7,8-dideoxy-3-hydroxy-8-octylamino-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.484
7,8-dideoxy-3-hydroxy-8-octylamino-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.0029
7,8-dideoxy-8-dodecylamino-3-hydroxy-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.056
7,8-dideoxy-8-dodecylamino-3-hydroxy-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.051
8-butylamino-7,8-dideoxy-3-hydroxy-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
0.32
8-butylamino-7,8-dideoxy-3-hydroxy-5-octylimino-6-oxa-3-epi-australine
-
pH and temperature not specified in the publication
1.8
cellobiose
-
pH 4.5, 25°C, recombinant wild-type enzyme and mutant W49A
2.8
cellobiose
-
vs. p-nitrophenyl-beta-D-glucopyranoside, 30°C, pH 6.0
0.56
cellopentaose
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
0.29
cellotetraose
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
0.85
cellotriose
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
370
D-galactose
-
versus 2-nitrophenyl-beta-D-galactopyranoside, pH 6.5, 40°C
0.012
D-glucono-delta-lactone
recombinant enzyme, using cellobiose as substrate, in 50 mM sodium citrate buffer pH 4.8, at 22°C
0.1
D-glucono-delta-lactone
recombinant enzyme, using 4-nitrophenyl-beta-D-glucopyranoside as substrate, in 50 mM sodium citrate buffer pH 4.8, at 22°C
0.41
D-glucose
-
pH 7.3, 40°C, versus substrate 4-nitrophenyl beta-D-glucopyranoside
1.1
D-glucose
recombinant enzyme, using cellobiose as substrate, in 50 mM sodium citrate buffer pH 4.8, at 22°C
2 - 5
D-glucose
pH 5.5, 60°C, with 4-nitrophenyl beta-D-glucopyranoside as substrate, wild-type enzyme
2.3
D-glucose
recombinant enzyme, using 4-nitrophenyl-beta-D-glucopyranoside as substrate, in 50 mM sodium citrate buffer pH 4.8, at 22°C
2.7
D-glucose
-
using 4-nitrophenyl-beta-D-glucopyranoside as substrate, in 50 mM citrate buffer, pH 4.8, at 50°C
3.25
D-glucose
-
using 4-nitrophenyl-beta-D-glucopyranoside as substrate, in 50 mM citrate buffer, pH 4.8, at 50°C
3.4
D-glucose
-
using cellobiose as substrate, in 50 mM citrate buffer, pH 4.8, at 50°C
17.6
D-glucose
EU918770
substrate 4-nitrophenyl beta-D-glucopyranoside, pH 5.0, 55°C
37.1
D-glucose
pH 5.5, 55°C, with 4-nitrophenyl beta-D-glucopyranoside as substrate
39.5
D-glucose
-
pH and temperature not specified in the publication
55.2
D-glucose
pH 6.0, 50°C, with 4-nitrophenyl beta-D-glucopyranoside as substrat, wild-type enzyme
66
D-glucose
-
versus 2-nitrophenyl-beta-D-galactopyranoside, pH 6.5, 40°C
518
D-glucose
H0HC94
mutant V176A, pH not specified in the publication, temperature not specified in the publication
558
D-glucose
H0HC94
mutant L178E, pH not specified in the publication, temperature not specified in the publication
558
D-glucose
H0HC94
mutant W127F, pH not specified in the publication, temperature not specified in the publication
666
D-glucose
H0HC94
mutant L178A, pH not specified in the publication, temperature not specified in the publication
686
D-glucose
H0HC94
wild-type, pH not specified in the publication, temperature not specified in the publication
0.03
delta-gluconolactone
-
vs. p-nitrophenyl-beta-D-glucopyranoside,30°C, pH 6.0
2.2
delta-gluconolactone
hydrolysis of p-nitrophenyl-beta-D-glucopyranoside
23
glucono-delta-lactone
-
40°C, pH 6.0, vs. genistein-7-O-beta-D-glucopyranoside
0.07
gluconolactone
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
2
gluconolactone
with para-nitrophenyl-beta-D-glucopyranoside as substrate
2.2
gluconolactone
with ortho-nitrophenyl-beta-D-glucopyranoside as substrate
4.7
gluconolactone
with 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
3.1
octyl-beta-D-glucopyranoside
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
4
octyl-beta-D-glucopyranoside
-
vs. 4-methylumbelliferyl-beta-D-glucopyranoside, 30°C, pH 6.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000055
7-(N-benzoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.0014
7-(N-benzoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.02
7-(N-benzoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.0003
7-(N-butylsulfonyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.0003
7-(N-butylsulfonyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.0025
7-(N-butylsulfonyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.00007
7-(N-pentoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.0002
7-(N-pentoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.0005
7-(N-pentoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.000017
7-pentylcyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.0007
7-pentylcyclophellitol aziridine
Homo sapiens
-
isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.0007
7-pentylcyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.00035
cyclophellitol
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.002
cyclophellitol
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.1
cyclophellitol
Homo sapiens
-
IC50 above 0.1 mM, isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.0004
cyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.0005
cyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.1
cyclophellitol aziridine
Homo sapiens
-
IC50 above 0.1 mM, isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.1
cyclophellitol thiirane
Homo sapiens
-
IC50 above 0.1 mM, GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.1
cyclophellitol thiirane
Homo sapiens
-
IC50 above 0.1 mM, isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.1
cyclophellitol thiirane
Homo sapiens
-
IC50 above 0.1 mM, isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.16
D-glucono-1,5-lactone
Physarum polycephalum
-
pH 4.5, 37°C, both 13000 Da and 230000 Da form
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.002
isoform GLU2, with phloridzin as substrate, at pH 5.5 and 30°C
0.0039
-
substrate: 2-nitrophenyl-beta-D-galactopyranoside, 70°C, pH 5.5
0.005
isoform GLU4, with 2,4-dihydroxy-1,4-benzoxazin-3-one glucoside as substrate, at pH 5.5 and 30°C
0.013
isoform GLU1, with trans-zeatin-O-glucoside as substrate, at pH 5.5 and 30°C
0.05
0.053
isoform GLU2, with daidzin as substrate, at pH 5.5 and 30°C
0.065
isoform GLU1, with phloridzin as substrate, at pH 5.5 and 30°C
0.071
isoform GLU1, with geniposide as substrate, at pH 5.5 and 30°C
0.077
isoform GLU4, with oleuropein as substrate, at pH 5.5 and 30°C
0.078
isoform GLU4, with genistin as substrate, at pH 5.5 and 30°C
0.086
isoform GLU2, with 2,4-dihydroxy-1,4-benzoxazin-3-one glucoside as substrate, at pH 5.5 and 30°C
0.09
0.1
0.104
0.14
0.149
isoform GLU4, with daidzin as substrate, at pH 5.5 and 30°C
0.17
0.28
after 163fold purification, using 2-nitrophenyl-beta-D-galactopyranoside as substrate, at 70°C
0.283
isoform GLU1, with 4-nitrophenyl beta-D-cellobioside as substrate, at pH 5.5 and 30°C
0.29
-
crude extract, using 4-nitrophenyl-beta-D-glucopyranoside substrate, at 37°C
0.291
0.3
after 163fold purification, using 2-nitrophenyl-beta-D-glucopyranoside as substrate, at 70°C
0.32
after 163fold purification, using 4-nitrophenyl-beta-D-xylopyranoside as substrate, at 70°C
0.34
isoform GLU4, with dhurrin as substrate, at pH 5.5 and 30°C
0.39
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, substrate cellobiose, pH 3.0, 65°C
0.472
isoform GLU2, with 4-nitrophenyl beta-D-glucopyranoside as substrate, at pH 5.5 and 30°C
0.54
-
purified enzyme, using 4-nitrophenyl.beta-D-glucopyranoside as substrate
0.58
isoform GLU2, with oleuropein as substrate, at pH 5.5 and 30°C
0.6
pH 5.5, 95°C, substrate: 4-nitrophenyl-alpha-L-rhamnopyranoside
0.69
0.7
0.75
after 163fold purification, using 4-nitrophenyl-beta-D-lactopyranoside as substrate, at 70°C
0.9
0.949
isoform GLU2, with dhurrin as substrate, at pH 5.5 and 30°C
0.95
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 6.0, 50°C, mutant enzyme I48W
1
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 6.0, 50°C, mutant enzyme I48W/I278F/T484Y
1.2
crude extract, using 4-nitrophenyl-beta-D-glucopyranoside as substrate, at pH 6.0 and 90°C
1.3
after 163fold purification, using 4-nitrophenyl-beta-D-cellobioside as substrate, at 70°C
1.4
1.7
after 68fold purification, using 2-nitrophenyl-beta-D-fucopyranoside as substrate, at pH 6.0 and 90°C
1.8
1.933
isoform GLU1, with genistin as substrate, at pH 5.5 and 30°C
10.4
wild-type, substrate 2-nitrophenyl beta-D-xylopyranoside, pH 3.0, 65°C
10.8
after 163fold purification, using cellotetraose as substrate, at 70°C
100
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
103
-
substrate 4-nitrophenyl beta-D-glucopyranoside, pH 4.8, 60°C, isoform beta-glu 2
103.4
substrate: gentiobiose, pH 5.5, 60°C, wild-type enzyme
105
-
using 4-nitrophenyl-beta-D-glucopyranoside as substrate, at pH 5.0 and 40°C
11.34
-
in cell-free extract for laminaribiose, maximum rate of all substrates tested
113
after 68fold purification, using 4-nitrophenyl-beta-D-fucopyranoside as substrate, at pH 6.0 and 90°C
117
118
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
119
substrate beta-D-glucopyranoside, pH not specified in the publication, temperature not specified in the publication
12
122
127
129
substrate laminaritetraose, pH not specified in the publication, temperature not specified in the publication
129.8
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
13
13.8
-
purified recombinant, substrate 4-nitrophenyl-beta-D-glucopyranoside
1300
pH 5.5, 95°C, substrate: 4-nitrophenyl-beta-D-glucopyranoside
131
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
133
14
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
14.1
-
partially purified mutant enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside
14.7
after 163fold purification, using 4-nitrophenyl-beta-D-fucopyranoside as substrate, at 70°C
140.9
wild-type, substrate 2-nitrophenyl beta-D-galactopyranoside, pH 3.0, 65°C
14000
purified recombinant enzyme, substrate 4-nitrophenyl-beta-D-galactopyranoside, pH 7.0, 90°C
151
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
1520
purified recombinant enzyme, substrate 4-nitrophenyl-beta-D-xylopyranoside, pH 7.0, 90°C
154
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
158.8
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 5.5, 60°C
16.2
after 163fold purification, using cellobiose as substrate, at 70°C
160
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Phoma aff. glomerata, GenBank Accession: HQ630999
169
17
17.9
-
purified enzyme, using 4-nitrophenyl-beta-D-glucopyranoside as substrate, in 0.1 M NaOAc buffer, pH 5.0, at 45°C
170
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
170.5
-
purified enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside
173
-
substrate 4-nitrophenyl beta-D-glucopyranoside, pH 4.8, 60°C, isoform beta-glu 2
175
substrate cellobiose, pH not specified in the publication, temperature not specified in the publication
176
-
purified enzyme, substrate 4-nitrophenyl beta-D-glucopyranoside, 60°C
178
18
185
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
187
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
189
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
19
19.9
substrate 4-nitrophenyl beta-D-galactopyranoside, presence of D-glucose, pH 6.0, 50°C
194
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
2.1
purified enzyme, substrate 4-nitrophenyl-alpha-L-arabinoopyranoside, recombinant wild-type enzyme
2.27
-
partially purified wild-type enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside
2.3
purified recombinant enzyme, substrate cellobiose, pH 7.0, 90°C
2.436
isoform GLU1, with daidzin as substrate, at pH 5.5 and 30°C
2.68
2.95
-
crude extract, at 50°C, in 50 mM sodium phosphate buffer, pH 6.0, using 4-nitrophenyl-beta-D-glucopyranoside as substrate
20
202.3
-
hydrolysis of 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one-beta-D-glucoside
204
H0HC94
wild-type, substrate cellobiose, pH not specified in the publication, temperature not specified in the publication
207.1
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
2088
-
purified enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside, pH 5.0, 65°C
21
211
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
212
substrate laminaribiose, pH not specified in the publication, temperature not specified in the publication
214
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
22
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
22.3
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 5.5, 60°C, mutant enzyme Y509T
226
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
229
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
23
230
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
24
24.36
-
after 57.5fold purification, in 50 mM sodium acetate, pH 5.5, at 37°C
248
25
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
25.7
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 6.0, 60°C
250
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
266.9
268
substrate gentiobiose, pH not specified in the publication, temperature not specified in the publication
27
27.2
substrate: 4-nitrophenyl beta-D-fucopyranoside, pH 6.0, 60°C
274
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
28
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
284
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
29
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
290
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
29200
purified recombinant enzyme, substrate 4-nitrophenyl-beta-D-fucopyranoside, pH 7.0, 90°C
3 - 8
3.36
substrate: sophorose, pH 6.0, 50°C, mutant enzyme I48W/I278F/T484Y
3.5
3.59
substrate: sophorose, pH 6.0, 50°C, mutant enzyme I278F
3.6
purified enzyme, substrate 4-nitrophenyl-beta-D-fucopyranoside, recombinant wild-type enzyme
3.7
substrate: sophorose, pH 6.0, 50°C, mutant enzyme I48W
3.73
-
tuberonic acid beta-D-glucoside as substrate, 4300fold purified protein, pH 4.0, 37°C
30
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
30400
purified recombinant enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside, pH 7.0, 90°C
309
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
31
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
31.6
311.9
purified recombinant His-tagged isozyme TaGlu1a
315
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Phoma aff. glomerata, GenBank Accession: HQ630999
32
32.39
-
after 11fold purification, at 50°C, in 50 mM sodium phosphate buffer, pH 6.0, using 4-nitrophenyl-beta-D-glucopyranoside as substrate
320
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
327
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
33
333
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
334
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
335
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
336
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
34
34.083
isoform GLU1, with 2,4-dihydroxy-1,4-benzoxazin-3-one glucoside as substrate, at pH 5.5 and 30°C
342
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
343
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
348
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
35
350
359
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
36
36.2
substrate: 4-nitrophenyl beta-D-galactopyranoside, pH 6.0, 60°C
36.3
substrate: substrate: cellobiose, pH 5.5, 60°C, wild-type enzyme
36.4
substrate 4-nitrophenyl beta-D-glucopyranoside, presence of D-glucose, pH 6.0, 50°C
364
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
376
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
379
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
383
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
387
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
39
39.4
substrate 4-nitrophenyl beta-D-glucopyranoside, enzyme expression induced by growth on rice bran hemicellulose
4.15
substrate: 4-nitrophenyl beta-D-xylopyranoside, pH 6.0, 60°C
4.46
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 6.0, 50°C, mutant enzyme T484Y
4.53
4.9
after 68fold purification, using 4-nitrophenyl-beta-D-mannopyranoside as substrate, at pH 6.0 and 90°C
405
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
406
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Phoma aff. glomerata, GenBank Accession: HQ630999
41.8
purified enzyme, substrate apigenin-7-glucoside, recombinant wild-type enzyme
427
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
43
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
44
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
440
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
45
454
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Phoma aff. glomerata, GenBank Accession: HQ630999
46
46.2
-
purified enzyme, pH 5.0, 50°C, substrate 4-nitrophenyl-beta-D-glucopyranoside
48
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
488
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
49.7
purified enzyme, substrate quercetin-4'-glucoside, recombinant wild-type enzyme
493
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
494
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
5.55
5.64
substrate: sophorose, pH 6.0, 50°C, mutant enzyme T484Y
5.7
purified enzyme, substrate 4-nitrophenyl-beta-D-galactopyranoside, recombinant wild-type enzyme
5.814
isoform GLU4, with 4-nitrophenyl beta-D-glucopyranoside as substrate, at pH 5.5 and 30°C
50
500
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
51
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
52
54
55
553
purified recombinant enzyme, substrate 4-nitrophenyl beta-D-glucopyranoside
56
569
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
57.14
-
crude filtrate, using 4-nitrophenyl-beta-D-glucopyranoside as substrate, in 0.1 M NaOAc buffer, pH 5.0, at 45°C
57.5
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 5.5, 60°C, wild-type enzyme
577
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
59
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
6.1
after 163fold purification, using 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 70°C
6.3
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, substrate 2-nitrophenyl beta-D-galactopyranoside, pH 3.0, 65°C
6.4
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, substrate 2-nitrophenyl beta-D-xylopyranoside, pH 3.0, 65°C
6.8
61.7
wild-type, substrate 4-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
63
642
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
672
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
68
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
7.139
isoform GLU1, with dhurrin as substrate, at pH 5.5 and 30°C
7.6
7.967
isoform GLU1, with oleuropein as substrate, at pH 5.5 and 30°C
70
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
70.9
-
after 244fold purification, using 4-nitrophenyl -beta-D-glucopyranoside substrate, as at 37°C
717
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
72.2
wild-type, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
73
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
739
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
75
77.86
-
purified enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside
79
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
8.5
after 68fold purification, using 4-nitrophenyl-beta-D-galactopyranoside as substrate, at pH 6.0 and 90°C
8.66
isoform GLU1, with 4-nitrophenyl beta-D-glucopyranoside as substrate, at pH 5.5 and 30°C
81
813
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
82
after 68fold purification, using 4-nitrophenyl-beta-D-glucopyranoside as substrate, at pH 6.0 and 90°C
83
-
using 4-nitrophenyl-beta-D-glucopyranoside as substrate, at pH 5.0 and 40°C
84
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
89
9.4
-
after 244fold purification, using 4-nitrophenyl-beta-D-cellobioside substrate, as at 37°C
9.5
9.65
90
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
94
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
94.6
substrate: sophorose, pH 5.5, 60°C, wild-type enzyme
9400
purified recombinant enzyme, substrate 4-nitrophenyl-beta-D-cellobioside, pH 7.0, 90°C
95
97.2
-
purified enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside
97.7
substrate 4-nitrophenyl beta-D-glucopyranoside, pH 5.0, 50°C
additional information
0.09
-
purified enzyme, using methyl beta-D-glucopyranoside as substrate
0.1
-
after 244fold purification, using 4-nitrophenyl-beta-D-glalactopyranoside substrate, as at 37°C
0.104
isoform GLU2, with 4-nitrophenyl beta-D-fucopyranoside as substrate, at pH 5.5 and 30°C
0.104
isoform GLU4, with 4-nitrophenyl beta-D-fucopyranoside as substrate, at pH 5.5 and 30°C
0.291
isoform GLU2, with 4-nitrophenyl beta-D-cellobioside as substrate, at pH 5.5 and 30°C
0.291
