Information on EC 3.2.1.40 - alpha-L-rhamnosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.2.1.40
-
RECOMMENDED NAME
GeneOntology No.
alpha-L-rhamnosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
rutin degradation (plants)
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-L-rhamnoside rhamnohydrolase
The enzyme, found in animal tissues, plants, yeasts, fungi and bacteria, utilizes an inverting mechanism of hydrolysis, releasing beta-L-rhamnose. Substrates include naringin, rutin, quercitrin, hesperidin, dioscin, terpenyl glycosides and many other natural glycosides containing terminal alpha-L-rhamnose.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-35-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Absidia sp.
strain 90, FFDCL-90, and strain 39, FFDCL-39, isolated from traditional Chinese Koji
-
-
Manually annotated by BRENDA team
strain NW240, RhaA and RhaB
-
-
Manually annotated by BRENDA team
strain S1
-
-
Manually annotated by BRENDA team
strain S1
-
-
Manually annotated by BRENDA team
strain IFO 4308
-
-
Manually annotated by BRENDA team
growth on L-rhamnose as sole carbon source
-
-
Manually annotated by BRENDA team
CECT 2663
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bacteroides JY-6
-
-
-
Manually annotated by BRENDA team
buckwheat
-
-
Manually annotated by BRENDA team
strain 310
-
-
Manually annotated by BRENDA team
strain 310
-
-
Manually annotated by BRENDA team
strain 706
-
-
Manually annotated by BRENDA team
strain 706
-
-
Manually annotated by BRENDA team
strain K-60, isolated from human intestine
-
-
Manually annotated by BRENDA team
strain K-60, isolated from human intestine
-
-
Manually annotated by BRENDA team
strain 709
-
-
Manually annotated by BRENDA team
strain 709
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 695
-
-
Manually annotated by BRENDA team
strain 695
-
-
Manually annotated by BRENDA team
isolate 009RG
-
-
Manually annotated by BRENDA team
Thermomicrobia bacterium
strain 708
-
-
Manually annotated by BRENDA team
strain 708
-
-
Manually annotated by BRENDA team
marine gastropod
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
20(S)-ginsenoside Rg2 + H2O
20(S)-ginsenoside Rh1 + alpha-L-rhamnose
show the reaction diagram
Absidia sp.
-
low activity cleaving the alpha-1,2-linkage
-
-
?
3-O-alpha-L-rhamnopyranosyl-alpha-D-mannopyranoside + H2O
alpha-L-rhamnose + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
4',5,7-trihydroxyflavanone 7-rhamnoglucoside + H2O
4',5,7-trihydroxyflavanone 7-glucoside + alpha-L-rhamnose
show the reaction diagram
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
show the reaction diagram
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnose
show the reaction diagram
4-nitrophenyl alpha-L-rhamnoside + H2O
alpha-L-rhamnose + 4-nitrophenol
show the reaction diagram
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
-
-
2.1% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
-
?
4-nitrophenyl-alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
show the reaction diagram
-
-
-
?
4-nitrophenyl-alpha-L-rhamnopyranoside + H2O
alpha-L-rhamnose + 4-nitrophenol
show the reaction diagram
-
-
-
?
6-O-alpha-L-rhamnosyl-D-glucopyranose + H2O
alpha-L-rhamnose + D-glucose
show the reaction diagram
-
rutinose
-
-
?
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
show the reaction diagram
convallotoxin + H2O
strophantidin + alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
frangulin + H2O
frangula emodin + alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
gellan + H2O
alpha-L-rhamnose + ?
show the reaction diagram
gellan + H2O
L-rhamnose + ?
show the reaction diagram
-
-
-
?
geranyl-beta-D-rutinoside + H2O
geranyl-beta-D-glycoside + alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
gypenoside-5 + H2O
ginsenoside Rd + alpha-L-rhamnose
show the reaction diagram
hesperidin + H2O
?
show the reaction diagram
-
34% of activity compared to naringin
-
-
?
hesperidin + H2O
? + alpha-L-rhamnose
show the reaction diagram
Thermomicrobia bacterium
cleavage of the alpha-1,6-linkage
-
-
?
hesperidin + H2O
hesperetin 7-glucoside + alpha-L-rhamnose
show the reaction diagram
hesperidin + H2O
hesperetin 7-O-beta-D-glucoside + L-rhamnose
show the reaction diagram
-
-
-
-
?