isoform GLU4, with 4-nitrophenyl beta-D-cellobioside as substrate, at pH 5.5 and 30°C
0.7
-
substrate 4-nitrophenyl alpha-D-arabinopyranoside, pH 6.5, 60°C
0.7
after 68fold purification, using 2-nitrophenyl-beta-D-galactopyranoside as substrate, at pH 6.0 and 90°C
1.4
substrate 4-nitrophenyl beta-D-xylopyranoside, presence of D-glucose, pH 6.0, 50°C
1.8
-
substrate 4-nitrophenyl beta-D-galactopyranoside, pH 6.5, 60°C
1.8
after 68fold purification, using 2-nitrophenyl-beta-D-glucopyranoside as substrate, at pH 6.0 and 90°C
117
substrate laminaritriose, pH not specified in the publication, temperature not specified in the publication
12
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
12
mutant N62Y/Q63K/L231F/V303A/E386G/A412V, substrate 4-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
122
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
122
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
13
after 163fold purification, using 4-nitrophenyl-beta-D-glucopyranoside as substrate, at 70°C
133
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
169
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
17
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
178
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
18
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
19
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
2.68
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 6.0, 50°C, mutant enzyme I278F
2.68
substrate: 4-nitrophenyl alpha-D-glucopyranoside, pH 6.0, 60°C
20
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
23
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
24
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
24
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
248
H0HC94
wild-type, substrate 4-nitrophenyl beta-D-glucopyranoside, pH not specified in the publication, temperature not specified in the publication
248
-
substrate 4-nitrophenyl beta-D-glucopyranoside, pH 7.0, 40°C
27
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
27
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
3 - 8
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
3 - 8
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
3.5
purified enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside, recombinant wild-type enzyme
3.5
-
after 244fold purification, using 4-nitrophenyl-alpha-L-arabinopyranoside substrate, as at 37°C
31.6
substrate: 4-nitrophenyl beta-D-glucopyranoside, pH 6.0, 50°C, wild-type enzyme
32
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
32
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
33
-
after 244fold purification, using 4-nitrophenyl-beta-D-xylopyranoside substrate, as at 37°C
34
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
34
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
350
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
36
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
39
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
4.53
-
chimeric beta-glucosidase No.8, after 32.35fold purification, at 30°C
4.53
-
chimeric beta-glucosidase No.8, after 32.35fold purification, at 30°C
45
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
45
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
46
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
46
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
5.55
-
chimeric beta-glucosidase No.6, after 32.65fold purification, at 30°C
5.55
-
chimeric beta-glucosidase No.6, after 32.65fold purification, at 30°C
50
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
50
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
54
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
6.8
after 163fold purification, using cellopentaose as substrate, at 70°C
63
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
63
-
using 4-nitrophenyl-beta-D-glucopyranoside as substrate, at pH 5.0 and 40°C
75
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
75
wild-type, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
81
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
9.5
after 163fold purification, using cellotriose as substrate, at 70°C
95
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
95
-
37°C, pH 5.0, release of 4-nitrophenol from 4-nitrophenyl beta-D-glucopyranoside, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
additional information
-
substrate specificity of wild-type and chimeric mutant enzymes, overview
additional information
-
comparison of enzyme activity in isolated Saccharomyces cerevisiae strains from wines and musts with activity of the purified enzyme from commercial preparation of Aspergillus niger
additional information
-
the enzyme has a specific activity of 1096438 unots/mg after 53fold purification, at 50°C
additional information
-
detection of enzyme activity and concentration of isoflavone aglycones during fermentation of soymilk, overview
additional information
-
determination of the anthocyanin content of fruits at different stages of ripening, overview
additional information
-
comparison of enzyme activity in isolated strains from wines and musts with activity of a commercial preparation from Aspergillus niger
additional information
substrate specificity of wild-type and mutant enzymes, overview
additional information
-
substrate specificity of wild-type and mutant enzymes, overview
additional information
-
detection of enzyme activity and concentration of isoflavone aglycones during fermentation of soymilk, overview
additional information
-
detection of enzyme activity and concentration of isoflavone aglycones during fermentation of soymilk, overview
additional information
-
assay described, enzyme activity measured in homogenates of 10 to 15 male and female flies before and after sucrose meals, monitoring by spectroscopy, values of relative activity shown, more activity produced by flies of the arid region than of those originating in sugar-rich environments, activity in desert females (Jordan Valley autumn line) decreased by 30.5% but increased in desert males by 14.7%
additional information
-
comparison of enzyme activity in isolated strains from wines and musts with activity of a commercial preparation from Aspergillus niger
additional information
-
enzyme activity in different wine varieties, overview
additional information
-
substrate specificity of wild-type and chimeric mutant enzymes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
4 - 4.5
4 - 5
4.2
4.5
4.5 - 5
4.5 - 5.5
4.6
4.8
5 - 5.5
5 - 6
5 - 7
5.2
5.4
5.5
5.6
5.8
6 - 6.5
6 - 7
6.2
6.4
6.5
6.6
6.6 - 7
6.7
6.8
7.2
3
-
the optimum pH of No. 6 chimeric beta-glucosidase is 3.0 in formate buffer, showing varying maximum activity according to the buffer used
3
-
the optimum pH of No. 6 chimeric beta-glucosidase is 3.0 in formate buffer, showing varying maximum activity according to the buffer used
4
-
incubation at pH 4.0 leads to 104.2% relative activity compared to the activity at pH 6.0
4.8
-
for non-immobilized and immobilized enzyme preparations
5
-
the optimum pH of No. 6 chimeric beta-glucosidase is 5.0 in succinate buffer, showing varying maximum activity according to the buffer used
5
-
the optimum pH of No. 6 chimeric beta-glucosidase is 5.0 in succinate buffer, showing varying maximum activity according to the buffer used
5
optimal pH-value of native enzyme and of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde
5 - 5.5
with 4-nitrophenyl beta-D-glucopyranoside as substrate
5.5
with 4-nitrophenyl beta-D-glucopyranoside as substrate
6
with 4-nitrophenyl beta-D-glucopyranoside as substrate
6
the maximum activity of BglA at 75°C is initially at pH 4.5 but after 1 h at 75°C is at pH 6.0
6.5
wild-type BGL1A, and mutants M177L, H231D, and K253A
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 6
-
approx. 35% of maximal activity at pH 2.5, approx. 50% of maximal activity at pH 6.0
2.6 - 7.8
-
approx. 50% of maximal activity at pH 3.5, approx. 60% of maximal activity at pH 7.8
2.8 - 6.8
-
approx. 30% of maximal activity at pH 3.5 and pH 6.8, respectively
3 - 4
-
rapid decrease in activity below pH 3.0 and above pH 4.0
3 - 5
3 - 6
3 - 7
3 - 7.5
3 - 8
3 - 9
3.5 - 7
-
pH 3.5: about 35% of maximal activity, pH 7.0: about 50% of maximal activity
3.5 - 8
3.5 - 8.5
-
approx. 60% of maxim activity at pH 4.0, approx. 70% of maximal activity at pH 8.0
4 - 10
4 - 6
4 - 7
4 - 8
4 - 8.5
4 - 9
4.5 - 6
pH 4.5: about 85% of maximal activity, pH 6.0: about 65% of maximal activity, native enzyme
4.5 - 6.5
4.5 - 8
5 - 10
5 - 6.5
5 - 7
5 - 7.5
5 - 9
5.5 - 7.5
7 - 8.5
more than 80% of maximum activity
3 - 5
pH 3.0: about 50% of maximal activity, pH 5.0: about 80% of maximal activity
3 - 5
pH 3.0: about 65% of maximal activity, pH 5.0: about 70% of maximal activity, beta-glucosidase TpBGL3
3 - 6
-
increase in activity until pH 5.5, sharp drop in activity above pH 6.0
3 - 6
-
approx. 70% of maximal activity at pH 3.0, approx. 5% of maximal activity at pH 6.0
3 - 7
-
approx. 20% of maximal activity at pH 3.0, approx. 10% of maximal activity at pH 7.0
3 - 7
-
approx. 30% of maximal activity at pH 3.0 and 65°C, approx. 5% of maximal activity at pH 6.0 and 65°C
3 - 7
-
approx. 20% of maximal activity at pH 3.0, approx. 10% of maximal activity at pH 7.0
3 - 7
-
approx. 20% of maximal activity at pH 3.5, approx. 40% of maximal activity at pH 7.0
3 - 7
-
approx. 65% of maximal activity at pH 3.0, approx. 10% of maximal activity at pH 6.0
3 - 7
-
approx. 80% of maximal activity at pH 3.0, approx. 18% of maximal activity at pH 6.0
3 - 8
-
increase of enzyme activity with pH increase, above 8 decrease of enzyme activity with increasing pH
3 - 9
-
approx. 50% of maximal activity at pH 4.0 and pH 6.0, respectively
3 - 9
-
approx. 60% of maximal activity at pH 3.0, approx. 5% of maximal activity at pH 9.0
3.5 - 8
-
activity range, 75% of maximal activity at pH 4.5 and pH 7.5, profile overview
3.5 - 8
Thermochaetoides thermophila
-
approx. 16% of maximal activity at pH 4.5 and pH 6.5, respectively
4 - 6
-
4.0: about 50% of maximal activity, pH 6.0: about 35% of maximal activity
4 - 7
pH 4.0: about 65% of maximal activity, pH 7.0: about 45% of maximal activity, enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde
4 - 8
pH 4.0: about 30% of maximal activity, pH 8.0: about 30% of maximal activity, substrate: 4-nitrophenyl beta-D-glucopyranoside
4 - 8
pH 4.0: about 45% of maximal activity, pH 8.0: about 60% of maximal activity, beta-glucosidase TpBGL1
4 - 8
activity dropped to 22% at pH 8.0 and to near zero at pH 4.0
4 - 8.5
-
approx. 5% of maximal activity at pH 4.0 and pH 8.5, respectively
4 - 9
20% of maximal activity at pH 5.0 and pH 9.0, half-maximal activity at pH 5.5 and pH 8.5
4 - 9
pH 4.0: about 40% of maximal activity, pH 9.0: about 90% of maximal activity
4.5 - 8
pH-profile of wild-type and mutant isozymes BGL1A, overview
4.5 - 8
pH-profile of wild-type isozyme BGL1B, overview
5 - 6.5
pH 5.0: about 30% of maximal activity, pH 6.5: about 60% of maximal activity, substrate: 4-nitrophenyl beta-D-glucopyranoside
5 - 6.5
pH 5.0: about 90% of maximal activity, pH 6.5: about 70% of maximal activity, substrate: 4-nitrophenyl beta-D-glucopyranoside
5 - 7
pH 5.0: about 60% of maximal activity, pH 7.0: about 80% of maximal activity
5 - 7
there is a significant activity loss (up to 60%) at pH 5.0 and 7.0, compared to the optimum at pH 6.0
5.5 - 7.5
-
approx. 505 of maximal activity at pH 5.5, approx. 25% of maximal activity at pH 7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
30
35
37
40
45
45 - 50
50
50 - 55
with 4-nitrophenyl beta-D-glucopyranoside as substrate
52
53
55
55 - 60
60
65
70
75
80
85
90
98
-
immobilized and soluble enzyme, substrate: 2-nitrophenyl-beta-D-galactopyranoside
25
-
assay at 25°C, substrates: 2-nitrophenyl beta-D-glucopyranoside and 4-nitrophenyl beta-D-glucopyranoside
25
-
assay at 25°C, substrates: 2-nitrophenyl beta-D-glucopyranoside and 4-nitrophenyl beta-D-glucopyranoside
55
with 4-nitrophenyl beta-D-glucopyranoside as substrate
60
with 4-nitrophenyl beta-D-glucopyranoside as substrate
90
optimal temperature of native enzyme and of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 35
10 - 60
10 - 65
-
approx. 155 of maximal activity at 10°C, approx. 50% of maximal activity at 60°C
20 - 50
25% of maximal activity at 20°C and 50°C, half-maximal activity at 28°C and 46°C
20 - 60
20 - 70
25 - 55
-
25°C: about 85% of maximal activity, 55°C: about 65% of maximal activity
30 - 100
30 - 55
30 - 60
30 - 90
-
approx. 50% of maximal activity at 30°C, approx. 15% of maximal activity at 90°C
35 - 80
Thermochaetoides thermophila
-
approx. 50% of maximal activity at 50°C, 10% of maximal activity at 80°C
40 - 60
40 - 75
40 - 80
43 - 52
60% activity at 43°C, and 65% at 52°C, using p-nitrophenyl-beta-D-glucopyranoside as substrate
50 - 65
50°C: about 45% of maximal activity, 65°C: about 50% of maximal activity, substrate: 4-nitrophenyl beta-D-glucopyranoside
50 - 80
50 - 90
60 - 100
60°C: about 70% of maximal activity, 100°C: about 75% of maxim al activity
60 - 95
70 - 110
70°C: about 45% of maximal activity, 110°C: about 30% of maximal activity
additional information
10 - 60
-
approx. 50% of maximal activity at 30°C, approx. 10% of maximal activity at 60°C
10 - 60
-
approx. 20% of maximal activity at 10°C and 60°C, respecttively
20 - 60
-
approx. 40% of maximal activity at 20°C, approx. 205 of maximal activity at 60°C
20 - 70
-
approx. 60% of maximal activity at 20°C, approx. 10% of maximal activity at 65%
20 - 70
-
approx. 25% of maximal activity at 20°C, approx. 15% of maximal activity at 70°C
30 - 100
30°C: about 40% of maximal activity, 100°C: about 30% of maximal activity
30 - 55
more than 50% activity between 30 and 52°C. Activity decreases rapidly at temperature above 55°C
30 - 60
-
approx. 70% of maximal activity at 30°C, approx. 13% of maximal activity at 60°C
40 - 60
40°C: about 50% of maximal activity, 60°C: about 85% of maximal activity, substrate: 4-nitrophenyl beta-D-glucopyranoside
40 - 60
40°C: about 65% of maximal activity, 60°C: about 70% of maximal activity, substrate: 4-nitrophenyl beta-D-glucopyranoside
40 - 75
-
approx. 20% of maximal activity at 40°C and pH 4.5, approx. 15% of maximal activity at 70°C and pH 4.5
50 - 80
-
50°C: about 40% of maximal activity, 80°C: about 60% of maximal activity
50 - 90
-
approx. 25% of maximal activity at 50°C, approx. 40% of maximal activity at 90°C
50 - 90
-
approx. 30% of maximal activity at 50°C, approx. 20% of maximal activity at 90°C
60 - 95
60°C: about 50% of maximal activity, 95°C: about 65% of maximal activity, native enzyme
60 - 95
60°C: about 50% of maximal activity, 95°C: about 75% of maximal activity, enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
4.2
4.4
4.5
4.7
4.9
5.1
5.6
4.5
-
isoelectric focusing, different isoenzymes probably due to different degrees of glycosylation
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fused enzyme to a cellulose-binding domain from Cex-exoglucanase
-
-
brenda
diverse strains isolated from sicilian wines and musts, e.g. strains CBS314 and Y8 with high enzyme activity
-
-
brenda
Littorina kurila
isoform G-II, exhibits both exo-glucanase and beta-D-glucosidase activities
-
-
brenda
best source of beta-glucosidase activity among 60 yeasts isolated from grape musts
-
-
brenda
isolation of isoforms beta-glu 1 and beta-glu 2 from hypercellulolytic Pol6 mutant
-
-
brenda
desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
-
-
brenda
able to grow at 4-20°C using beta-glycoside substrates such as cellobiose, as carbon source
UniProt
brenda
Thermochaetoides thermophila
RuBGX1, beta-glucosidase/xylosidase activity, EC 3.2.1.37 and 3.2.1.21, as D272 is the catalytic nucleophile, and E167 and E481 are the catalytic acids; isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
UniProt
brenda
-
-
-
brenda
enzyme is purified from the protoplast fusant of Aspergillus oryzae 3.481 and Aspergillus niger 3.316
-
-
brenda
parent wild-type strain NIAB 442 and a deoxyglucose- and streptomycin-resistant mutant strain thereof
-
-
brenda
from feces of Lama glama at the Ribeirao Preto Municipal Zoo (SP, Brazil)
-
-
brenda
from feces of Lama glama at the Ribeirao Preto Municipal Zoo (SP, Brazil)
-
-
brenda
CelG, beta-glucosidase; subsp. carotovorum, strain LY34, gene celG
SwissProt
brenda
isozyme BGL1A; gene bgl1A, isozyme BGL1A
SwissProt
brenda
isozyme BGL1B; gene bgl1B, isozyme BGL1B
SwissProt
brenda
isozyme BGL1A; gene bgl1A, isozyme BGL1A
SwissProt
brenda
isozyme BGL1B; gene bgl1B, isozyme BGL1B
SwissProt
brenda
a filamentous fungus, strain A19, isolated after nitrous acid mutagenesis from the cellulolytic fungus N1, five isozymes
-
-
brenda
mutant strain A19 is isolated from the cellulolytic fungus strain N1
-
-
brenda
microbial metagenome of Lake Poraque, Amazon, Brazil
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in immature fruits the reactive cells are very few and located in the inner mesocarp zone, thereafter, in green mature fruits a great number of reactive cells are found distributed in the whole mesocarp. Finally in black fruits numerous reactive cells are located only in the inner mesocarp close by the woody endocarp, whereas the outer mesocarp cells are devoted to polymeric anthocyanins accumulation
brenda
additional information
-
maximal enzyme synthesis, if cells grown in wheat bran medium
brenda
-
3 isoforms, isoform Gb-1 most strongly induced by growth in cellulose medium
brenda
-
3 different forms in the culture filtrate, 1 form intracellular
brenda
-
maximal enzyme synthesis, if cells grown in wheat bran medium
brenda
Sporotrichum pulverulentum
-
five different forms in culture filtrate, 1 form cell-wall bound
brenda
Thermochaetoides thermophila
-
3 different forms, one with cellobiose-activity, two with exclusive aryl-beta-glucosidase activity
brenda
-
two forms, one membrane-bound, one extracellular
brenda
-
potent formation of cellobiase activity by induction by sophorose
brenda
-
beta-glucosidase and cellulases are secreted upon growth on cellulose. No secretion when grown on cellobiose
brenda
-
the termite egg-recognition pheromone consists of beta-glucosidase and lysozyme
brenda
-
the termite egg-recognition pheromone consists of beta-glucosidase and lysozyme
brenda
-
cell and tissue in situ localization of the enzyme during fruit ripening, overview
brenda
-
infection by fruit flies reduces the enzyme activity in fruits, enzyme activityis highest in october
brenda
-
beta-glucosidases are bound to mycelia during active growth when rapid cellulolysis occurs
brenda
-
presence of isoform Pyk10 restricts root colonization by Piriformospora indica, resulting in repression of defence responses and the upregulation of responses leading to a mutualistic interaction between the two symbiotic partners
brenda
-
both beta-glucosidase and lysozyme are major salivary compounds
brenda
-
both beta-glucosidase and lysozyme are major salivary compounds
brenda
young, isozyme TaGlu1a, isozyme expression profile, overview
brenda
young, isozyme TaGlu1b, isozyme expression profile, overview
brenda
young, isozyme TaGlu1c, isozyme expression profile, overview
brenda
stipe cell wall, enzyme is more highly expressed in the elongating apical stipe than in non-elongating basal regions
brenda
-
stipe cell wall, enzyme is more highly expressed in the elongating apical stipe than in non-elongating basal regions
-
brenda
additional information
-
construction of 3 chimeric enzymes derived from substituting segments from the C-terminus of Cellvibrio gilvus and Agrobacterium tumefaciens beta-glucosidase genes
brenda
additional information
-
cultivation in corn-cob by solid state fermentation
brenda
additional information
-
cultivation in corn-cob by solid state fermentation
-
brenda
additional information
-
cells grown on straw of Leptochloa fusca, a salt-resistant grass, resulting in high enzyme activity, or on salt culture medium with different carbon sources added, overview
brenda
additional information
-
chomosomal DNA, one gene coding for a cellobiose and aryl-glucoside hydrolysing enzyme, one gene coding for an only aryl-glucoside hydrolyzing enzyme
brenda
additional information
-
mutant strain PN-120 produces a beta-glucosidase that is 16fold more active than the corresponding enzyme isolated from the parental strain
brenda
additional information
-
construction of 3 chimeric enzymes derived from substituting segments from the C-terminus of Cellvibrio gilvus and Agrobacterium tumefaciens beta-glucosidase genes
brenda
additional information
-
cultivation on cellulose or Pinus taeda wood, biopulping conditions, optimization and evaluation, overview
brenda