hesperidin + H2O
hesperetin 7-O-glucoside + alpha-L-rhamnose
show the reaction diagram
hesperidin + H2O
L-rhamnose + ?
show the reaction diagram
-
-
-
?
high-methoxyl pectin + H2O
pyranoside + alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
methyl 3-O-alpha-L-rhamnopyranosyl-alpha-D-mannopyranoside + H2O
alpha-L-rhamnose + methyl alpha-D-mannose
show the reaction diagram
-
-
-
-
?
methyl 3-O-alpha-L-rhamnopyranosyl-alpha-D-xylopyranoside + H2O
alpha-L-rhamnose + methyl alpha-D-xylose
show the reaction diagram
-
-
-
-
?
methyl 3-O-alpha-L-rhamnopyranosyl-alpha-L-rhamnopyranoside + H2O
alpha-L-rhamnose + methyl alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
methyl 4-O-alpha-L-rhamnopyranosyl-alpha-D-galactopyranoside + H2O
alpha-L-rhamnose + methyl alpha-D-galactose
show the reaction diagram
-
-
-
-
?
methyl 4-O-alpha-L-rhamnopyranosyl-alpha-D-mannopyranoside + H2O
alpha-L-rhamnose + methyl alpha-D-mannose
show the reaction diagram
-
-
-
-
?
methyl 4-O-alpha-L-rhamnopyranosyl-alpha-D-xylopyranoside + H2O
alpha-L-rhamnose + alpha-D-xylose
show the reaction diagram
-
-
-
-
?
muscat glycoside extract
linalool + alpha-terpineol + citronellol + nerol + geraniol + ?
show the reaction diagram
-
-
-
-
?
naringin + H2O
4',5,7-trihydroxyflavanone 7-O-beta-D-glucoside L-rhamnose
show the reaction diagram
-
-
-
-
?
naringin + H2O
4',5,7-trihydroxyflavanone-7-beta-D-glucoside + alpha-L-rhamnose
show the reaction diagram
naringin + H2O
4',5,7-trihydroxyflavanone-7-beta-D-glucoside + L-rhamnose
show the reaction diagram
substrate naringin is preferred over hesperidin
-
-
?
naringin + H2O
?
show the reaction diagram
naringin + H2O
? + alpha-L-rhamnose
show the reaction diagram
Thermomicrobia bacterium
preferred substrate, cleavage of the alpha-1,2-linkage
-
-
?
naringin + H2O
beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
show the reaction diagram
naringin + H2O
L-rhamnose + ?
show the reaction diagram
neohesperidin + H2O
5-hydroxy-2-(3-hydroxy-4-methoxyphenyl)-4-oxo-3,4-dihydro-2H-chromen-7-yl beta-D-glucopyranoside + alpha-L-rhamnose
show the reaction diagram
Bacteroides JY-6
-
-
-
-
?
p-nitrophenol-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
show the reaction diagram
p-nitrophenyl alpha-L-rhamnoside + H2O
p-nitrophenol + alpha-L-rhamnose
show the reaction diagram
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
show the reaction diagram
-
-
6.1% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
-
?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
p-nitrophenol + alpha-L-rhamnopyranose
show the reaction diagram
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucopyranose
show the reaction diagram
-
2.9% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactopyranose
show the reaction diagram
-
1.6% of activity compared to p-nitrophenyl-alpha-L-rhamnopyranoside
-
?
periplor alpha-L-rhamnoside + H2O
periplogenin + alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
phenylethyl-beta-D-rutinoside + H2O
phenylethyl-beta-D-glycoside + alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
polygalacturonic acid + H2O
D-galacturonic acid
show the reaction diagram
-
-
-
-
?
poncirin + H2O
poncirein + alpha-L-rhamnose
show the reaction diagram
Bacteroides JY-6
-
-
-
-
?
proscillaridin A + H2O
?
show the reaction diagram
proscillaridin A + H2O
pyranosyl 3,14-dihydroxybufa-4,20,22-trienolid + alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
quercetin 3-alpha-L-rhamnopyranoside + H2O
quercetin + L-rhamnose
show the reaction diagram
-
31% of activity compared to naringin
-
-
?
quercitrin + H2O
quercetin + L-rhamnose
show the reaction diagram
rhamnogalacturonan tetramer + H2O
?
show the reaction diagram
Thermomicrobia bacterium
-
-
-
?