additional information
-
cultivation on cellulose or Pinus taeda wood, biopulping conditions, optimization and evaluation, overview
-
brenda
additional information
-
screening of 102 pure yeast cultures isolated from wine ecosystems for enzyme activity
brenda
additional information
-
screening of 102 pure yeast cultures isolated from wine ecosystems for enzyme activity
-
brenda
additional information
-
the fungus is fed-batch cultivated on cellulose
brenda
additional information
-
cultivation in corn-cob by solid state fermentation
brenda
additional information
-
cultivation in corn-cob by solid state fermentation
-
brenda
additional information
isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
two different oleuropein-degradative-beta-glucosidases are present
brenda
-
isoform Pyk10 is localized in ER bodies and has beta-D-glucosidase and beta-D-fucosidase activities. Jacalin-related lectins regulate the size of the active Pyk10 complexes, with two types of lectins working antagonistically
brenda
-
two different oleuropein-degradative-beta-glucosidases are present
brenda
-
detergent-solubilized and papain-released forms
brenda
Thermochaetoides thermophila
-
one cellobiase and one aryl-beta-glucosidase
-
brenda
-
variation in the number of isoforms, depending on culture medium used, due to proteolytic cleveage of a single polypeptide
-
brenda
-
most effective induction of enzyme synthesis in medium containing quercetin
-
brenda
-
increasing activity by acclimation with cellobiose
-
brenda
despite lacking a classical N-terminal signal peptide, the enzyme is a secretory protein
-
brenda
-
despite lacking a classical N-terminal signal peptide, the enzyme is a secretory protein
-
-
brenda
-
most enzyme synthesis if grown in medium containing yeast extract
-
brenda
Sporotrichum pulverulentum
-
high extracellular activities, if cellulose serves as carbon source
-
brenda
-
absorption of enzyme to mycelium, if cells grown on glucose medium
-
brenda
-
stimulation of enzyme synthesis by cellobiose as carbohydrate source
brenda
-
stimulation of enzyme synthesis by cellobiose as carbohydrate source
brenda
-
expression of mRNA higher with cellobiose than with glucose as a carbon source
brenda
-
induction of enzyme synthesis by addition of cellobiose or laminaribiose to the medium
brenda
Sporotrichum pulverulentum
-
cell bound activity if cellobiose dominating in the medium
brenda
-
enzyme beta-glucosidase exists as a long fibrillar structure of isoform AsGlu1 homomultimer, i.e. type I and heteromultimer of isoforms AsGlu1 and AsGlu2, i.e. type II
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the glycoside hydrolase family 1, GH1
evolution
-
the enzyme belongs to the glycoside hydrolase family 1, GH1
-
malfunction
enzyme deletion mutants lacking either the N-terminal 10 amino acids or the C-terminal 10 residues are biologically inactive
malfunction
-
enzyme deletion mutants lacking either the N-terminal 10 amino acids or the C-terminal 10 residues are biologically inactive
-
metabolism
-
the interaction of cellobiose dehydrogenase (CDH) and beta-GLU (beta-glucosidase) determines the conversion of cellobiose to cellobionolactone or glucose. The formation of cellobionolactone from cellobiose as a result of the action of CDH depends on the availability of quinones (for CDH), which are formed by the interaction of laccase with a phenolic compound. At low quinone concentrations, cellobiose is transformed by beta-GLU to glucose
metabolism
-
the interaction of cellobiose dehydrogenase (CDH) and beta-GLU (beta-glucosidase) determines the conversion of cellobiose to cellobionolactone or glucose. The formation of cellobionolactone from cellobiose as a result of the action of CDH depends on the availability of quinones (for CDH), which are formed by the interaction of laccase with a phenolic compound. At low quinone concentrations, cellobiose is transformed by beta-GLU to glucose
-
physiological function
-
ball-milled crude cellulosics, such as newsprint, de-inked newsprint, glossy writing paper, toilet paper and beech sawdust are substantially solubilised by extracellular cellulases within 110 h of growth. The type of crude cellulosic material greatly influences the pattern of enzyme production. Growth on carboxymethyl cellulose medium is accompanied by high endoglucanase (E.C. 3.2.1.4) activity. The cellulase complex e.g. exo-/3-1,4-glucanase (E.C.3.2.1.-); endo-/3-1,4-glucanase (E.C.3.2.1.4) and 8-glucosidase (E.C.3.2.1.21) displays quite different properties depending on whether it is formed on low or highly substituted carboxymethyl cellulose
physiological function
-
beta-glucosidase activity of strain C464 is among the highest reported for filamentous fungi, i.e. 25 IU/ml cell-associated acitivity and 7 IU/ml extracellular activity
physiological function
-
beta-glucosidase and cellulases are secreted upon growth on cellulose. No secretion when grown on cellobiose
physiological function
-
in solid state fermentation using lignocellulosic materials as substrates, Myceliophthora thermophila JCP 1-4 is the best producer of endoglucanase (357,51 U/g), beta-glucosidase (45.42 U/g), xylanase (93,11 U/g) and avicelase (3.58 U/g) among the strain tested
physiological function
-
strain produces 40.4 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
physiological function
enzyme causes a decrease in the molecular size of stipe wall beta-glucan by removing glucose and is more highly expressed in the elongating apical stipe than in non-elongating basal regions
physiological function
-
expression of beta-glucosidase in the chloroplast genome of tobacco. The recombinant enzyme exhibits high enzymatic activity at pH 5, and at 40°C. Recombinant plants show a similar phenotype compared with the wild type plants
physiological function
the enzyme may be involved in plant defence
physiological function
-
beta-glucosidase activity of strain C464 is among the highest reported for filamentous fungi, i.e. 25 IU/ml cell-associated acitivity and 7 IU/ml extracellular activity
-
physiological function
-
strain produces 40.4 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
-
physiological function
Thermothelomyces thermophilus JCP 1-4
-
in solid state fermentation using lignocellulosic materials as substrates, Myceliophthora thermophila JCP 1-4 is the best producer of endoglucanase (357,51 U/g), beta-glucosidase (45.42 U/g), xylanase (93,11 U/g) and avicelase (3.58 U/g) among the strain tested
-
physiological function
-
enzyme causes a decrease in the molecular size of stipe wall beta-glucan by removing glucose and is more highly expressed in the elongating apical stipe than in non-elongating basal regions
-
additional information
enzyme-substrate docking studies, overview
additional information
-
synergism of the purified enzyme BglHi2 and Trichderma reesei cellulase in the hydrolysis reaction, overview
additional information
-
synergism of the purified enzyme BglHi2 and Trichderma reesei cellulase in the hydrolysis reaction, overview
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
101000
102000
110000
113000
114000
115000
116000
118000
120000
125000
130000
133000
135000
136000
140000
the membrane fractions of cells grown in presence of cellobiose contain two isozymes of 75 and 140 kDa, SDS-PAGE
165000 - 182000
Sporotrichum pulverulentum
-
gel filtration, five different forms in culture filtrate
167000
170000
182000
beta-glucosidase TpBGL3, dynamic light scattering at pH 6
200000
210000
220000
230000
240000
27000
275000
300000
313000
320000
33000
330000
380000
42000
43000
460000
49000
50000
51500
53000
54000
55000
57000
57346
-
1 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 1 * 57346, mass spectrometry
58000
59000
59700
60000
65000
66000
6688
-
MALDI-TOF mass spectrometry, in the presence of 2-deoxy-D-glucose
68000
70000
71000
74000
75000
76000
80000
82000
85000
90000
92000
94000
96000
98000
-
x * 98000, SDS-PAGE, both isoforms beta-glu 1 and beta-glu 2 from hypercellulolytic Pol6 mutant
additional information
102000
beta-glucosidase TpBGL3, dynamic light scattering at pH 6
113000
beta-glucosidase TpBGL1, dynamic light scattering at pH 4
120000
-
beta-glucosidase B, +/-10%, determined by 5-20% linear sucrose gradient centrifugation
130000
-
x * 130000, calculated, x * 130000, SDS-PAGE, and x * 230000, SDS-PAGE of enzyme purified in presence of Ca2+ or enzyme in crude extract
167000
beta-glucosidase TpBGL1, dynamic light scattering at pH 4
220000
-
beta-glucosidase C, +/-10%, determined by 5-20% linear sucrose gradient centrifugation
230000
-
x * 130000, calculated, x * 130000, SDS-PAGE, and x * 230000, SDS-PAGE of enzyme purified in presence of Ca2+ or enzyme in crude extract
50000
mutant enzyme R170A/R220A/Y227F/R459G, monomer, gel filtration
50000
x * 66000, tagged recombinant enzyme, SDS-PAGE, x * 50000, detagged recombinant enzyme, SDS-PAGE
53000
x * 53000, recombinant His-tagged isozyme BGL1A, SDS-PAGE
55000
-
1 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 1 * 57346, mass spectrometry
55000
2 * 55000, SDS-PAGE after heating at 95°C,mutant enzyme R170A/R220A/Y227F
58000
-
alpha=39000 Da, beta=19000 Da, chromatography on P-100 and S-300 columns
60000
x * 60000, recombinant His-tagged isozyme BGL1B, SDS-PAGE
66000
x * 66000, tagged recombinant enzyme, SDS-PAGE, x * 50000, detagged recombinant enzyme, SDS-PAGE
71000
mutant enzyme R170A/R220A/Y227F/R448E, monomer, gel filtration
75000
the membrane fractions of cells grown in presence of cellobiose contain two isozymes of 75 and 140 kDa, SDS-PAGE
85000
2 * 85000, SDS-PAGE, difference to deduced molecular weight is due to glycosylation
96000
mutant enzyme R170A/R220A/Y227F/R449R, monomer, gel filtration
additional information
formation of both homo- and heterohexamers by the isozyme
additional information
formation of both homo- and heterohexamers by the isozyme
additional information
formation of both homo- and heterohexamers by the isozyme
additional information
formation of both homo- and heterohexamers by the isozymes
additional information
formation of both homo- and heterohexamers by the isozymes
additional information
formation of both homo- and heterohexamers by the isozymes
additional information
dimer structure, SAXS scattering and energetic analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotrimer
hexamer
homodimer
homotetramer
monomer
octamer
oligomer
tetramer
trimer
additional information
?
-
x * 63000-64000, native enzyme, SDS-PAGE, x * 66000-69000, recombinant dalcochinase with N-terminal truncation and polyhistidine tag, SDS-PAGE
?
x * 66000, tagged recombinant enzyme, SDS-PAGE, x * 50000, detagged recombinant enzyme, SDS-PAGE
?
-
x * 98000, SDS-PAGE, both isoforms beta-glu 1 and beta-glu 2 from hypercellulolytic Pol6 mutant
?
x * 53000, recombinant His-tagged isozyme BGL1A, SDS-PAGE
?
x * 60000, recombinant His-tagged isozyme BGL1B, SDS-PAGE
dimer
2 * 85000, SDS-PAGE, difference to deduced molecular weight is due to glycosylation
dimer
2 * 55000, SDS-PAGE after heating at 95°C,mutant enzyme R170A/R220A/Y227F
heterotrimer
-
1 * 165200, plus 1 * 87900, plus 1 * 56800, SDS-PAGE
-
hexamer
6 * 64085.41, recombinant His-tagged TaGlu1b, SDS-PAGE, gel filtration, and mass spectrometry
hexamer
6 * 64141.25, recombinant His-tagged isozyme TaGlu1a, SDS-PAGE, gel filtration, and mass spectrometry
hexamer
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
homodimer
beta-glucosidase TpBGL1 is a stable homodimer in solution. The oligomerization state does change in response to decreasing the pH from 6 to 4 at 20°C
homodimer
beta-glucosidase TpBGL3 is a stable homodimer in solution. The oligomerization state does change in response to decreasing the pH from 6 to 4 at 20°C
homodimer
-
beta-glucosidase TpBGL3 is a stable homodimer in solution. The oligomerization state does change in response to decreasing the pH from 6 to 4 at 20°C
-
homodimer
-
beta-glucosidase TpBGL1 is a stable homodimer in solution. The oligomerization state does change in response to decreasing the pH from 6 to 4 at 20°C
-
monomer
-
1 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 1 * 57346, mass spectrometry
monomer
1 * 127000, calculated from sequence
monomer
1 * 78276, calculated from sequence
monomer
1 * 80000, calculated from sequence
monomer
1 * 96873, calculated from sequence
monomer
1 * 97117, calculated from sequence
monomer
1 * 54100, calulated, 1 * 59000, SDS-PAGE of recombinant His-tagged protein
monomer
-
1 * 54100, calulated, 1 * 59000, SDS-PAGE of recombinant His-tagged protein
-
monomer
1 * 50000, mutant enzyme R170A/R220A/Y227F/R459G, SDS-PAGE
monomer
1 * 71000, mutant enzyme R170A/R220A/Y227F/R448E, SDS-PAGE
monomer
1 * 96000, mutant enzyme R170A/R220A/Y227F/R449R, SDS-PAGE
monomer
native-PAGE shows Bgl1A in the form of a monomer and dimer
octamer
-
composed of 8 identical subunits, ability of each octamer to link with each other to form long polymeric assemblies, crystal structure analysis
octamer
composed of 8 identical subunits, (alpha/beta)-8-barrel-structural fold, crystal structure analysis
octamer
-
composed of 8 identical subunits, (alpha/beta)-8-barrel-structural fold, crystal structure analysis
oligomer
-
x * 130000, calculated, x * 130000, SDS-PAGE, and x * 230000, SDS-PAGE of enzyme purified in presence of Ca2+ or enzyme in crude extract
oligomer
-
x * 115000, isoform beta-glucosidase 1, x * 94000 plus x * 21000, isoform beta-glucosidase 2, x * 94000 plus x * 21000, isoform beta-glucosidase 3, x * 52000, isoform beta-glucosidase 4, x * 49000 plus x * 46000, isoform beta-glucosidase 5, x * 77000, isoform beta-glucosidase 6, SDS-PAGE
oligomer
[Humicola] grisea var. thermoidea IFO 9854
-
x * 115000, isoform beta-glucosidase 1, x * 94000 plus x * 21000, isoform beta-glucosidase 2, x * 94000 plus x * 21000, isoform beta-glucosidase 3, x * 52000, isoform beta-glucosidase 4, x * 49000 plus x * 46000, isoform beta-glucosidase 5, x * 77000, isoform beta-glucosidase 6, SDS-PAGE
-
tetramer
composed of 4 identical subunits, X-ray diffraction study
additional information
-
quarternary structure analysis, structure and kinetics of multimers of different size, overview
additional information
the main-chain fold of the enzyme belongs to the (beta/alpha)8 barrel structure, the active site is located at the bottom of a pocket formed by large surface loops, surrounding the C termini of the barrel of beta-strands
additional information
-
the main-chain fold of the enzyme belongs to the (beta/alpha)8 barrel structure, the active site is located at the bottom of a pocket formed by large surface loops, surrounding the C termini of the barrel of beta-strands
additional information
oligomerization in BglA can assist in fine-tuning the specificity of the active centre by modulating the loops surrounding the cavity, BglB aglycon site structure, overview
additional information
-
oligomerization in BglA can assist in fine-tuning the specificity of the active centre by modulating the loops surrounding the cavity, BglB aglycon site structure, overview
additional information
determination and analysis of the subsite -1, i.e. glycone site, of isozyme BGL1A, overview, the loop region covering on the (beta/alpha)8 barrel is significantly deviated forming a unique subsite +1, i.e. aglycone site, of BGL1A
additional information
-
determination and analysis of the subsite -1, i.e. glycone site, of isozyme BGL1A, overview, the loop region covering on the (beta/alpha)8 barrel is significantly deviated forming a unique subsite +1, i.e. aglycone site, of BGL1A
additional information
molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview
additional information
molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview
additional information
-
molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview
additional information
-
enzyme exists in a 130000 Da and in a 230000 Da form. Kinetic data for some substrates are different for the two forms, while no difference is observed in optimum pH and temperature
additional information
secondary structure prediction and homology molecular modeling
additional information
-
secondary structure prediction and homology molecular modeling
additional information
-
secondary structure prediction and homology molecular modeling
-
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview
additional information
formation of both homo- and heterohexamers by the isozymes, the hexameric form is the active form, smaller oligomers or monomers are inactive, the N-terminal region of isozyme TaGlu1a is located at the dimer-dimer interface and plays a crucial role in hexamer formation, primary structure of the aglycone binding site, overview
additional information
-
capillary LCESI/MS peptide sequence determination and protein identification
additional information
enzyme specifically interacts with chimeric lectin beta-glucosidase aggregating factor resulting in high molecular weight complexes
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
-
recombinant dalcochinase is apparently composed of differently post-translationally modified forms with similar properties compared to the native enzyme
glycoprotein
-
carbohydrate content: 11% galactose, 4% mannose, 1% glucose
glycoprotein
-
carbohydrate content, w/w: 8.8 cellobiase A, 9.4 cellobiase B, 7.2 cellobiase C
glycoprotein
-
contains alpha-D-mannose-, alpha-D-glucose- and 2-O-D-mannose-residues
glycoprotein
the enzyme is N-glycosylated at residue N43 and N237, which is not essential for activity
glycoprotein
12 putative N-glycosylation sites
glycoprotein
2 putative N-glycosylation sites
glycoprotein
7 putative N-glycosylation sites
glycoprotein
-
enzyme from mutant strain contains 70%, w/w, carbohydrate, wild-type enzyme 60% carbohydrate, w/w
glycoprotein
sequence contains two potential N-glycosylation sites and sixteen O-glycosylation sites
glycoprotein
-
sequence contains two potential N-glycosylation sites and sixteen O-glycosylation sites
-
glycoprotein
-
the extracellular enzyme contains 82.3% carbohydrate
glycoprotein
-
the extracellular enzyme contains 82.3% carbohydrate
-
glycoprotein
-
8% carbohydrate content, both isoforms beta-glu 1 and beta-glu 2 from hypercellulolytic Pol6 mutant
glycoprotein
sequence contains at least 16 potentiyl N-glycosylation sites. Treatment with PNGase F leads to a decrease in molecular mass
glycoprotein
-
23.4% carbohydrate content, w/w, enzymatic removal of carbohydrate moiety decreases thermal stability
glycoprotein
the enzyme contains nine potential N-glycosylation sites at Asn67, Asn75, Asn259, Asn330, Asn362, Asn423, Asn476, Asn644, and Asn661, removing the sugar chains of recombinant BGLII with Endo-H does not affect its properties including thermo-stability, optimal temperature, optimal pH, pH stability, and activation by organic solvents
glycoprotein
-
the enzyme contains nine potential N-glycosylation sites at Asn67, Asn75, Asn259, Asn330, Asn362, Asn423, Asn476, Asn644, and Asn661, removing the sugar chains of recombinant BGLII with Endo-H does not affect its properties including thermo-stability, optimal temperature, optimal pH, pH stability, and activation by organic solvents
-
glycoprotein
-
beta-glucosidase I, 0.12%, w/w, carbohydrate, beta-glucosidase II, 9%, w/w, carbohydrate
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure
covalent intermediate of mutant E165P, in which glucose is bound to nucleophile E373. Structure confirms a double displacement mechanism
purified recombinnat enzyme, hanging drop vapour diffusion method, micro-seeding, the protein crystallized in 1.6 M ammonium sulfate, 100 mM HEPES, pH 7.0, within 4 weeks, X-ray diffraction structure determination and analysis
-
purified wild-type enzyme, 0.002 ml of protein solution containing 4 mg/ml protein in 20 mM MES, pH 6.0, are mixed with 0.001 ml of reservoir solution containing 0.2 M ammonium sulphate, MES buffer, pH 6.5, and 30% w/v polyethyleneglycol-monomethylether 5500, 20°C, several days, X-ray diffraction structure determination and anaylsis at 2.7 A resolution, molecular replacement method, modeling
hanging drop vapor diffusion method, using 0.04 M potassium dihydrogen phosphate pH 5.1, 16% (w/v) PEG 8000, and 20% (v/v) glycerol, at 20°C
structures of Lin1840 wild-type and mutant D270A in complexes with sophorose and laminaribiose. Residue Arg572 forms many hydrogen bonds with sophorose and laminaribiose at subsite +1, a key factor for substrate selectivity. The opposite side of subsite +1 from Arg572 is connected to a large empty space, which may be subsite +2 for the binding of sophorotriose
free enzyme and its covalent intermediate with 2-deoxy-2-fluoroglucoside at 2.2 A and 1.55 A resolution, respectively. The complex with the 2-fluoroglucoside includes a glycerol molecule, which may make a nucleophilic attack on the anomeric carbon in a transglycosylation reaction. Sugars are positioned as acceptors for transglycosylation by their interactions with E176, the catalytic acid/base, and Y131. Residues I179, N190 and N245 appear to interact with the substrates
in complex with a covalent intermediate, 2-deoxy-2-fluoroglucoside and, n-octyl-beta-D-thioglucopyranoside, microbatch under oil method, using 0.1 M Bis-Tris, pH 6.5, and 20% PEG MME 5000
purified recombinant enzyme, free and in a complex with 2,4-dinitrophenyl-2-deoxy-2-fluoro-beta-D-glucopyranoside inhibitor, growth of small crystals in 18% w/v PEG 8000 with 0.1 M sodium cacodylate, pH 6.5, and 0.2 M zinc acetate, 1-2 days, microseeding into 23% w/v PEG MME 5000, 0.2 M ammonium sulfate, and 0.1 M MES, pH 6.7, resulting in larger crystals, 1-2 months, X-ray diffraction structure determination and analysis at 2.15 A and 2.75 A resolution, respectively, molecular replacement, screening and method optimization, overview
structures of the BGlu1 E176Q mutant, its complexes with cellotetraose, cellopentaose and laminaribiose, and its covalent intermediate with 2-deoxy-2-fluoroglucoside are determined at 1.65, 1.95, 1.80, 2.80, and 1.90 A resolution, respectively
-
thioredoxin/His6-tagged 4BGlu12 fusion protein complexed with 2,4-dinitrophenyl-2-deoxy-2-fluoro-beta-D-glucopyranoside, hanging drop vapor diffusion method, using 19% polyethylene glycol (3350 or 2000) in 0.1 M Tris-HCl pH 8.5, 0.16 M NaCl, at 15°C
isozyme BglB with bound inhibitors 2-deoxy-2-fluoro-alpha-D-glucopyranose or thiocellobiose, glucose, or as BglB-cellotetraose complex, X-ray difraction structure determination and analysis at 2.15-2.45 A resolution
isozyme BGL1A in substrate-free and gluconolactone complexed forms, sitting-drop vapor diffusion method at 25 °C, using a mixture of 0.001 ml of protein solution containing 10 mg/ml protein in 20 mM TrisHCl, pH 7.5, 150 mM NaCl, with or without 10 mM D-glucono-1,5-lactone, and 0.001 ml of a reservoir solution containing 12% isopropanol, 15% PEG 6000 and 0.1M sodium citrate, pH 5.8, the cryoprotectant solution contains 20% MPD, 15% PEG 6000 and 0.1M sodium citrate, pH 5.8, X-ray diffraction structure determination and analysis at 1.5-1.9 A resolution, modeling
mutant enzyme R170A/R220A/Y227F, hanging-drop vapour-diffusion method, the structure is determined at 2.35 A resolution, stable homotetrameric structure, a dimeric form of the enzyme is constructed and its crystal structure is solved at a resolution of 1.70 A
to 0.98 A resolution. Enzyme is a highly N-glycosylated three-domain dimeric protein
to 2.2 A resolution. Enzyme is a highly N-glycosylated three-domain dimeric protein
wild-type Dhr1, and Dhr1 mutant E189D in complex with dhurrin, hanging drop vapour diffusion method, 0.002 ml of 8 mg/ml protein in 20 mM Tris, pH 7.0, mixed with an equal volume of reservoir solution containing 0.1 M HEPES, pH 7.5, 2.0 M ammonium sulfate, and 50 mM NaCl, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution
-
at a resolution of 2.05A. It is composed of an (alpha/beta)8 domain similar to a triose phosphate isomerase barrel, a five-stranded alpha/beta sandwich domain (both of which are important for active-site organization), and a C-terminal fibronectin type III
mutant E349G, to 1.9 A resolution, and docking studies of flavonoid substrates
purified recombinant wild-type and selenomethionine-substituted enzymes, hanging drop vapour diffusion method, 3-5 mg/ml protein in 20 mM MES buffer, pH 6.2, crystallization in microplates at 20°C within 4 days, precipitant is 90 mM bis-Tris propane buffer, pH 7.4, with 16-20% PEG 3350, 0.1-0.2 M NaI for the wild-type enzyme, and 20-24% PEG 3350, 0.1-0.25 M NaI for the selenomethionine-labeled enzyme, mixture of 0.001 ml of protein and reservoir solution, X-ray diffraction structure determination and analysis at 2.4 A resolution, MAD method, model building
-
purified recombinant enzyme complexed with a substrate aglycone, 20°C, hanging drop vapour diffusion method, 0.001 ml of 3.7 mg/ml protein in solution mixed with 0.001 ml reservoir solution containing 10 mM HEPES, pH 7.2, 1 M LiSO4, and 150 mM NaCl, X-ray diffraction structure determination and preliminary analysis at 1.7 A resolution, molecular replacement
-
purified recombinant isozyme TaGlu1a, X-ray diffraction structure determination and analysis at 1.8 A resolution
in ligand-free form, and in complex form with D-glucose, with inhibitor isofagomine, and D-fucose, wild-type and mutants in residue N223, to 1.2-1.9 A resolution
molecular modeling of structure. Residues Asp333 and Glu530 may act as the catalytic nucleophile and acid/base, respectively. Residues Val87, Leu187, Thr368, and Trp474 may participate in substrate recognition and binding
-
to 2.75 A resolution. The predicted aglycone region is surrounded by hydrophobic residues Val220, Pro294, and Ala237. The residues His174 and Trp342 delimit the access to the -1 subsite and are critical to define the active site architecture
crystal structure of mutant E191D,F198V is determined at 1.9 A resolution in complex with DIMBOA-glucoside
purified recombinant Glu1 mutant E191D in complex with cyclic inhibitor glucoetrazole, the crystallization solution is miced with 0.005 ml glycerol and 0.003 ml of inhibitor solution, X-ray diffraction structure determination and analysis at 1.95 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C174V
H0HC94
contrary to uncompetitive inhibition of wild-type by glucose, mutant is competitively inhibited
H229S
H0HC94
contrary to uncompetitive inhibition of wild-type by glucose, mutant is competitively inhibited
L178E
C174V
-
contrary to uncompetitive inhibition of wild-type by glucose, mutant is competitively inhibited
-
H229S
-
contrary to uncompetitive inhibition of wild-type by glucose, mutant is competitively inhibited
-
L178E
D463A
-
the variant exhibits kinetic constants similar to the wild type enzyme
D487A
-
the variant exhibits kinetic constants similar to the wild type enzyme
D496A
-
the variant exhibits kinetic constants similar to the wild type enzyme
D501A
-
the variant exhibits kinetic constants similar to the wild type enzyme
E490A
-
the variant exhibits greatly reduced kcat and kcat/Km values toward the natural substrate cellobiose (67000 and 61000fold, respectively)
W49A
-
site-directed mutagenesis, the mutation reduces the transglucosylation activity of the enzyme due to a large decrease in binding capacity for Glc at site +1 and an increase in binding ability at site-1, while the hydrolytic activity is only slightly decreased compared to the wild-type enzyme, the mutant shows altered kinetics, overview
W49D
-
site-directed mutagenesis, the mutation reduces the transglucosylation activity of the enzyme due to a large decrease in binding capacity for Glc at site +1 and an increase in binding ability at site-1, while the hydrolytic activity is only slightly decreased compared to the wild-type enzyme, the mutant shows altered kinetics, overview
W49G
-
site-directed mutagenesis, the mutation reduces the transglucosylation activity of the enzyme due to a large decrease in binding capacity for Glc at site +1 and an increase in binding ability at site-1, while the hydrolytic activity is only slightly decreased compared to the wild-type enzyme, the mutant shows altered kinetics, overview
W49N
-
site-directed mutagenesis, the mutation reduces the transglucosylation activity of the enzyme due to a large decrease in binding capacity for Glc at site +1 and an increase in binding ability at site-1, while the hydrolytic activity is only slightly decreased compared to the wild-type enzyme, the mutant shows altered kinetics, overview
D463A
-
the variant exhibits kinetic constants similar to the wild type enzyme
-
D487A
-
the variant exhibits kinetic constants similar to the wild type enzyme
-
D496A
-
the variant exhibits kinetic constants similar to the wild type enzyme
-
D501A
-
the variant exhibits kinetic constants similar to the wild type enzyme
-
E490A
-
the variant exhibits greatly reduced kcat and kcat/Km values toward the natural substrate cellobiose (67000 and 61000fold, respectively)
-
G294A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294C
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294D
-
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
G294E
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294F
-
site-directed mutagenesis, the mutant shows 1.5fold higher activities for substrate recognition than the wild-type enzyme
G294H
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294I
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294K
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294L
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294M
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294N
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294P
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G294Q
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294R
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G294S
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G294T
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294V
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294W
-
site-directed mutagenesis, the mutant shows 1.5fold higher activities for substrate recognition than the wild-type enzyme
G294Y
-
site-directed mutagenesis, the mutant shows 1.6fold higher activities for substrate recognition than the wild-type enzyme
E495L
-
isoform AsGlu2. Mutation assembles the AsGlu2 into fibrillar homomultimers. The mutant AsGlu2 homomultimer is highly stable and has relatively faster electric mobility in native gel than the AsGlu1 homomultimer. Multimerization increases enzyme affinity to substrates
F417S
significantly impaired catalytic activity with cellobiose and lactose as substrates, 1000fold decrease in apparent kcat of cellobiose, 47fold decrease in kcat of lactose. Mutant produces improved total galactooligosaccharides yields by transgalactosylation
F417Y
mutant retains the capacity to hydrolyze both cellobiose and lactose with the same relative substrate selectivity as the wild-type, but with about 10fold lower turnover numbers. Mutant produces improved total galactooligosaccharides yields by transgalactosylation
N222F
significantly impaired catalytic activity with cellobiose and lactose as substrates
N294T
significantly impaired catalytic activity with cellobiose and lactose as substrates
Y296F
significantly impaired catalytic activity with cellobiose and lactose as substrates. Mutant produces improved total galactooligosaccharides yields by transgalactosylation
F417S
-
significantly impaired catalytic activity with cellobiose and lactose as substrates, 1000fold decrease in apparent kcat of cellobiose, 47fold decrease in kcat of lactose. Mutant produces improved total galactooligosaccharides yields by transgalactosylation
-
F417Y
-
mutant retains the capacity to hydrolyze both cellobiose and lactose with the same relative substrate selectivity as the wild-type, but with about 10fold lower turnover numbers. Mutant produces improved total galactooligosaccharides yields by transgalactosylation
-
N222F
-
significantly impaired catalytic activity with cellobiose and lactose as substrates
-
N294T
-
significantly impaired catalytic activity with cellobiose and lactose as substrates
-
Y296F
-
significantly impaired catalytic activity with cellobiose and lactose as substrates. Mutant produces improved total galactooligosaccharides yields by transgalactosylation
-
D409H
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, obligated GD heterozygotes
E165P
crystallization data of covalent intermediate with substrate, in which glucose is bound to nucleophile E373
F225S
-
0.65% of wild-type specific activity with p-nitrophenyl-beta-D-glucopyranoside
L444P
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, obligated GD heterozygotes
M172L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, and altered substrate specificity
N370S
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, obligated GD heterozygotes, and homozygote GD patients
N370S/D409H
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, homozygote GD patients
N370S/L444P
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, homozygote GD patients
Q307N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, and altered substrate specificity
V168Y
-
12% of wild-type specific activity with p-nitrophenyl-beta-D-glucopyranoside
W345M
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, and altered substrate specificity
Y308A
-
0.3% of wild-type specific activity with p-nitrophenyl-beta-D-glucopyranoside
Y308F
-
6% of wild-type specific activity with p-nitrophenyl-beta-D-glucopyranoside
F304I
mutant enzyme shows no activity with 4-nitrophenyl beta-D-glucopyranoside
I278F
decreased activities towards 4-nitrophenyl beta-D-glucopyranoside, hydrolysis activity on sophorose, which is much higher than the activity on 4-nitrophenyl beta-D-glucopyranoside
I48W
decreased activities towards 4-nitrophenyl beta-D-glucopyranoside, hydrolysis activity on sophorose, which is much higher than the activity on 4-nitrophenyl beta-D-glucopyranoside
I48W/I278F/T484Y
decreased activities towards 4-nitrophenyl beta-D-glucopyranoside, hydrolysis activity on sophorose, which is much higher than the activity on 4-nitrophenyl beta-D-glucopyranoside
T484Y
decreased activities towards 4-nitrophenyl beta-D-glucopyranoside, hydrolysis activity on sophorose, which is much higher than the activity on 4-nitrophenyl beta-D-glucopyranoside
W69I
mutant enzyme shows no activity with 4-nitrophenyl beta-D-glucopyranoside
Y509T
introduction of mutation Y509T causes the increase of the Km value, but does not affect the kcat value
I278F
-
decreased activities towards 4-nitrophenyl beta-D-glucopyranoside, hydrolysis activity on sophorose, which is much higher than the activity on 4-nitrophenyl beta-D-glucopyranoside
-
I48W
-
decreased activities towards 4-nitrophenyl beta-D-glucopyranoside, hydrolysis activity on sophorose, which is much higher than the activity on 4-nitrophenyl beta-D-glucopyranoside
-
I48W/I278F/T484Y
-
decreased activities towards 4-nitrophenyl beta-D-glucopyranoside, hydrolysis activity on sophorose, which is much higher than the activity on 4-nitrophenyl beta-D-glucopyranoside
-
T484Y
-
decreased activities towards 4-nitrophenyl beta-D-glucopyranoside, hydrolysis activity on sophorose, which is much higher than the activity on 4-nitrophenyl beta-D-glucopyranoside
-
W69I
-
mutant enzyme shows no activity with 4-nitrophenyl beta-D-glucopyranoside
-
Y509T
-
introduction of mutation Y509T causes the increase of the Km value, but does not affect the kcat value
-
R572K
mutation in residue important for substrate recognition, 10fold increase in Km value for sophorose
R572K
Listeria innocua Clip11262 ATCC BAA-680
-
mutation in residue important for substrate recognition, 10fold increase in Km value for sophorose
-
E176A
-
inactive under standard assay conditions, mutant can be rescued by (small nucleophiles) acetate and azide but not as mutant E176Q
E176D
-
inactive under standard assay conditions, mutant can not be rescued by any small nucleophile
E176Q
-
E176Q active site mutant can be effectively rescued by small nucleophiles, such as acetate, azide and ascorbate, for hydrolysis of aryl glycosides in a pH-independent manner above pH 5. Cellotriose, cellotetraose, cellopentaose, cellohexaose and laminaribiose are not hydrolyzed by the mutant and instead exhibit competitive inhibition
E172A
site-directed mutagenesis, inactive catalytic residue mutant
E370A
site-directed mutagenesis, inactive catalytic residue mutant
D229N
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A
D229N/K253A
site-directed mutagenesis, mutation of the isozyme BGL1A residues from subsite +1 to the correspondent residues of isozyme BGL1B, the double mutant has a hydrolytic activity at neutral pH that is restored to that of the wild-type enzyme
H231D
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A
K253A
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A
M177L
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows catalytic efficiency similar to the wild-type BGL1A
V173C
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows catalytic efficiency similar to the wild-type BGL1A
E446N
beta-fucosidase activity is 26.49% compared to wild-type activity, beta-glucosidase activity is 21.37% compared to wild-type activity, beta-galactosidase activity is 15.7% compared to wild-type activity
N172A
beta-fucosidase activity is 18.38% compared to wild-type activity, beta-glucosidase activity is 17.65% compared to wild-type activity, beta-galactosidase activity is 13.4% compared to wild-type activity
E417S
mutant with reduced pH optimum, increased Km and turnover number for 2-nitrophenyl-beta-1,4-D-glucopyranoside
F426Y
mutant with unchanged pH optimum, slight increased Km and slight reduced turnover number for 2-nitrophenyl-beta-1,4-D-glucopyranoside
M424K
mutant with increased pH optimum, slight increased Km and reduced turnover number for 2-nitrophenyl-beta-1,4-D-galactopyranoside
R170A/R220A/Y227F/R448E
mutant enzyme occurs as monomer, melting temperature is decreased form 110°C for the wild-type enzyme to 73-75°C for the mutant enzyme
R170A/R220A/Y227F/R449R
mutant enzyme occurs as monomer, melting temperature is decreased form 110°C for the wild-type enzyme to 73-75°C for the mutant enzyme
R170A/R220A/Y227F/R459G
mutant enzyme occurs as monomer, melting temperature is decreased form 110°C for the wild-type enzyme to 73-75°C for the mutant enzyme
F198A
F471Y
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
G464F
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
G464S
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
G464S/S465L
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
S465L
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
Y378A
site-directed mutagenesis, the mutant shows 300-380% increased catalytic eficiency with substrates 2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one and 2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one, respectively
Y378F
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
A375P
-
Km (2-nitrophenyl beta-D-glucopyranoside) decreased compared to wild-type, kcat (2-nitrophenyl beta-D-glucopyranoside) decreased. Relative efficacy toward (2-nitrophenyl beta-D-glucopyranoside) similar to wild-type. Km (dhurrin) similar to wild-type, kcat drastically decreased
F469Y
-
Km (2-nitrophenyl beta-D-glucopyranoside) increased compared to wild-type, kcat (2-nitrophenyl beta-D-glucopyranoside) decreased. Relative efficacy toward (2-nitrophenyl beta-D-glucopyranoside) significantly decreased by factor 2.5. Km (dhurrin) similar to wild-type, kcat drastically decreased
V196F/L203F
-
Km (2-nitrophenyl beta-D-glucopyranoside) decreased compared to wild-type, kcat (2-nitrophenyl beta-D-glucopyranoside) decreased. Relative efficacy toward (2-nitrophenyl beta-D-glucopyranoside) similar to wild-type. Km (dhurrin) similar to wild-type, kcat drastically decreased
E190Q
mutant construcuted for analysis of the relative contribution of the residue to specificity and catalysis. E190 favors the binding of the initial portion of alkyl-type aglycones
E194A
mutant construcuted for analysis of the relative contribution of the residue to specificity and catalysis. E190 favors the binding of the initial portion of alkyl-type aglycones
E451A
-
the double mutant shows decreased activity compared to the wild type enzyme
E451S
-
the double mutant shows decreased activity compared to the wild type enzyme
K201A
mutant construcuted for analysis of the relative contribution of the residue to specificity and catalysis. K201 is relevant for binding of D-glucose units
K201F
mutant construcuted for analysis of the relative contribution of the residue to specificity and catalysis. K201 is relevant for binding of D-glucose units
M453A
mutant construcuted for analysis of the relative contribution of the residue to specificity and catalysis. M453 favors the binding of the second D-glucose unit of oligosaccharidic aglycones
Q39E
-
the double mutant shows decreased activity compared to the wild type enzyme
Q39E/E451A
-
the double mutant shows decreased activity compared to the wild type enzyme
Q39E/E451S
-
the double mutant shows decreased activity compared to the wild type enzyme
Q39N
-