rhamnosyl-glucose + H2O
glucose + alpha-L-rhamnose
show the reaction diagram
-
gellan as carbon-source
-
-
?
rutin + H2O
3-glycosylquercetin + alpha-L-rhamnose
show the reaction diagram
rutin + H2O
?
show the reaction diagram
-
63% of activity compared to naringin
-
-
?
rutin + H2O
? + alpha-L-rhamnose
show the reaction diagram
Thermomicrobia bacterium
low activity, cleavage of the alpha-1,6-linkage
-
-
?
rutin + H2O
alpha-L-rhamnose + quercetrin
show the reaction diagram
rutin + H2O
L-rhamnose + ?
show the reaction diagram
-
-
-
?
saikosaponin C + H2O
? + alpha-L-rhamnose
show the reaction diagram
scilliglaucosidin alpha-L-rhamnoside + H2O
scilliglaucosidin + alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
scilliphaeosidin alpha-L-rhamnoside + H2O
scilliphaeosidin + alpha-L-rhamnose
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-L-rhamnoside + H2O
alpha-L-rhamnose + ?
show the reaction diagram
gellan + H2O
alpha-L-rhamnose + ?
show the reaction diagram
Q93RE7
hydrolytic reaction, release of rhamnose from the disaccharide
-
-
?
gypenoside-5 + H2O
ginsenoside Rd + alpha-L-rhamnose
show the reaction diagram
Absidia sp.
-
-
-
-
?
quercitrin + H2O
quercetin + L-rhamnose
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2S,6R,8S,8aS)-6-methyloctahydroindolizine-1,2,8-triol
-
-
(2S,3R,4S)-benzyl-3,4-dihydroxy pyrrolidine
-
IC50 is 0.168 mM
(2S,3R,4S)-deacetyl anisomycin
-
IC50 is 0.137 mM
(2S,3S,4R)-benzyl-3,4-dihydroxy pyrrolidine
-
competitive
(2S,3S,4R)-deacetyl anisomycin
-
competitive
(2S,3S,4S)-2-methyl-3,4-dihydro-2H-pyrrole-3,4-diol
-
-
(2S,3S,4S)-2-methylpyrrolidine-3,4-diol
-
-
(2S,3S,4S)-anisomycin
-
competitive
(2S,3S,4S)-deacetyl anisomycin
-
competitive
(3S,4R)-3,4-dihydroxy-5-spirocyclopropyl-DELTA-pyrroline
-
-
(3S,4S)-3,4-dihydroxy-5-spirocyclopropyl-DELTA-pyrroline
-
72% inhibition at 1 mM
(6S,7S,8S)-4-azaspiro[2.5]octane-6,7,8-triol
-
72% inhibition at 1 mM
1,10-phenanthroline
less effective inhibitor, when the 1,10-phenanthroline concentration is raised to 10 mM, the activity of isoform RhaB1 decreases by 50%; less effective inhibitor, when the 1,10-phenanthroline concentration is raised to 10 mM, the activity of isoform RhaB2 decreases by 50%
4-Chloromercuriphenylsulfonate
-
strong inhibition
6-deoxy-D-glucose
alpha-L-rhamnose
Citric acid
-
no other organic acids, highest inhibition at low pH
CuCl2
D-glucose
ethanol
FeCl3
1 mM, 76% residual activity
five-membered ring azasugars
-
with L-rhamnose configuration, substitution at the nitrogen shifts the inhibition mechanism from mixed to competitive
-
HgCl2
L-fucose
L-Lyxose
-
competitive
L-Mannose
Bacteroides JY-6
-
competitive
L-rhamnose
methyl-alpha-D-mannoside
-
competitive
Mg2+
-
2 mM, 63% inhibition
p-chlormercuriphenylsulfonic acid
Bacteroides JY-6
-
modification of cysteines
p-chloromercuribenzoate
-
1 mM, 11% residual activity
p-chloromercuribenzoic acid
0.1 mM, 50% residual activity
p-hydroxymercuribenzoate
-
-
phosphoramidon
isoform RhaB1 shows 23.8% residual activity at 1 mM; isoform RhaB2 shows 42.5% residual activity at 1 mM
polyhexamethylene biguanide
1 mM reduces the activity of isoform RhaB1 to 10.9% and isoform RhaB2 to 36.0% residual activity; 1 mM reduces the activity of isoform RhaB1 to 10.9% residual activity
Sodium acetate
-
above 0.3 M , at pH 5
thiorphan
less effective inhibitor; less effective inhibitor