the double mutant shows decreased activity compared to the wild type enzyme
Q39N/E451S
-
the double mutant shows decreased activity compared to the wild type enzyme
E178A
-
3500fold reduction in catalytic efficiency, E178 ist the general acid/base catalyst of Bgl3
E383Q
-
1000000fold reduction in catalytic efficiency, E383 is the catalytic nucleophile of Bgl3
A433V
-
random mutagenesis, identification of the thermostable mutant, kinetics in comparison to the wild-type enzyme
L444F
-
random mutagenesis, identification of the thermostable mutant, kinetics in comparison to the wild-type enzyme
N178I
-
random mutagenesis, identification of the thermostable mutant, substrate-saturation study, binding of a second substrate molecule increases the turnover with D-cellobiose
N317Y
-
random mutagenesis, identification of the thermostable mutant, kinetics in comparison to the wild-type enzyme
N317Y/L444F
-
random mutagenesis, identification of the thermostable mutant, substrate-saturation study, binding of a second substrate molecule increases the turnover with D-cellobiose
N317Y/L444F/A422V
-
random mutagenesis, identification of the thermostable mutant, substrate-saturation study, binding of a second substrate molecule increases the turnover with D-cellobiose
N439S
-
random mutagenesis, identification of the thermostable mutant, kinetics in comparison to the wild-type enzyme
S319C
-
random mutagenesis, identification of the thermostable mutant, the mutant shows highly increased thermotolerance and activity with D-cellobiose compared to the wild-type enzyme
D206N
catalytically active mutant enzyme, similar temperature optimum like wild-type enzyme. The high-catalytic turn-over rate by D206N for beta-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures
D206Q
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides
Q77R
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides
N62Y/Q63K/L231F/V303A/A412V
mutations observed in all the clones isolated
N62Y/Q63K/L231F/V303A/E386G/A412V
additional mutation in nucleophile residue E386, mutation completely abolishes activity. The addition of 2 M sodium formate as an external nucleophile leads to the recovery of 4.60% activity with accumulation of oligosaccharides. At pH 3.0 and low concentrations of sodium formate buffer, the hyperthermophilic glycosynthase shows kcat values similar to those of the wild-type and 17fold higher than those observed at the usual reactivation conditions in 2 M sodium formate at pH 6.5
D242G
mutant loses 96% of wild-type activity, activity is partially restored after addition of NaN3
D58A
dramatic decrease in kcat compared to wild-type, activity is highly recovered after addition of NaN3
E458G
dramatic decrease in kcat compared to wild-type, activity is partially restored after addition of NaN3
F224I
mutation the aglycone binding region, flavonoid glucoside hydrolysis is not affected
F310E
mutation the aglycone binding region, flavonoid glucoside hydrolysis is not affected
F310L
mutation the aglycone binding region, flavonoid glucoside hydrolysis is not affected
N220S
mutation the aglycone binding region, increases the catalytic efficiency on both quercetin 3-glucoside and 4-nitrophenyl-beta-D-glucoside
N221S
mutation the aglycone binding region, increases the catalytic efficiency on both quercetin 3-glucoside and 4-nitrophenyl-beta-D-glucoside
W243F
Km (4-nitrophenyl beta-D-glucopyranoside) close to wild-type, kcat decreased to 34% compared to wild-type
W322A
mutation the aglycone binding region, residue is important for substrate accomodation. Mutation W322A results in a large reduction of hydrolytic activity on 3-glucosylated flavonoids
F224I
-
mutation the aglycone binding region, flavonoid glucoside hydrolysis is not affected
-
F310L
-
mutation the aglycone binding region, flavonoid glucoside hydrolysis is not affected
-
N220S
-
mutation the aglycone binding region, increases the catalytic efficiency on both quercetin 3-glucoside and 4-nitrophenyl-beta-D-glucoside
-
W322A
-
mutation the aglycone binding region, residue is important for substrate accomodation. Mutation W322A results in a large reduction of hydrolytic activity on 3-glucosylated flavonoids
-
P172L/L167W
the enzyme has mutations on the left wall of the substrate binding site and shows decreased sensitivity of the catalytic activity to pH and, thus, the pH profile for optimal activity is expanded from pH 6.0 to a pH range from pH 5.0 through pH 7.0
E191A
site-directed mutagenesis, inactive TaGlu1a mutant
E407A
site-directed mutagenesis, inactive TaGlu1a mutant
F198A
site-directed mutagenesis, the TaGlu1a mutant shows reduced activity with substrates 2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one and 2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one with highly incresed Km values, respectively
D772A
the mutant shows less than 1/10000 activity of the wild type enzyme
N223Q
mutation results in reduced glucose tolerance and transglycosylation activity, and drastically changed substrate specificity
N223Y
mutation results in reduced glucose tolerance and transglycosylation activity, and drastically changed substrate specificity
D261N
the D261N substitution leads to a drastic decrease in relative efficiency of ZmGlu1 on all substrates tested, but little effect on the Km
E191D/F198V
inactive mutant, F198 substitution causes a rearrangement of residues F205, F466, and E464 involved in aglycone binding
F193A
increase in affinity for a small polar aglycone, deep decrease in kcat value. 7.8% of wild-type activity for substrate 4-nitrophenyl-beta-D-glucoside, 3% for substrate 4-methylumbelliferyl-beta-D-glucoside, respectively
F193A/F200K/W373K/F461L
almost complete loss of catalytic activity, extensive alterations in strucutre
F198V
mutant shows drastic effect on catalytic efficacy, kcat is reduced by 90% for hydrolysis of 4-methylumbelliferyl beta-D-glucopyranoside compared to wild-type. Mutant is unable to hydrolyze 4-nitrophenyl beta-D-glucopyranoside. Only negligible activity toward substrate 2-nitrophenyl beta-D-glucopyranoside compared to wild-type
F198V/F205L/P377A
mutant shows a drastic reduced relative efficacy for all test substrated due to a decreased turnover
F200K
1.1% of wild-type activity for substrate 4-nitrophenyl-beta-D-glucoside, 0.3% for substrate 4-methylumbelliferyl-beta-D-glucoside, respectively
F205L
Mutant shows similar relative efficacy compared to wild-type toward all substrates tested. Mutant shows no significant effect on hydrolysis of 4-nitrophenyl beta-D-glucopyranoside other than doubling the kcat value compared to wild-type
F461L
120% of wild-type activity for substrate 4-nitrophenyl-beta-D-glucoside, 119% for substrate 4-methylumbelliferyl-beta-D-glucoside, respectively
F466S
mutant exhibits a marked increase in relative efficiency in comparison to wild-type ZmGlu1 on all substrates tested (from 28 to 123%), because of increased substrate turnover. Mutant has little effect on dhurrin hydrolysis compared to wild-type (3% of relative efficacy compared to Sorghum Dhr1)
F466S/A467S
the A467S substitution in ZmGlu1 has no detectable effect on substrate specificity and catalytic efficiency in the case of 4-nitrophenyl beta-D-glucopyranoside or 2-nitrophenyl beta-D-glucopyranoside hydrolysis, and only a lower Km is obtained for 4-methylumbelliferyl beta-D-glucuronide compared to mutant F466S. Mutant has little effect on dhurrin hydrolysis compared to wild-type (3% of relative efficacy compared to Sorghum Dhr1)
K81E
mutant not able to bind chimeric lectin beta-glucosidase aggregating factor
M263F
mutant shows reduced relative efficacy by 40 to 50% on 4-nitrophenyl beta-D-glucopyranoside and 4-methylumbelliferyl beta-D-glucopyranoside whereas it shows an increase of about 60% relative efficacy on 2-nitrophenyl beta-D-glucopyranoside compared to wild-type
N481E
mutant with lowered affinity to cimeric lectin beta-glucosidase aggregating factor
P377A
P377A mutation leads to changes (decreases) in both kcat and Km for all substrated with no decrease in the overall relative efficiency
T82Y
mutant not able to bind chimeric lectin beta-glucosidase aggregating factor
W373K
large decrease in kcat value. 0.5% of wild-type activity for substrate 4-nitrophenyl-beta-D-glucoside, 0.04% for substrate 4-methylumbelliferyl-beta-D-glucoside, respectively
Y473F
kcat is increased by 110% to 450% depending on the substrate tested. Enhanced turnover is compensated by a slight increase in Km of this mutant giving a 40% to 250% (depending on the substrate tested) better relative efficacy over the wild-type enzyme. Mutation leads to a significant effect towards dhurrin hydrolysis (10% relative efficacy as compared to Sorghum Dhr1)
additional information
L178E
H0HC94
specific activity is1.8 times increased on substrate cellobiose
L178E
-
specific activity is1.8 times increased on substrate cellobiose
-
F198A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
F198A
site-directed mutagenesis, the mutant shows 24-28fold reduced activity with substrates 2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one and 2-O-beta-D-glucopyranosyl-4-hydroxy-7-demethoxy-1,4-benzoxazin-3-one, respectively
additional information
-
construction of chimeric enzymes between Thermotoga maritima and Agrobacterium tumefaciens beta-glucosidases, three chimeric genes are constructed by shuffling at three selected regions, only two chimeric enzymes are active and show altered properties, e.g. decreased thermal stability, pH optima, and kinetics, overview
additional information
-
construction of chimeric enzymes between Thermotoga maritima and Agrobacterium tumefaciens beta-glucosidases, three chimeric genes are constructed by shuffling at three selected regions, only two chimeric enzymes are active and show altered properties, e.g. decreased thermal stability, pH optima, and kinetics, overview
-
additional information
construction of a lactic-acid producing Saccharomyces cerevisiae strain expressing isoform Bgl1 on cell surface by fusing the mature protein to the C-terminal half region of alpha-agglutinin. Strain is able to grow on cellobiose and glucose minimal medium at the same rate. The maximum rate of L-lactate production on cellobiose is 2.8 g per l and similar to that on glucose
additional information
-
construction of a lactic-acid producing Saccharomyces cerevisiae strain expressing isoform Bgl1 on cell surface by fusing the mature protein to the C-terminal half region of alpha-agglutinin. Strain is able to grow on cellobiose and glucose minimal medium at the same rate. The maximum rate of L-lactate production on cellobiose is 2.8 g per l and similar to that on glucose
additional information
-
rapid construction of a library of mutant BGL1 from Aspergillus oryzae by yeast cell surface engineering
additional information
co-expression of beta-glucosidase and endoglucanase in Saccharomyces cerevisiae. Ethanol fermentation from 20 g per l barley beta-glucan with the co-displaying strain reaches 7.94 g per l ethanol after 24 h of fermentation. The conversion rate of ethanol is 69.6% of the theoretical ethanol concentration
additional information
-
co-expression of beta-glucosidase and endoglucanase in Saccharomyces cerevisiae. Ethanol fermentation from 20 g per l barley beta-glucan with the co-displaying strain reaches 7.94 g per l ethanol after 24 h of fermentation. The conversion rate of ethanol is 69.6% of the theoretical ethanol concentration
additional information
-
swapping analysis of isoforms AsGlu1 and AsGlu2 shows that the C-terminal segment of AsGlu1 is critical for fibrillar multimerization
additional information
-
mutant strain 51 SMr is resistant to streptomycin and deoxyglucose, the mutation partially stabilizes the beta-glucosidase
additional information
-
the deoxyglucose- and streptomycin-resistant mutant strain shows 1.2-1.5fold higher thermostability and resistance against 4 M urea, and has a lower activation energy compared to the of parent wild-type strain NIAB 442
additional information
construction of inactive Cba3 deletants lacking either the N-terminal 10 amino acids or the C-terminal 10 residues
additional information
-
construction of inactive Cba3 deletants lacking either the N-terminal 10 amino acids or the C-terminal 10 residues
-
additional information
-
mutant strain PN-120 produces a beta-glucosidase that is 10fold more active with a 3fold higher affinity for cellobiose than the corresponding enzyme isolated from the parental strain, the mutation of strain PN-120 affects the catalytic site
additional information
-
naturally occurring deletion mutantions involved in Gaucher's disease development with reduced enzyme activity
additional information
-
isolation of isoforms beta-glu 1 and beta-glu 2 from hypercellulolytic Pol6 mutant
additional information
-
immobilization of the enzyme on chitosan-clay composite, crosslinking with glutaraldehyde, kinetic modeling of thermal inactivation and reactivity, overview
additional information
-
fusion of BGL1 to the cellulose-binding domain CBD2 of Trichoderma reesei cellobiohydrolase CBHII, recombinant enzymes are constructed with single and double copies of CBD2 fused at the N-terminus of BGL1 to mimic the two-domain organization displayed by cellulolytic enzymes in nature, the mutant shows a 2-4fold increased activity compared to the wild-type enzyme
additional information
-
to study the mechanism of substrate specificity further, eight chimeric beta-glucosidases are constructed by replacing peptide sequences within the C-terminal region of Zea mays Glu1 with the homologous peptide sequences of Sorghum Dhr1 or vice versa. Replacing the peptide 466FAGFTERY473 of Zea mays Glu1 with the homologous peptide 462SSGYTERF469 of Sorghum Dhr1 or replacing the peptide 481NNNCTRYMKE490 in Glu1 with the homologous peptide 477ENGCERTMKR486 of Dhr1 is sufficient to confer to Zea mays Glu1 the ability to hydrolyze dhurrin
additional information
-
construction of chimeric enzymes between Thermotoga maritima and Agrobacterium tumefaciens beta-glucosidases, three chimeric genes are constructed by shuffling at three selected regions, only two chimeric enzymes are active and show altered properties, e.g. decreased thermal stability, pH optima, and kinetics, overview
additional information
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
construction of chimeric enzymes between Thermotoga maritima and Agrobacterium tumefaciens beta-glucosidases, three chimeric genes are constructed by shuffling at three selected regions, only two chimeric enzymes are active and show altered properties, e.g. decreased thermal stability, pH optima, and kinetics, overview
-
additional information
mutations in within residues S1 to T29 show no effect on binding of chimeric lectin beta-glucosidase aggregating factor
additional information
-
mutations in within residues S1 to T29 show no effect on binding of chimeric lectin beta-glucosidase aggregating factor
additional information
-
to study the mechanism of substrate specificity further, eight chimeric beta-glucosidases are constructed by replacing peptide sequences within the C-terminal region of Zea mays Glu1 with the homologous peptide sequences of Sorghum Dhr1 or vice versa. Replacing the peptide 466FAGFTERY473 of Zea mays Glu1 with the homologous peptide 462SSGYTERF469 of Sorghum Dhr1 or replacing the peptide 481NNNCTRYMKE490 in Glu1 with the homologous peptide 477ENGCERTMKR486 of Dhr1 is sufficient to confer to Zea mays Glu1 the ability to hydrolyze dhurrin
additional information
creation of chimeric mutants (Chim21 and Chim16) which are produced by reciprocal domain-swapping between ZmGlu1 and (Sorghum) SbDhr1: ZmGlu1 hydrolyzes dhurrin with a lower catalytic efficiency only when a C-terminal octapeptide 466-477 is exchanged with the homologous octapeptide of SorghumDhr1 (462-469). This peptide substitution leading to amino acid substitutions at four sites is found in Chim21 and Chim16 (with an extra 22 amino acids substitution) enables ZmGlu1 to hydrolyze dhurrin with less than 10% of the relative efficiency of SorghumDhr1 (7.4% for Chim21 and 9.5% for Chim16)
additional information
-
creation of chimeric mutants (Chim21 and Chim16) which are produced by reciprocal domain-swapping between ZmGlu1 and (Sorghum) SbDhr1: ZmGlu1 hydrolyzes dhurrin with a lower catalytic efficiency only when a C-terminal octapeptide 466-477 is exchanged with the homologous octapeptide of SorghumDhr1 (462-469). This peptide substitution leading to amino acid substitutions at four sites is found in Chim21 and Chim16 (with an extra 22 amino acids substitution) enables ZmGlu1 to hydrolyze dhurrin with less than 10% of the relative efficiency of SorghumDhr1 (7.4% for Chim21 and 9.5% for Chim16)
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 7
the activity drops by 50% at pH 2.5 and 6.0, and is negligible from pH 7.0 upward
706319
3 - 10
3 - 7
3 - 8
3 - 9
3.3 - 10.3
-
fairly stable, 90% of the original activity retains after incubation at 4°C for 16 h
710240
3.5
42% of the initial activity for the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde remains, the activity of free enzyme is completely lost
746352
3.5 - 4
90°C, 1 or 2 h, more than 80% of the maximum activity is retained
728007
3.5 - 7
3.5 - 8.5
-
approx. 30% loss of activity after 2 h at pH 3.5 and 30°C, approx. 20% loss of activity after 2 h at pH 8.5 and 30°C
655773
4 - 10
4 - 4.5
4 - 6
4 - 6.5
4 - 7
4 - 8
4 - 9
4.5 - 6
4.5 - 8
5 - 10
5 - 6
5 - 7
5 - 7.5
5 - 8
5 - 8.5
mutated recombinant beta-glucosidase is fairly stable at pH 5.0 and 8.5, exhibiting 60 and 62% activities, respectively. It retains over 50% of the original activity between pH 4-7.5. Between pH values 6.0 and 7.2, it retains over 98% activity after incubation at 37°C for 2 h
696166
5 - 9
6
beta-glucosidase TpBGL1 shows higher stability at pH 6 than at pH 4
746720
6 - 12
-
complete loss of activity below pH 6.0 after 4 h at 20°C, 37% loss of activity after 4 h at pH 12.0 and 20°C
655770
6 - 7.5
6 - 8
6 - 9
3 - 10
-
the enzyme retains about 60% activity at pH 3-6 and only 20% activity at pH 10
763210
3 - 10
about 60% activity at pH 3.0, about 80% activity at pH 4.0, the enzyme is stable at pH 5.0-9.0, activity drops sharply at pH 10.0
702747
3 - 7
no activity at pH 3.0 and 7.0, about 20% activity at pH 4.0, about 40% activity at pH 6.0
701871
3 - 8
-
increase of enzyme activity with pH increase, above 8 decrease of enzyme activity with increasing pH
702988
3 - 9
-
40% loss of activity after 24 h at 0°C and pH 3.0, approx. 20% loss of activity after 24 h at 0°C and pH 4.0-9.0
654873
3 - 9
-
40% loss of activity after 24 h at 0°C and pH 3.0, approx. 205 loss of activity after 24 h at 0°C and pH 4.0-9.0
654873
4
-
incubation at pH 4.0 leads to 43.3-44.2% residual activity compared to the activity at pH 6.0
701455
4
-
incubation at pH 4.0 leads to 79.4% residual activity compared to the activity at pH 6.0
701455
4
-
incubation at pH 4.0 leads to 62.4% residual activity compared to the activity at pH 6.0
701455
4
-
incubation at pH 4.0 leads to 98.4% residual activity compared to the activity at pH 6.0
701455
4
-
incubation at pH 4.0 leads to 27% residual activity compared to the activity at pH 6.0
701455
4
-
incubation at pH 4.0 leads to 119.6% residual activity compared to the activity at pH 6.0
701455
4
-
incubation at pH 4.0 leads to 79.7-89.6% residual activity compared to the activity at pH 6.0
701455
4
-
incubation at pH 4.0 leads to 88.5% residual activity compared to the activity at pH 6.0
701455
4
-
incubation at pH 4.0 leads to 45.1% residual activity compared to the activity at pH 6.0
701455
4 - 6
-
about 80% of the relative activity at 45°C is retained at both pH 4.0 and 5.0. 5% activity at pH 3.5
715222
4 - 6
stable in the range of pH 4.0 to 6.0 while outside this pH range no residual activity is measured, at 65°C the residual activity is 50% at pH 5.0 and 6.0 (after 24 h) and 20% at pH 4.0
701870
4 - 6.5
-
the enzyme activity remains more than 70% after incubating at pH 4.0-6.5 at 4°C for 24 h
705193
4 - 7
-
the free enzyme is stable at pH 7.0 (half-life of 50 days) but not at pH 4.0 (half-life of 4 days)
704235
4 - 8
native and recombinant enzyme are stable over a broad pH range of 4.0-8.0 with maximum retention of their catalytic activity. However, activities decline quickly below pH 4.0
751822
4.5 - 6
the enzyme is unstable below pH 6.0, at pH 6.0 its half-life at 75°C is 28 days but at pH 4.5 is 13 h
702822
4.5 - 6
-
stable within, soluble and immobilized enzyme preparations
326305
5 - 10
37°C, 1 h, enzyme retains more than 80% activity
739692
5 - 6
Melanocarpus sp.
-
purified enzyme, stable
679482
5 - 8
37°C, 1 h incubation, the enzyme retains more than 80% of its maximum activity
724664
5 - 9
-
rapid inactivation below and above for cellulose-immobilized Cex-cellulose-binding domain fused to beta-glucosidase
326302
5 - 9
37°C, 1 h, enzyme retains more than 80% activity
739692
5 - 9
-
residual activity is 80-100% between pH ranges 5.0-8.0, the stability of the enzyme in mycelia extract is comparatively low at acidic pH and the enzyme is most stable at pH 9.0, the purified enzyme shows more than 95% residual activity between pH ranges 6.0-7.0
702717
8
the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde retains 79.6% of the initial activity underalkaline conditions (pH 8.0), which is higher by 32% compared with native enzyme
746352
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
the enzyme is stable from 10-30°C, about 75% activity at 40°C, about 30% activity at 50°C, almost inactive at 50°C
100
15
the enzyme is stable at temperatures lower than 15°C, as it retains 70% of the original activity after incubation at pH 7.5 and 15°C for 1 h
20 - 40
25 - 45
-
the enzyme displays good stability when it is kept at 25 and 37°C, with approximate half-lives of 160 and 3.5 h, respectively. When the enzyme is kept at 45°C, less than 5% of initial activity is detectable after 30 min
25 - 75
-
comparison of thermostability of the parent wild-type and the mutant strain at 25-75°C over 15 min
30
30 - 120
the enzyme retains more than 80% of its maximum activity from 30°C to 120°C
30 - 40
30 - 70
-
under pH 4.5, the relative activity of beta-glucosidase at 30°C and 60°C is about 44% and 40%. After incubation at 70°C and pH 4.5 for 1 h, beta-glucosidase still retains about 85% of its original activity
35
37
37 - 45
-
enzyme is stable at temperatures lower than 37°C, and about 32% of the activity is lost after incubation at 45°C for 30 min
37 - 55
-
the purified beta-glucosidase is stable for 100 min at 37°C, but unstable at 55°C with half-life of 20 min, complete loss of activity occurs after 120 min at 55°C
40
40 - 50
enzyme activity decreases rapidly during the first 10 min and then gradually decreases to about 30% until 60 min when incubated at 40-50°C
40 - 80
40 - 85
-
after 40 h at 40°C, 50°C, 60°C and 70°C, the enzyme shows about 90%, 25%, 25% and less than 5% activity, respectively. The half-lifes of the free enzyme are 2, 8, and 12 h at 70°C, 60°C, and 50°C. When the temperature increases to 85°C, the enzyme loses its activity in 30 min
41 - 70
-
chimeric beta-glucosidase No. 6 is stable up to 60°C, chimeric beta-glucosidase No. 8 is stable up to 70°C above which activity decreases, the heat stability of the wild type enzyme is at 41°C
42
is fairly stable in 50 mM sodium acetate buffer, pH 5.6, at temperatures up to 42°C, while retaining only 48% of the original activity at 50°C for 10 min. It is completely inactivated upon incubation at 60°C for 10 min
45
50
50 - 60
Thermochaetoides thermophila
-
no loss of activity after 2 h, deglycosylated beta-glucosidase, 50% loss of activity after 18 min
54
Thermochaetoides thermophila
-
completely stable cell-bound cellobiase, cell-bound aryl-beta-glucosidase loses 50% of its activity in 5 h
55
55 - 60
-
the purified enzyme is thermostable up to 60 min in water at 55°C and shows half-lives of 7 and 14 min when incubated in the absence or presence of 50 mM D-glucose, respectively, at 60°C
60
60 - 80
the half-lives of the enzyme at 60, 70, and 80°C are 250, 24.3, and 0.4 h
60 - 85
-
the enzyme is sensitive to heat, activity is decreasing slowly between 60 and 80°C, and significantly at 85°C
60 - 87
-
chimeric beta-glucosidase No. 6 is stable up to 60°C, chimeric beta-glucosidase No. 8 is stable up to 70°C, above which activity decreases, the heat stability of the wild type enzyme is at 41°C
60 - 90
-
about 50% activity at 60°C, about 30% activity at 70°C, about 10% activity at 80°C, no activity at 90°C
65
70
70 - 80
mutant enzymes R170A/R220A/Y227F/R448E, R170A/R220A/Y227F/R449R or R170A/R220A/Y227F/R459G are immediately inactivated
73 - 75
melting temperature of mutant enzymes R170A/R220A/Y227F/R448E, R170A/R220A/Y227F/R449R or R170A/R220A/Y227F/R459G
75
80
80 - 90
at temperatures between 80 and 90°C, beta-glucosidase TpBGL1 is more unstable at pH 4 than pH 6
85
85 - 90
the enzyme retains nearly 100% of its original activity over 120 min of incubation
90
95
additional information
100
beta-glucosidase TpBGL1 at pH 6 can not be completely unfolded at 100°C. At pH 4 TpBGL1 drastically loses regular secondary structure at temperatures higher than 80°C with a complete unfolding at 100°C. At both pH values, the processes are essentially irreversible
100
beta-glucosidase TpBGL3 can be thermally denatured at pH 4 and at pH 6, the process is irreversible
20 - 40
the enzyme is most stable at 20°C to 30°C, and begins to lose activity after 40 min at 40°C or higher
30 - 40
-
stable at 30°C retaining 90% of the original activity for more than 24 h, after 3 h of incubation at 40°C the enzyme retains 50% of its activity, after 1 h of incubation at 50°C the enzyme retains 57% of its activity
30 - 40
-
stable at 30°C retaining 90% of the original activity for more than 24 h, after 3 h of incubation at 40°C the enzyme loses 70-85% of its activity, after 1 h of incubation at 50°C the enzyme retains 20% of its activity
30 - 40
-
stable at 30°C retaining 90% of the original activity for more than 24 h, after 3 h of incubation at 40°C the enzyme loses 70-85% of its activity, after 1 h of incubation at 50°C the enzyme retains 43% of its activity
30 - 40
-
stable within this range, rapid decrease in activity below 30°C and above 40°C
4
-
beta-glucosidases B and C, stored at 4°C for several months without loss of activity
40
purified recombinant His-tagged enzyme, 30 min, 80% remianing activity
40 - 80
the purified enzyme shows a half-life of 10 h at 65°C, about 20% activity at 40°C, about 60% activity at 50°C, about 90% activity at 60°C, about 80% activity at 70°C, less than 20% activity at 80°C
40 - 80
-
the purified enzyme has about 80% and 46% residual activities at 60°C and 80°C, unpurified mycelia extract enzyme has 86%, 60% and 22% residual activities at 40°C, 60°C, and 80°C, respectively. The thermal stability 70°C is 64%
50
-
half-life: 22-24 min, 2fold enhanced stability of Gaucher disease liver enzyme compared to control liver
50
-
enzyme from mutant strain stable up to for 30 min, wild-type enzyme retains 75% of its initial activity
50
-
after 15 min at various temperatures ranging from 30 to 70°C, the original activity retained up to 50°C
50
-
half-life of the free enzyme is 44.9 min, of the dried-composite immobilized enzyme 134.2 min, and of the wet-composite immobilized enzyme 135.7 min
55
-
purified enzyme, 4 h, pH 3.5, stable up to, rapid decrease in activity above
55
-
half-life of the free enzyme is 28.4 min, of the dried-composite immobilized enzyme 88.0 min, and of the wet-composite immobilized enzyme 101.1 min
55
loses 90% after 3 min, indicating the RuBGX1 is a mesophilic enzyme
60
-
purified recombinant and native enzymes, stable up to for 50 min
60
-
stable at temperatures below 60°C. The half-lives of the purified enzyme at 30, 40, 50, 60 and 70°C are 141.4, 90.0, 58.7, 27.1 and 1.4 h, respectively
60
-
half-life of the healthy leukocyte enzyme is 3.5 min, of the healthy fibroblast 3 min, and half-life of the Gaucher's disease enzyme from leukocyte is about 6 min, and from fibroblast 3 min, thermostability, overview
60
-
heat stability of wild-type and mutant enzymes at 60°C, overview, the wild-type enzyme is inactivated within 1 min, homozygote mutants are inactive after 2 min, heterozygotes after 2-4 min
60
-
extracellular enzyme: 25% loss of activity in 1 h, intracellular enzyme: 80% loss of activity in 1 h
60
no loss in activity after 24 h of incubation at 60°C at pH 4-6
60
-
half-life of the free enzyme is 13.4 min, of the dried-composite immobilized enzyme 78.3 min, and of the wet-composite immobilized enzyme 45.7 min
60
purified His-tagged recombinant enzyme, rapid loss of activity
60
-
stable for 1 h, immobilized enzyme shows better stability
60
-
the enzyme is very stable at 60°C displaying a half-life of 855.6 min but it is easily denatured above this temperature
60
loses 90% after 3 min, indicating the RuBGX1 is a mesophilic enzyme
65
-
the half-life at 65°C without Ca2+ is 35 min, the half-life at 65°C wit Ca2+ is 70 min
65
-
half-life of the free enzyme is 1.1 min, of the dried-composite immobilized enzyme 7.4 min, and of the wet-composite immobilized enzyme 9.5 min
70
1 h, the native enzyme retains 67% of its activity while the recombinant enzyme preserves 35%
70
-
totally stable up to, retaining 70% of its activity after 1 h incubation at 75°C
75
-
heating the crude extract to 75°C for 5 min leads to 0.5-2.9% residual activity
75
-
heating the crude extract to 75°C for 5 min leads to 5.7% residual activity
75
-
heating the crude extract to 75°C for 5 min leads to 6.4% residual activity
75
-
heating the crude extract to 75°C for 5 min leads to 2.1% residual activity
75
-
heating the crude extract to 75°C for 5 min leads to 7.4% residual activity
75
-
heating the crude extract to 75°C for 5 min leads to 6.8% residual activity
75
-
heating the crude extract to 75°C for 5 min leads to 4.4-29.1% residual activity
75
-
heating the crude extract to 75°C for 5 min leads to 10.5% residual activity
75
-
heating the crude extract to 75°C for 5 min leads to 8.0% residual activity
75
-
heating the crude extract to 75°C for 5 min leads to 12.6% residual activity
75
-
sharp decline of activity above, increase thermostability by addition of DTT and/or divalent cations
80
the recombinant enzyme retains 30% of maximal activity after 25 min
80
-
pH 5.5, 1 h, immobilized enzyme, no loss of activity in absence of substrate
80
at pH 4 the ellipticity at 222 nm of beta-glucosidase TpBGL1 remains relatively constant at temperatures lower than 80°C. A progressive decrease is observed when the temperature is increased above 80°C
80
enzyme shows high thermostability not losing its activity at 80°C for 2 h in 0.05 M Na-phosphate buffer of pH 6.8 with Tm of 100.0°C in 0.02 M Tris-HCl buffer of pH 8.2
85
about 45% loss of activity after 8 h, about 60% loss of activity after 24 h
85
7 h, 84% of the residual activity of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde is retained, 63% of the residual activity of the native enzyme is retained. The temperature stability of the immobilized enzyme is better than that of the free enzyme
90
-
pH 5.5, 1 h, immobilized enzyme, 30% loss of activity in absence of substrate
90
-
pH 5.5, 1 h, immobilized enzyme, 72% loss of activity in absence of substrate
90
pH 3.5-4.5, 1 or 2 h, more than 80% of the maximum activity is retained
90
for beta-glucosidase TpBGL3 at both pH 6 and 4, the ellipticities at 222 nm remain relatively constant at temperatures lower than 90°C. A decrease in the ellipticities at 222 nm is observed at temperatures higher than 90°C, suggesting a loss of regular secondary structure, the process is irreversible
additional information
-
thermoinactivation followed first-order kinetics, overview
additional information
thermostability is improved in presence of cellobiose, glucose, or sucrose
additional information
-
thermostability is improved in presence of cellobiose, glucose, or sucrose
additional information
-
thermal inactivation kinetics of free and immobilized enzyme, overview
additional information
hyperthermostable native enzyme, thermostability is even increased by immobilization on gelatin
additional information
-
hyperthermostable native enzyme, thermostability is even increased by immobilization on gelatin
additional information
oligomerization contributes to thermostability
additional information
-
thermoinactivation followed first-order kinetics, overview
additional information
-
thermostability of wild-type and mutant enzymes, overview
additional information
most heat stable under extremely acidic conditions, pH 3.5
additional information
-
most heat stable under extremely acidic conditions, pH 3.5
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin required for stabilizing the enzyme preparation
-
cellulose-binding domain-beta-glucosidase fusion protein: in solution stable for 24 h at 25°C, pH 7.0, if immobilized on cellulose: stable up to 7 weeks at 4°C or 37°C
-
enzyme is highly piezostable and thermostable, with increased enzyme inactivation at 25°C and pressures from 100 to 300 MPa. At a constant pressure of 400 MPa, no enzyme inactivation occurrs. Enzyme has an unfolding pressure of 800 MPa at 85°C. Two-step inactivation process due to pressure, which is most pronounced at low temperatures. An increase in pH from 5.5 to 6.5 has a stabilizing effect
increased thermal stability by immobilization on concanavalin A-Sepharose, DEAE- or CM-Sephadex
less glycosylated cellobiase is resistant towards proteolytic as well as endoglycosidase-H digestion and shows higher stability than native enzyme due to increased aggregation of the protein
-
stable in the presence of cetyl-trimethylammonium bromide
-
stable in the presence of urea
the residual activity of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde is 68% of the initial activity at the end of 10 repeated cycles
Zn2+ greatly improves the reusability, glucose tolerance and high-temperature stability of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde
increased thermal stability by immobilization on concanavalin A-Sepharose, DEAE- or CM-Sephadex
-
increased thermal stability by immobilization on concanavalin A-Sepharose, DEAE- or CM-Sephadex
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetonitrile
dimethyl sulfoxide
dimethylformamide
20% v/v, not inhibitory, 50% v/v, 48% loss of activity
DMSO
Ethanol
Ethyl acetate
isopropanol
Methanol
n-Butanol
additional information
acetonitrile
20% v/v, not inhibitory, 50% v/v, 54% loss of activity
acetonitrile
Thermotoga petrophila DSM 13996
-
20% v/v, not inhibitory, 50% v/v, 54% loss of activity
-
dimethyl sulfoxide
-
significantly resistant even at high concentrations
DMSO
10% v/v, 106% of initial activity, 20% v/v, 112.6% of initial activity
DMSO
-
10% v/v, 106% of initial activity, 20% v/v, 112.6% of initial activity
-
Ethanol
-
enzyme is active and stable in presence of 12% v/v ethanol and 5 g per l glucose. Up to 10% ethanol, increase in activity to 120%
Ethanol
10% v/v, 180% of initial activity, 20% v/v, 70% of initial activity
Ethanol
-
10% v/v, 180% of initial activity, 20% v/v, 70% of initial activity
-
Ethanol
10%, 127% of initial activity, 50%, 0.6% of initial activity
Ethanol
-
10%, 16-24% inhibition of isoform A, 10-29% inhibition of isoform B
Ethanol
-
the immobilized enzyme shows about 200% activity at 15% (v/v)
Ethanol
-
the immobilized enzyme shows about 200% activity at 15% (v/v)
-
Ethyl acetate
20% v/v, not inhibitory, 50% v/v, 56% loss of activity
Ethyl acetate
Thermotoga petrophila DSM 13996
-
20% v/v, not inhibitory, 50% v/v, 56% loss of activity
-
isopropanol
10%, 107% of initial activity, 50%, 0.2% of initial activity
Methanol
10%, 121% of initial activity, 50%, 1.3% of initial activity
Methanol
-
the immobilized enzyme shows about 175% activity at 15% (v/v)
Methanol
-
the immobilized enzyme shows about 175% activity at 15% (v/v)
-
additional information
-
the immobilized enzyme is not influenced by acetonitrile
additional information
-
the immobilized enzyme is not influenced by acetonitrile
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4C, 0.05 M acetate buffer, pH 5.0, 2 weeks
4°C, in 20 mM citrate-phosphate buffer, half-lives of 4 days at pH 4.0 and 50 days at pH 7.0
-
4°C, purified, crude supernatant, and heat-treated enzyme remaine stable for 1 year
90% of beta-Glu2 activity is retained when the enzyme is incubated for 6 days in the presence of 5 mg of BSA/ml or non-specific IgG
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
117fold to homogeneity from fresh leaves by chilled acetone and ammonium sulfate precipitation, ion exchange chromatography and gel filtration
-
18fold by ammonium sulfate fractionation, ion exchange and adsorption chromatography, and gel filtration to homogeneity
-
a single step concanvalin A affinity chromatography for native PRGH1 improves the yield and reduced the purification time
ammonium sulfate precipitation and Sepharose-4B-L-tyrosine-1-naphthylamine column chromatography
-
ammonium sulfate precipitation, butyl Sepharose column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
ammonium sulfate precipitation, butyl-Toyopearl 650M column chromatography, DEAE-Toyopearl 650M column chromatography, TSK gel filtration
-
ammonium sulfate precipitation, Concanavalin A-Sepharose column chromatography, Shodex-phenyl HIC-814 column chromatography, and Sephacryl S-200 gel filtration
-
ammonium sulfate precipitation, Macro-Prep methyl HIC column chromatography, Source 15 Q column chromatography, and Sephacryl S-300 gel filtration
-
ammonium sulfate precipitation, Sephadex G-200 gel filtration, and DEAE-cellulose column chromatography
-
ammonium sulfate precipitation, Source 15Q column chromatography, Biogel P4 gel filtration, and phenyl-Superose column chromatography
-
ammonium sulfate precipitation, Source 15Q column chromatography, Biogel P4 gel filtration, and Source 15 isopropyl column chromatography
ammonium sulfate, Butyl-Toyopearl, hydroxyapatite, Q-Sepharose, Sephacryl S-300
-
ammonium sulfate, gel filtration, anion-exchange, reversed-phase HPLC
-
ca. 4300fold, yield of 1.1%, ammonium sulfate precipitation, CM-Sepharose, ConA Sepharose, Superdex 200, Resource S, hydroxyapatite
-
CM-Sephadex C-50 gel filtration, DEAE-Sephadex A-50 gel filtration, Sephadex G-200 gel filtration, and Con A Sepharose column chromatography
-
DEAE Sepharose column chromatography, ammonium sulfate precipitation, Sephacryl S-100 gel filtration, and phenyl-Sepharose column chromatography
-