ZnCl2
1 mM, 73% residual activity
[4-([[(2S,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]methyl]amino)-5-hydroxy-6-methylpyridin-2-yl]methyl dihydrogen phosphate
-
-
[4-([[(2S,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl]amino)-5-hydroxy-6-methylpyridin-2-yl]methyl dihydrogen phosphate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-fructose
-
threefold activation
EDTA
a slight activating influence on isoform RhaB1 is observed for EDTA at 10 mM
additional information
L-rhamnose induces the enzyme at transcriptional level, mechanism
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057 - 6.1
4-nitrophenyl alpha-L-rhamnopyranoside
3.38
4-nitrophenyl-alpha-L-rhamnoside
-
pH 8.0, 55°C
2.2
6-O-alpha-L-rhamnosyl-D-glucopyranose
-
-
0.06 - 3.39
hesperidin
0.17 - 7
naringin
0.82
neohesperidin
Bacteroides JY-6
-
-
2 - 2.65
p-nitrophenyl alpha-L-rhamnoside
0.119 - 2.9
p-nitrophenyl-alpha-L-rhamnopyranoside
0.33 - 1.52
p-nitrophenyl-alpha-L-rhamnoside
0.93
poncirin
Bacteroides JY-6
-
-
0.07
proscillaridin A
-
-
0.077 - 0.89
quercitrin
0.13 - 1.77
rutin
0.88 - 1.6
saikosaponin C
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00003
(1R,2S,6R,8S,8aS)-6-methyloctahydroindolizine-1,2,8-triol
-
-
0.0029
(2S,3R,4S)-benzyl-3,4-dihydroxy pyrrolidine
-
pH 6.7, 30°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside
0.0026
(2S,3S,4R)-deacetyl anisomycin
-
pH 6.7, 30°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside
0.00014
(2S,3S,4S)-2-methyl-3,4-dihydro-2H-pyrrole-3,4-diol
-
-
0.0055
(2S,3S,4S)-2-methylpyrrolidine-3,4-diol
-
-
0.058
(2S,3S,4S)-anisomycin
-
pH 6.7, 30°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside
0.0029
(2S,3S,4S)-deacetyl anisomycin
-
pH 6.7, 30°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside
0.057
(3S,4R)-3,4-dihydroxy-5-spirocyclopropyl-DELTA-pyrroline
-
-
2
Cu2+
Bacteroides JY-6
-
-
1.28 - 19.88
L-rhamnose
2.6
prunin
-
pH 5.5, 40°C
0.0032
[4-([[(2S,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]methyl]amino)-5-hydroxy-6-methylpyridin-2-yl]methyl dihydrogen phosphate
-
-
0.003
[4-([[(2S,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl]amino)-5-hydroxy-6-methylpyridin-2-yl]methyl dihydrogen phosphate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.168
(2S,3R,4S)-benzyl-3,4-dihydroxy pyrrolidine
Penicillium decumbens
-
IC50 is 0.168 mM
0.137
(2S,3R,4S)-deacetyl anisomycin
Penicillium decumbens
-
IC50 is 0.137 mM
500
D-glucose
Pseudoalteromonas sp.
-
above, pH 7.8, 40°C
95
D-ribose
Pseudoalteromonas sp.
-
pH 7.8, 40°C
200
L-fucose
Pseudoalteromonas sp.
-
above, pH 7.8, 40°C
20
L-rhamnose
Pseudoalteromonas sp.
-
pH 7.8, 40°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.46
-
hesperidin
2.44
Absidia sp.
-
purified enzyme
2.89
-
purified enzyme
13.3
-
60°C, pH 5.5
17.9
substrate 4-nitrophenyl alpha-L-rhamnopyranoside, pH 4.0, 40°C
29.5
substrate hesperidin, pH 4.0, 40°C
82
-
p-nitrophenyl-alpha-L-rhamnopyranoside
85.3
substrate naringin, pH 4.0, 40°C
89.9
Bacteroides JY-6
-
-
108.9
Thermomicrobia bacterium
purified recombinant enzyme
263.9
Thermomicrobia bacterium
purified recombinant enzyme
526
-
pH 9.5, 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.9
Thermomicrobia bacterium
-
5.5 - 6.5
-
-
5.5 - 6.5
-
-
6.7
-
assay at
7.9
Thermomicrobia bacterium
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 10
Absidia sp.