DEAE Sepharose column chromatography, MonoQ column chromatography, and hydroxyapatite column chromatography
enzymes from wild-type strain NIAB 442, 17fold, and the deoxyglucose- and streptomycin-resistant mutant strain, 23fold, to homogeneity by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
further purification of a cellulase preparation, chromatography steps, to homogeneity
-
further purification of commercially available enzyme preparation, to homogeneity, chromatography steps
-
heat treatment and His-Trap affinity chromatography
HPGPLC column chromatography, Sephacryl S-200 gel filtration and DEAE Sephadex gel filtration
-
isolation of isoforms beta-glu 1 and beta-glu 2 from hypercellulolytic Pol6 mutant
-
native beta-glu2 60fold to homogeneity by ammonium sulfate precipitation, gel filtration, anion exchange chromatography, and chromatofocusing
-
native CBG, cation-exchange chromatography, Octyl-Sepharose, chromatofocusing, gel filtration, recombinant CBG, Octyl-Sepharose
-
native enzyme 10.2fold to homogeneity by anion exchange chromatography, ultrafiltration, and affinity chromatography using 4-aminobenzyl, 1-thio-beta-D-galactopyranoside
-
native enzyme 105fold to homogeneity by anion exchange chromatography and gel filtration
-
native enzyme 12fold in a two-step process involving hydrophobic interaction chromatography, with an additional anion exchange chromatography step
native enzyme 144fold by ammonium sulfate fractionation, anion exchange chromatography, and affinity chromatography on microcrystalline cellulose, to homogeneity, method optimization, overview
-
native enzyme 217fold from flower to homogeneity by anion exchange and hydrophobic interaction chromatography, gel filtration, concanavalin A affinity chromatography and again anion exchange chromatography
-
native enzyme 23.6fold from crude culture extract by ammonium sulfate fractionation, gel filtration, anion exchange chromatography, ultrafiltration, again gel filtration, followed by hyrophobic interaction chromatography and ultrafiltration
-
native enzyme 35.5fold to homogeneity by ammonium sulfate fractionation, dialysis, anion exchange chromatography, gel filtration, and ultrafiltration
-
native enzyme 36fold from petals to homogeneity by ammonium sulfate fractionation, two steps of ion exchange chromatography, and ultrafiltration
-
native enzyme 45fold to homogeneity by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
-
native enzyme 46.3fold to homogeneity by ammonium sulfate fractionation, dialysis, anion exchange chromatography, gel filtration, and ultrafiltration
-
native enzyme 50fold from culture filtrate by ammonium sulfate precipitation, cation-exchange and hydrophobic interaction chromatography, and gel filtration
-
native enzyme 626fold from acetone powder of viscera by two steps of anion exchange chromatography, hydrophobic interaction chromatography, and two steps of gel filtration
-
native enzyme from culture supernatant to homogeneity by anion exchange chromatography and gel filtration
-
native enzyme from roots, 4199fold by ammonium sulfate fractionation, anion and cation exchange chromatography, hydrophobic interaction chromatography, gel filtration, and heparin affinity chromatography, to homogeneity
native enzyme partially from juice of ripe fruits by ammonium sulfate fractionation
-
native extracellular enzyme 130.3fold from culture supernatant by ultrafiltration, anion exchange chromatography and gel filtration to homogeneity
-
native extracellular isozyme by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native piceid-beta-D-glucosidase 12.6fold by ammonium sulfate fractionation, anion exchange chromatography, and freeze drying
-
native wild-type and mutant enzymes partially by anion exchange chromatography and gel filtration 29fold and 16fold, respectively
-
Ni-NTA column chromatography
Ni-NTA resin column chromatography and Mono-S column chromatography
partial
partially, subcellular fractionation, sucrose density gradient centrifugation
-
purified 138.85fold by ammonium sulfate precipitation, DE-22 ion exchange and Sephadex G-150 gel filtration chromatography
-
purified by salting out with ammonium sulfate and using specifically designed Sepharose-4B-l-tyrosine-1-naphthylamine hydrophobic interaction chromatography. Purification: 155fold, enzyme yield: 54%
-
purified in the presence and absence of 2-deoxy-D-glucose by ultrafiltration, DEAE Sephadex A-50 gel filtration, high-performance gel-permeation liquid chromatography, and Sephacryl S-200 gel filtration
-
Q Sepharose column chromatography, Superdex 75 gel filtration, Resource Q column chromatography, Source 30S column chromatography, Superdex 200 gel filtration, and phenyl Sepharose column chromatography
Q-Sepharose resin column chromatography and Sephacrly S-100 gel filtration
-
recombinant beta-glucosidase purified by gel filtration to apparent homogeneity, 21fold with an overall enzyme yield of 6.8%
recombinant BglA 52.9fold from Escherichia coli by ammonium sulfate fractionation, ion exchange and adsorption chromatography, and gel filtration
recombinant enzyme 1112.2fold from Spodoptera frugiperda Sf9 cells by ammonium sulfate fractionation, gel filtration and anion exchange chromatography, cleavage of the signal peptide
recombinant enzyme 16fold to homogeneity by ion exchange chromatography and gel filtration
recombinant enzyme 23.3fold from yeast by immobilized metal-ion affnity chromatography, following hydrophobic interaction chromatography, insertion of a polyhistidine-tag either after the N-terminal alpha-factor signal sequence or at the C-terminus fails to assist in purification by immobilized metal-ion affnity chromatography due to post-translational processing at both termini
-
recombinant enzyme 24fold from Trichoderma reesei strain Rut-C30 by ultrafiltration, two steps of gel filtration, and ion exchange chromatography
recombinant enzyme from Escherichia coli by immobilized metal-affinity chromatography and removal of the tags, followed by cation exchange chromatography and gel filtration to about 95% purity
recombinant extracellular His6-tagged enzyme from Escherichia coli strain JM101 culture supernatant by cobalt affinity chromatography, cleavage of the fusion protein with thrombin
recombinant His-tagged Dhr1 and mutant E189D from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged enzyme 6.4fold from Escherichia coli to homogeneity by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli by heat treatment at 75°C, and nickel affinity chromatography
-
recombinant His-tagged enzyme lacking the potential signal sequence from Pichia pastoris strain KM71H by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography
recombinant His-tagged Glu1b from Escherichia coli by nickel affinity chelating chromatography, ultrafiltration, and gel filtration
-
recombinant His-tagged isozyme BGL1A from Escherichia coli by ammonium sulfate fractionation, hydrophobic interaction chromatography, and nickel affinity chromatography
recombinant His-tagged isozyme BGL1A from Escherichia coli by anion exchange and affinity chromatography, and gel filtration
recombinant His-tagged isozyme BGL1B from Escherichia coli by ammonium sulfate fractionation, hydrophobic interaction chromatography, and nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and two steps of anion exchange chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and selenomethionine-labeld enzymes from Escherichia coli by immobilized metal-ion affinity chromatography column
-
recombinant N-terminally His-tagged wild-type and chimeric mutant enzymes from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His6-tagged cytosolic isozyme from Sf9 insect cells by nickel affinity and ion exchange chromatography to homogeneity
-
recombinant wild-type and mutant enzymes from Escherichia coli by metal affinity chromatography and gel filtration to homogeneity
recombinant wild-type and mutant isozyme TaGlu1a from Escherichia coli by metal affinity chromatography and gel filtration to homogeneity
to homogeneity by ammonium sulfate fractionation, gel filtration, ion exchange chromatography, and adsorption chromatography
-
to homogeneity, 2step chromatography
to homogeneity, chromatography steps
to homogeneity, chromatography steps, preparative gel electrophoresis
thermophilic anaerobic bacterium
-
to homogeneity, chromatography steps, wild-type and enzyme from mutant strain
-
to homogeneity, chromatography techniques
to homogeneity, crude enzyme preparation by further chromatography steps
-
to homogeneity, five different extracellular forms, chromatography steps
Sporotrichum pulverulentum
-
to homogeneity, preparative isoelectric focusing, 1step chromatography
-
to homogeneity, recombinant enzyme
Tpen_1494 is ligated into p6xHis119 downstream of the BLMA promoter to create p6xHisTpbgl. Recombinant Tpbgl, with eight additional amino acids (Met-Glu-(His)6) at the N-terminus, is expressed in Escherichia coli harboring p6xHisTpbgl
using ammonium sulfate precipitation followed by ion-exchange chromatography
Halalkalibacterium halodurans
-
using Ni-NTA chromatography
ammonium sulfate precipitation, Source 15Q column chromatography, Biogel P4 gel filtration, and Source 15 isopropyl column chromatography
-
ammonium sulfate precipitation, Source 15Q column chromatography, Biogel P4 gel filtration, and Source 15 isopropyl column chromatography
-
recombinant N-terminally His-tagged wild-type and chimeric mutant enzymes from Escherichia coli by nickel affinity chromatography
-
recombinant N-terminally His-tagged wild-type and chimeric mutant enzymes from Escherichia coli by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
bgl operon, gene bglB, contruction of a genomic library, DNA and amino acid sequence determination and analysis, determination of bgl operon structure and organization, overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) as His-tagged proteins, subcloning in Escherichia coli strain DH5alpha
cDNA expressed in insect cells, Baculovirus expression system
cDNA is expressed in insect cells, Baculovirus expression system
cloned in frame with the Saccharomyces cerecisiae a-factor secretory signal and expressed in Pichia pastoris strain X-33
cloned into the pET-28b vector. His-tagged MeBglD2 is expressed in Escherichia coli BL21(DE3) cells
DNA and amino acid sequence determination and anaylsis, expression analysis by semi-quantitative RT-PCR, stable expression of the 35S-GmICHG:GFP fusion gene in Arabidopsis thaliana T87 cells using an Agrobacterium tumefaciens GV3101(pMP90) transformation system, phylogenetic analysis
enzyme with an N-terminal truncation following the propeptide and eight histidine residues enabling its purification by immobilized metal-ion affnity chromatography, functional, methanol-inducible enzyme expression in Pichia pastoris strain GS115 and Saccharomyces cerevisiae strains DY150 and DBY746, addition of 0.5% casamino acids to the culture medium stabilizes the pH of the culture and increaseds the protein yield by 3-5folds, insertion of a polyhistidine-tag either after the N-terminal alpha-factor signal sequence or at the C-terminus fails to assist in purification by immobilized metal-ion affnity chromatography due to post-translational processing at both termini, expression in Escherichia coli strain BL21(DE3) as insoluble and inactive protein, which can be made soluble by co-expression with bacterial chaperonin GroESL
-
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli under regulation of a T7/lac promoter. On induction with isopropyl-beta-D-1-thiogalactopyranoside, the enzyme expresses at 40% of the cell protein producing 238 mg/liter culture. With increase in culture cell density to A600 12 in auto-inducing M9NG medium, beta-glucosidase production increases 3fold. Approximately 70% of the expressed enzyme is in a soluble form, while the rest is in an insoluble fraction of the cell lysate
Halalkalibacterium halodurans
-
expressed in Pichia pastoris
expressed in Trichoderma reesei
expression as fusion protein with alpha-agglutinin on surface of Saccharomyces cerevisiae cells
expression in Escherichia coli
expression in lactic-acid producing Saccharomyces cerevisiae strain, expression on cell surface by fusing the mature protein to the C-terminal half region of alpha-agglutinin
expression in Pichia pastoris
expression in Saccharomyces cerevisiae
expression of His-tagged isozyme BGL1A in Escherichia coli
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
expression of His-tagged wild-type Bgl3B in Escherichia coli strain Tuner (DE3), and of His-tagged selenomethionine-labeled enzyme in Escherichia coli strain B834 (DE3)
-
expression of N-terminally His6-tagged cytosolic isozyme in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha, display of the enzyme on the cell surface of Saccharomyces cerevisiae
-
expression of wild-type and mutant hybrid of BGL1-CBD2 domain with cellobiohydrolase CBHII in in Saccharomyces cerevisiae strain CENPK42 under the control of phosphoglycerate-kinase-1 promoter PGK1P and terminator PGK1T and yeast mating pheromone alpha-factor secretion signal MFalpha1S, subcloning in Escherichia coli
-
gene bgl2, DNA and amino acid sequence determination and anaylsis, expression of a His-tagged cDNA fragment excluding the potential signal sequence in Pichia pastoris strain KM71H
gene bglA, DNA and amino acid sequence determination and analysis, cDNA library construction, expression in Escherichi coli
gene bglA, recombinant expression in Escherichia coli strain BL21 Codon-Plus
gene bglb, DNA and amino acid sequence determination and anaylsis, expression of N-terminally His-tagged wild-type and chimeric mutant enzymes in Escherichia coli
-
gene bglu1, expression in in Escherichia coli with N-terminal thioredoxin and hexahistidine tags
gene cba3, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of the extracellular His6-tagged enzyme in Escherichia coli strain JM101, transformants expressing recombinant Cba3 grow readily in minimal media using cellobiose as the sole carbon source
gene cbg1, DNA and amino acid sequence determination and anaylsis, expression of N-terminally His-tagged wild-type and chimeric mutant enzymes in Escherichia coli
-
gene cel3a, DNA and amino acid sequence determination and analysis, subcloning and expression in Escherichia coli, expression in Trichoderma reesei
gene celG encoded in the celEFG operon, construction of a cosmid library and cloning of the celEFG operon, genetic organizatin, DNA and amino acid sequence determination and analysis, phylogenetic tree, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene identification in Escherichia coli
heterogeneous expression in Pichia pastoris strain GS115
isozyme BGL1A, DNA and amino acid sequence determination and analysis, transcription analysis, expression of C-terminally His-tagged enzyme in Escherichia coli
isozyme BGL1B, DNA and amino acid sequence determination and analysis, transcription analysis, expression of C-terminally His-tagged enzyme in Escherichia coli
isozyme TaGlu1a, DNA and amino acid sequence determination and analysis, isozyme expression profile, expression of wild-type and mutant isozyme TaGlu1a in Escherichia coli
isozyme TaGlu1b, DNA and amino acid sequence determination and analysis, isozyme expression profile, expression in Escherichia coli
isozyme TaGlu1c, DNA and amino acid sequence determination and analysis, isozyme expression profile, expression in Escherichia coli
methanol-inducible expression of wild-type and mutant enzymes in Pichia pastoris strain X-33
-
native and mutated cDNA sequences cloned into vector pPICZalphaB and expressed in Pichia pastoris
overexpression in Escherichia coli
overexpression of Dhr1 and mutant E189D in Escherichia coli as His-tagged proteins
-
overexpression of His-tagged enzyme in Escherichia coli strain JM109
overexpression of His-tagged Glu1b in Escherichia coli as soluble protein
-
single gene, genomic organization, DNA and amino acid sequence determination and analysis, expression in Spodoptera frugiperda Sf9 cells using the baculovirus infection system
wild type and mutant enzymes Q77R, D206N, D206Q, E207S and E399S are expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of glucose to avicel or cellobiose culture media drastically represses the production of enzyme
BGLU21 by cold, 2,4-dichlorophenoxyacetate and methyl jasmonate
BGLU22 by NaCl, 2,4-dichlorophenoxyacetate and methyl jasmonate
BGLU23 by 2,4-dichlorophenoxyacetate and methyl jasmonate
expression in the presence of glucose, maltose, lactose, glycerol, starch, wheat bran and gruel. The highest level of beta-glucosidase activity is produced with wheat bran at the concentration of 3%
-
growth on methyl cellulose supports the highest yield of beta-glucosidase (177.5 U/mg) at pH 6.0 and 30°C
-
optimum conditions for beta-glucosidase production are at 37C, pH 6.5 in the MRS medium. Presence of maltose, tryptone, MnSO4, propanol, 0.2% NaCl and alanine increase the yield of enzyme
rice bran-based solid-state fermentation of Penicillium citrinum YS40-5 leads to a high yield of beta-glucosidase
senescence-induced loss in photosynthesis enhances cell wall beta-glucosidase activity
-
the highest levels of total activity are obtained in liquid media supplemented with avicel or carboxymethyl cellulose
-
the mRNA expression levels of beta-glucosidase increases rapidly concomitant with berry redcolouring
-
addition of glucose to avicel or cellobiose culture media drastically represses the production of enzyme
-
addition of glucose to avicel or cellobiose culture media drastically represses the production of enzyme
-
-
optimum conditions for beta-glucosidase production are at 37C, pH 6.5 in the MRS medium. Presence of maltose, tryptone, MnSO4, propanol, 0.2% NaCl and alanine increase the yield of enzyme
KX664087
optimum conditions for beta-glucosidase production are at 37C, pH 6.5 in the MRS medium. Presence of maltose, tryptone, MnSO4, propanol, 0.2% NaCl and alanine increase the yield of enzyme