-
40% of maximal activity at pH 4.0, 10% at pH 10.0
4 - 7.9
Thermomicrobia bacterium
50% of maximal activity at pH 4.0 and pH 7.9
4.4 - 5.5
isoform RhaB2 maintains over 60% of its activity in the pH range from 4.4 to 5.5
5 - 9
Bacteroides JY-6
-
-
5 - 7.5
isoform RhaB1 maintains over 60% of its activity in the pH range from 5.0 to 7.5
5 - 8.7
Thermomicrobia bacterium
50% of maximal activity at pH 5.0 and pH 8.7
5.5 - 9.5
Thermomicrobia bacterium
activity measured, no enzyme activity at pH 4.3 of cells on beads in contrast to measured activity of free cells
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 60
70
Thermomicrobia bacterium
;
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 40
-
activity measured, 6% activity maintained at 4°C, thermo-inactivation above 50°C
30 - 60
35 - 75
-
-
40 - 80
Thermomicrobia bacterium
low activity above; low activity above
50 - 60
-
-
50 - 70
70
-
74% of maximum activity
80
-
36% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
Thermomicrobia bacterium
sequence calculation
4.9
-
isoelectric focusing
5
-
isoelectric focusing
6
calculated from amino acid sequence; isoelectric focusing
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Thermomicrobia bacterium
recombinant Echerichia coli cells carrying the rhmA gene of Thermomicrobia bacterium
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus sp. (strain GL1)
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
-
4 * 41000, SDS-PAGE
68000
x * 90000, SDS-PAGE, x * 68000, calculated
70000
-
disc gel electrophoresis, gel filtration
87000
-
gel filtration, SDS-PAGE
88000
-
1 * 88000, SDS-PAGE
92000
x * 92000, SDS-PAGE
95000
-
SDS-PAGE, amino acid analysis
96000
-
x * 96000, SDS-PAGE
98000
5 * 98300, deduced from gene sequence, 5 * 98000, SDS-PAGE
98300
5 * 98300, deduced from gene sequence, 5 * 98000, SDS-PAGE
100000
102000
-
x * 102000, SDS-PAGE
104000
Thermomicrobia bacterium
2 * 104000, recombinant enzyme, SDS-PAGE
105000
1 * 106000, deduced from gene sequence, 1 * 105000, SDS-PAGE
106000
1 * 106000, deduced from gene sequence, 1 * 105000, SDS-PAGE
107000
Thermomicrobia bacterium
2 * 107000, recombinant enzyme, SDS-PAGE
109000
-
x * 109000, SDS-PAGE
112000
-
gel filtration, SDS-PAGE
120000
Bacteroides JY-6
-
2 * 120000, SDS-PAGE
170000
-
gel filtration
210000
Thermomicrobia bacterium
recombinant enzyme, gel filtration; recombinant enzyme, gel filtration
240000
Bacteroides JY-6
-
gel filtration, SDS-PAGE
500000
gel filtration, PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
crystallized form, 1908 amino acids of residues 3-956, 43 glycerol molecules, four calcium ions, 1755 water molecules identified in the crystallized form
monomer
pentamer
5 * 98300, deduced from gene sequence, 5 * 98000, SDS-PAGE
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native and selenomethionine-derivaties, 1.9 A resolution with a final R-factor of 18.2%, hanging-drop method, data-collection and statistics indicated, overall structure shown, quaternary structure, catalytic domain and active cleft determined, complex with the reaction product rhamnose determined and refined at 2.1 A with a final R-factor of 19.5%
-
native and selenomethionine-derivaties, crystallized at 293 K, hanging-drop vapour diffusion with PEG 8000 as a precipitant, data collection and statistics indicated
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 7
-
stable between, 21% loss of activity after 24 h at pH 2.0
136381
3 - 7
Absidia sp.