-
-
rice bran-based solid-state fermentation of Penicillium citrinum YS40-5 leads to a high yield of beta-glucosidase
EU918770
rice bran-based solid-state fermentation of Penicillium citrinum YS40-5 leads to a high yield of beta-glucosidase
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
biofuel production
biotechnology
degradation
food industry
industry
molecular biology
a reporter gene for the localization of mammalian cells and transgenic tissues based on detection of the bglA (SYNbglA) gene of Caldocellum saccharolyticum that encodes a thermophilic beta-glucosidase is presented. SYNbglA expression can be localized in situ or detected quantitatively in colorimetric assays and can be co-localized with Escherichia coli beta-galactosidase. SYNbglA can be detected in tissue wholemounts and in frozen and wax embedded sections
nutrition
synthesis
biofuel production
biodegradation of lignocellulosic biomass involves a concerted attack by several enzymes, including beta-glucosidases as key component. Current methodologies for biomass conversion to biofuels employ physical and/or chemical pretreatments that disrupt the lignocellulosic biomass in plant cell walls in combination with enzymatic hydrolysis of the cellulose to produce free sugars. Thus, stable cellulolytic enzymes with high enzymatic activity in pretreatment biomass conditions, including high temperatures and acidic conditions, are essential at an industrial scale production. These two features makes beta-glucosidase TpBGL1 to be of significant biotechnological interest
biofuel production
biodegradation of lignocellulosic biomass involves a concerted attack by several enzymes, including beta-glucosidases as key component. Current methodologies for biomass conversion to biofuels employ physical and/or chemical pretreatments that disrupt the lignocellulosic biomass in plant cell walls in combination with enzymatic hydrolysis of the cellulose to produce free sugars. Thus, stable cellulolytic enzymes with high enzymatic activity in pretreatment biomass conditions, including high temperatures and acidic conditions, are essential at an industrial scale production. These two features makes beta-glucosidase TpBGL3 to be of significant biotechnological interest
biofuel production
the saccharification yield of rice straw using Trichoderma reesei cellulase is improved by the addition of MeBglD2. These results show that MeBglD2 can be used to improve plant biomass saccharification, because both substrates and products can activate its enzymatic activity
biofuel production
-
biodegradation of lignocellulosic biomass involves a concerted attack by several enzymes, including beta-glucosidases as key component. Current methodologies for biomass conversion to biofuels employ physical and/or chemical pretreatments that disrupt the lignocellulosic biomass in plant cell walls in combination with enzymatic hydrolysis of the cellulose to produce free sugars. Thus, stable cellulolytic enzymes with high enzymatic activity in pretreatment biomass conditions, including high temperatures and acidic conditions, are essential at an industrial scale production. These two features makes beta-glucosidase TpBGL3 to be of significant biotechnological interest
-
biofuel production
-
biodegradation of lignocellulosic biomass involves a concerted attack by several enzymes, including beta-glucosidases as key component. Current methodologies for biomass conversion to biofuels employ physical and/or chemical pretreatments that disrupt the lignocellulosic biomass in plant cell walls in combination with enzymatic hydrolysis of the cellulose to produce free sugars. Thus, stable cellulolytic enzymes with high enzymatic activity in pretreatment biomass conditions, including high temperatures and acidic conditions, are essential at an industrial scale production. These two features makes beta-glucosidase TpBGL1 to be of significant biotechnological interest
-
biotechnology
immobilization of the enzyme on gelatin, overview, the very stable gelatin-immobilized enzyme can be used in continuous synthesis of beta-glucosides by transglucosylation
biotechnology
-
the enzyme might be useful as biocatalyst in the synthesis of glyco-conjugates, overview
biotechnology
production of isoflavone aglycones by the enzyme. Isoform BGL1 shows broad substrate specificity to various isoflavone glycosides, the residual ratio is reached to 6.2% of the total amount of isoflavone glycosides and the hydrolysis reaction is almost finished within 48 h
biotechnology
-
the beta-glucosidase has a potential for biotechnological applications in the bioconversion of lignocellulosic materials
biotechnology
the bifunctional beta-glucosidase/xylosidase can be used in simultaneous saccharification of cellulose and xylan into fermenantable glucose and xylose
degradation
-
beta-glucan can be completely degraded to glucose at high temperature with a combination of the hyperthermophile Pyrococcus furiosus endocellulase (EGPf) and beta-glucosidase (BGLPf). beta-Glucans are polysaccharides of D-glucose monomers formed by beta(1->3),(1->4) mixed-linkage bonds. They occur most commonly as cellulose in plants, in the bran of cereal grains, the cell wall of baker's yeast, and in certain fungi, mushrooms, and bacteria
degradation
EU918770
a 3.43fold synergistic effect by combining with Trichoderma reesei cellulases is observed
degradation
enzyme shows increased thermal stability and saccharification yield on pretreated corn stover compared with Hypocrea jecorina Cel3A
degradation
-
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase
degradation
-
using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively
degradation
addition of beta-glucosidase to the rice straw hydrolysis reaction containing a commercial cellulase results in increase of reducing sugars being released
degradation
-
application of enzyme in fed-batch hydrolysis of cellulose and high-temperature simultaneous saccharification and fermentation. beta-Glucosidase is suitable for lignocellulose conversion into ethanol
degradation
-
enzyme shows synergistic effects when commercial cellulase when is supplemented with the crude beta-glucosidase leading to improved sugar release of up to 548.4 mg/gds from paddy straw at 40°C
degradation
-
highly efficient synergistic effects exist between TN0602 and cellulases for cellulose hydrolysis
degradation
-
saccharification of pretreated paddy straw by supplementing beta-glucosidase enzyme results in 1.34fold higher glucose release
degradation
the supplementation of BglP significantly enhances the glucose yield from sugarcane bagasse, especially in the presence of high concentrations of glucose or xylose
degradation
use for bioethanol production from different cellulosic biomass sources. Using simultaneous saccharification and fermentation, 9.47 g/l and 14.32 g/l of bioethanol can be obtained from carboxymethyl cellulose and pretreated rice straw, respectively
degradation
the high-catalytic turn-over rate by mutant enzyme D206N for beta-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures
degradation
-
enzyme shows synergistic effects when commercial cellulase when is supplemented with the crude beta-glucosidase leading to improved sugar release of up to 548.4 mg/gds from paddy straw at 40°C
-
degradation
Thermothelomyces thermophilus JCP 1-4
-
using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively
-
degradation
Bacillus subtilis RA10
-
saccharification of pretreated paddy straw by supplementing beta-glucosidase enzyme results in 1.34fold higher glucose release
-
degradation
Thermotoga petrophila RUK-10
-
highly efficient synergistic effects exist between TN0602 and cellulases for cellulose hydrolysis
-
degradation
-
the supplementation of BglP significantly enhances the glucose yield from sugarcane bagasse, especially in the presence of high concentrations of glucose or xylose
-
degradation
-
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase
-
degradation
-
a 3.43fold synergistic effect by combining with Trichoderma reesei cellulases is observed
-
food industry
beta-glucosidases play an important role in the flavor formation of fruits, wine and sweet potato by the production of monoterpene alcohols such as linalool, alpha-terpeneol, citronellol, nerol, and geranol, supplementation with beta-glucosidases from external sources may enhance aroma release thus benefiting the winemaking process
food industry
-
the enzyme is used for fermentation of Sicilian table olives
food industry
-
the enzyme is used for fermentation of Sicilian table olives
-
industry
-
application in simultaneous saccharification and fermentation, evaluation of the suitability of plant glycosyl hydrolases in lignocellulose conversion
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
Thermochaetoides thermophila
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
industry
the enzyme is widely used in cellulose hydrolysis and the biological conversion and transformation of flavonoids and saponins. The properties of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde, including thermal stability, pH stability, reusability, and tolerance of glucose, are greatly improved compared with free Tpebgl3. The coordinating metal cation Zn2+ enables the immobilized enzyme to exhibit higher catalytic efficiency. The addition of Zn2+ can greatly advance the reusability, thermostability, and glucose tolerance of immobilized enzyme, which is beneficial for industrial applications
industry
potentially an important industrial enzyme due to the broad specificity, catalytic efficiency and thermostability
industry
-
the enzyme is widely used in cellulose hydrolysis and the biological conversion and transformation of flavonoids and saponins. The properties of the enzyme immobilized on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde, including thermal stability, pH stability, reusability, and tolerance of glucose, are greatly improved compared with free Tpebgl3. The coordinating metal cation Zn2+ enables the immobilized enzyme to exhibit higher catalytic efficiency. The addition of Zn2+ can greatly advance the reusability, thermostability, and glucose tolerance of immobilized enzyme, which is beneficial for industrial applications
-
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
-
nutrition
-
the enzyme is useful in enological applications during the final stages of alcoholic fermentations in addition to yeast strains, overview
nutrition
the enzyme is useful in rice polishing by degradation and assimilation of rice bran hemicellulose of the outer grain skin
nutrition
-
the enzyme is useful in tofu production where it hydrolyses isoflavone glucosides allowing the preparation of aglycone isoflavone-enriched tofu
nutrition
-
the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview
nutrition
-
the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview
nutrition
-
the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview
nutrition
-
use of Bifidobacterium lactis for fermentation of soymilk. Beta-glucosidase produced by Bifidobacterium lactis hydrolyzes isoflavone beta-glycosides to isoflavone aglycones resulting in significant decrease in the concentration of beta-glycosides and likely in improvement of he biological functionality of soymilk
nutrition
-
use of Lactobacillus acidophilus for fermentation of soymilk. Beta-glucosidase produced by Lactobacillus acidophilus hydrolyzes isoflavone beta-glycosides to isoflavone aglycones resulting in significant decrease in the concentration of beta-glycosides and likely in improvement of he biological functionality of soymilk
nutrition
-
use of Lactobacillus casei for fermentation of soymilk. Beta-glucosidase produced by Lactobacillus casei hydrolyzes isoflavone beta-glycosides to isoflavone aglycones resulting in significant decrease in the concentration of beta-glycosides and likely in improvement of he biological functionality of soymilk
nutrition
-
properties of the thermostable beta-glucosidase from Sulfolobus shibatae immobilized on silica gel by cross-linking with transglutaminase indicate possible suitability of this preparation for hydrolysis of lactose during milk and whey processing. Due to high thermal stability the immobilized enzyme can be used at temperatures, which restrict microbial growth during a long operating time of continuous-flow reactor
nutrition
-
the enzyme is useful in tofu production where it hydrolyses isoflavone glucosides allowing the preparation of aglycone isoflavone-enriched tofu
-
nutrition
-
the enzyme is useful in rice polishing by degradation and assimilation of rice bran hemicellulose of the outer grain skin
-
nutrition
-
the enzyme is important in hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk, overview
-
nutrition
-
properties of the thermostable beta-glucosidase from Sulfolobus shibatae immobilized on silica gel by cross-linking with transglutaminase indicate possible suitability of this preparation for hydrolysis of lactose during milk and whey processing. Due to high thermal stability the immobilized enzyme can be used at temperatures, which restrict microbial growth during a long operating time of continuous-flow reactor
-
synthesis
-
increased hydrolysis of cellobiose by immobilized enzyme preparation
synthesis
co-expression of beta-glucosidase and endoglucanase in Saccharomyces cerevisiae. Ethanol fermentation from 20 g per l barley beta-glucan with the co-displaying strain reaches 7.94 g per l ethanol after 24 h of fermentation. The conversion rate of ethanol is 69.6% of the theoretical ethanol concentration
synthesis
construction of a lactic-acid producing Saccharomyces cerevisiae strain expressing isoform Bgl1 on cell surface by fusing the mature protein to the C-terminal half region of alpha-agglutinin. Strain is able to grow on cellobiose and glucose minimal medium at the same rate. The maximum rate of L-lactate production on cellobiose is 2.8 g per l and similar to that on glucose
synthesis
-
optimization of culture condition for production of beta-glucosidase from Aspergillus niger and subsequent use for hydrolysis of ginsenosides. Presence of wheat bran and KH2PO4 and stirring speed have significant effect on enzyme activity
synthesis
-
use of enzyme for syntheses of pyridoxine glycosides in di-isopropylether. Synthesis of 7-O-(alpha-D-glucopyranosyl)pyridoxine, 7-O-(beta-D-glucopyranosyl)pyridoxine, 6-O-(alpha-D-glucopyranosyl)pyridoxine, 7-O-(alpha-D-galactopyranosyl)pyridoxine, 7-O-(beta-D-galactopyranosyl)pyridoxine, 6-O-(alpha-D-galactopyranosyl)pyridoxine, 7-O-(alpha-D-mannopyranosyl)pyridoxine, 7-O-(beta-D-mannopyranosyl)pyridoxine, 6-O-(alpha-D-mannopyranosyl)pyridoxine in yields ranging from 23% to 40%
synthesis
-
the enzyme is useful in synthetic biology to produce complex bioactive glycosides and to avoid chemical hazards
synthesis
glucose production from cellulose material using beta-glucosidase from Pyrococcus furioses and endocellulase from Pyrococcus horikoshii. The combination reaction can produce only glucose without the other oligosaccharides from phosphoric acid swollen Avicel
synthesis
preparation of lactose-free pasteurized milk with a recombinant thermostable beta-glucosidase
synthesis
immobilization of enzyme on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde. The optimal conditions of immobilized enzyme are the same as that of the free enzyme, the highest activity with cellobiose as the substrate approaches 1.7 U/g. Immobilization improves the thermostability, pH stability and glucose tolerance, the residual activity is 68% of the initial activity at the end of 10 repeated cycles. 2 mM Zn2+ increases the relative activity of the immobilized enzyme to 192% and 199% with cellobiose and 4-nitrophenyl-beta-D-glucopyranoside as substrates, respectively and improves the reusability, high-temperature stability, and glucose tolerance
synthesis
Bacillus sp. ZJ1308
-
optimized medium composition for beta-glucosidase expression is corn cob (51.8 g/l), beef extract (23.8 g/l), salicin (0.5 g/l), MnSO4·H2O (0.363 g/l), MgSO4·7H2O (0.4 g/l), and NaCl (5 g/l). Under the optimal conditions, the activity of beta-glucosidase is up to 4.71 U/ml
synthesis
-
the optimal medium composition for beta-glucosidase production is 2.99% (w/v) bagasse, 0.33% (w/v) yeast extract, 0.38% (w/v) Triton X-100, 0.39% (w/v) NaNO3, and pH 8.0 at 30°C. Large-scale production in 7-l stirred tank bioreactor results in beta-glucosidase production of up to 23.29 IU/g within 80 h of incubation
synthesis
-
the enzyme can constitute a valuable biocatalyst for the synthesis of disaccharides involving beta(1-3) linked disaccharide structures as, for example, Bifidus factors
synthesis
-
immobilization of enzyme on macroporous resin NKA-9 modified with polyethylenimine and glutaraldehyde. The optimal conditions of immobilized enzyme are the same as that of the free enzyme, the highest activity with cellobiose as the substrate approaches 1.7 U/g. Immobilization improves the thermostability, pH stability and glucose tolerance, the residual activity is 68% of the initial activity at the end of 10 repeated cycles. 2 mM Zn2+ increases the relative activity of the immobilized enzyme to 192% and 199% with cellobiose and 4-nitrophenyl-beta-D-glucopyranoside as substrates, respectively and improves the reusability, high-temperature stability, and glucose tolerance
-
synthesis
-
the optimal medium composition for beta-glucosidase production is 2.99% (w/v) bagasse, 0.33% (w/v) yeast extract, 0.38% (w/v) Triton X-100, 0.39% (w/v) NaNO3, and pH 8.0 at 30°C. Large-scale production in 7-l stirred tank bioreactor results in beta-glucosidase production of up to 23.29 IU/g within 80 h of incubation
-
synthesis
-
the enzyme is useful in synthetic biology to produce complex bioactive glycosides and to avoid chemical hazards
-
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Release 2023.1 (January 2023)
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