-
purified enzyme, stable
666777
3 - 5.5
-
RhaB retains over 85% of maximal activity
665264
3 - 8
-
-
136392
3 - 9
isoform RhaB1 remains active over a broad range of pH values, showing 90-100% remaining relative activities from pH 4.0 to 7.5, and over 40% at pH 3 and 9, after 5 h at 37°C; the stability of isoform RhaB2 is lower than that of isoform RhaB1, with 80-85% enzymatic activity from pH 5.0 to 7.0, and only 17% and 12% at pH 3.0 and 9.0, respectively
705564
3.5
-
naringinase complex, unstable below
695677
4 - 5.5
-
RhaA retains over 85% of maximal activity
665264
4.5 - 5
-
naringinase complex, most stable within this range
695677
5 - 7
-
-
654992
5.5 - 9
-
-
136399
7.5 - 9
-
24 h, without substrate, 95% residual activity
715802
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 40
-
stable below 40°C for 1 h
40 - 60
-
at low enzyme concentration, activity rapidly decreases within the first 30 min incubation time but afterwards remains stable at about 45% of the initial value for 5 h. Addition of bovine serum albumine or increasing enzyme concentration up to 0.1 g/l renders the enzyme stable for 5 h without initial losses of activity
40
Thermomicrobia bacterium
completely stable for 24 h at pH 5.0-6.9; loss of 22% activity within 24 h at pH 7.9
55 - 65
isoform RhaB2 retains 43% and 25% activity after 5 h incubation at 55°C and 65°C, respectively
57
-
immobilized enzyme, 6 months
70
-
2 h, 10% residual activity
75
4 h, 50% residual stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of bovine serum albumine or increasing enzyme concentration up to 0.1 g/l renders the enzyme stable for 5 h without initial losses of activity
-
pepstatin stabilizes
-
phenylmethanesulfonyl fluorid stabilizes
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CCl4
-
immobilized naringinase is stable
CH2Cl2
-
immobilized naringinase is stable
CHCl3
-
immobilized naringinase is stable
cyclohexane
-
immobilized naringinase is stable
ethylacetate
-
immobilized naringinase is stable
toluene
-
immobilized naringinase is stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several months, no loss of activity
-
3-5°C, pH 3.5, potassium hydrogen phthalate /HCl buffer, immobilized enzyme, 1 year, 10-15% loss of activity
-
stability of immobilized enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
buckwheat, partial
-
from cells grown on rhamnose as sole carbon source
-
gel filtration
Thermomicrobia bacterium
HiTrap chelating column chromatography, gel filtration; HiTrap chelating column chromatography, gel filtration
native and recombinant proteins, gel filtration, SDS-PAGE
-
native enzyme from strain FFDCL-90, by ammonium sulfate fractionation and ion exchange chromatography
Absidia sp.
-
of the recombinant protein
-
recombinant enzyme 63fold from Escherichia coli by heat treatment at 60°C, hydrophobic interaction and ion exchange chromatography; recombinant enzyme 85fold from Escherichia coli by heat treatment at 60°C, hydrophobic interaction and ion exchange chromatography
Thermomicrobia bacterium
recombinant protein, gel filtration, SDS-PAGE
-
recombinant Rham from Escherichia coli
saracen corn
-
to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834-DE3 containing pET3a-RhaB plasmid
-
expressed in Escherichia coli BL21 S1 cells; expressed in Escherichia coli BL21 S1 cells
expressed in Escherichia coli BL21-DE3 pRIL cells, recombinant strain of Echerichia coli carrying the rhmA gene from Thermomicrobia bacterium, immobilization on Ca2+ alginate beads and packaging the beads onto a column to design a bioreactor for production of rhamnose from naringin
Thermomicrobia bacterium
expressed in Escherichia coli strain HMS174-DE3, transformation with mutant plasmids, pD567N, pE572Q, pD579N, or pE841Q for mutant generation
-
expression in Escherichia coli
expression in Escherichia coli, gene has no homology to other glycoside hydrolases
-
gene rhaM, contsruction of a genomic library, DNA and mino acid sequence determination and analysis, expression in Escherichia coli
gene rhmA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli; gene rhmB, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
Thermomicrobia bacterium
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme activity is downregulated by D-glucose; the enzyme activity is downregulated by D-glucose
the enzyme activity is upregulated by L-rhamnose; the enzyme activity is upregulated by L-rhamnose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D567N
-
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
D579N
-
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
E572Q
-
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
E841Q
-
mutagenesis of catalytic amino acid residues identifed by crystallization studies, enzyme activity reduced
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
enzyme efficiently releases monoterpenols from an aroma precursor from muscat grape juice
degradation
-
recombinant rhamnosidase is thermostable and highly active for naringin hydrolysis up to more than 77%, thus producing L-rhamnose and prunin from citrus peel waste
nutrition
synthesis
Show AA Sequence (245 entries)
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