Information on EC 1.1.99.B3 - glucooligosaccharide oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.99.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
glucooligosaccharide oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[beta-D-hexosyl-(1->4)]n-beta-D-hexose + acceptor = [beta-D-hexosyl-(1->4)]n-D-hexono-1,5-lactone + reduced acceptor
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
carbohydrate:acceptor oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated as fungal strain KD-3 from soil, identified as Paraconiothyrium sp. according to 18S rDNA and ITS-5.8 S rDNA analysis
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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
4-O-methyl-alpha-D-glucopyranosyl uronic acid-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + O2
4-O-methyl-alpha-D-glucopyranosyl uronic acid-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylono-1,5-lactone + H2O2
show the reaction diagram
6-deoxy-D-glucose + 2,6-dichlorophenol indophenol
?
show the reaction diagram
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hexoses as substrates determined, 2,6-dichlorophenol indophenol as electron acceptor
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?
6-deoxy-D-glucose + O2
?
show the reaction diagram
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hexoses as substrates determined
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?
alpha-L-arabinofuranosyl-(1->2)-[alpha-L-arabinofuranosyl-(1->3)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose + O2
alpha-L-arabinofuranosyl-(1->2)-[alpha-L-arabinofuranosyl-(1->3)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylono-1,5-lactone + H2O2
show the reaction diagram
alpha-L-arabinofuranosyl-(1->3)-beta-D-xylopyranosyl-(1->4)-D-xylose + O2
alpha-L-arabinofuranosyl-(1->3)-beta-D-xylopyranosyl-(1->4)-D-xylono-1,5-lactone + H2O2
show the reaction diagram
arabinoxylan + O2
?
show the reaction diagram
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?
Avicel + O2
?
show the reaction diagram
beech wood xylan + O2
?
show the reaction diagram
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?
beta-(1->3,1->4)-glucan + O2
?
show the reaction diagram
beta-D-glucose + 2,6-dichlorophenol indophenol
D-glucono-1,5-lactone + ?
show the reaction diagram
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DCIP, electron acceptor specificity determined
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?
beta-D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
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kinetic parameters for various sugars shown, enzyme properties compared to other sugar oxidizing enzymes
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?
carboxymethyl cellulose + O2
?
show the reaction diagram
cello-oligosaccharide + acceptor
?
show the reaction diagram
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?
cellobiose + 2,6-dichlorophenol indophenol
?
show the reaction diagram
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disaccharides as substrates determined, 2,6-dichlorophenol indophenol as electron acceptor
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?
cellobiose + acceptor
?
show the reaction diagram
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?
cellobiose + O2
?
show the reaction diagram
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disaccharides as substrates determined
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?
cellobiose + O2
? + H2O2
show the reaction diagram
cellobiose + O2
cellobiono-1,5-lactone + H2O2
show the reaction diagram
cellohexaose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
cellohexaose + O2
cellohexaono-1,5-lactone + H2O2
show the reaction diagram
cellopentaose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
cellopentaose + O2
cellopentaono-1,5-lactone + H2O2
show the reaction diagram
cellotetraose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
cellotetraose + O2
cellotetraono-1,5-lactone + H2O2
show the reaction diagram
cellotriose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
cellotriose + O2
? + H2O2
show the reaction diagram
cellotriose + O2
cellotriono-1,5-lactone + H2O2
show the reaction diagram
cellulose + O2
?
show the reaction diagram
D-fructose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
D-galactose + 2,6-dichlorophenol indophenol
?
show the reaction diagram
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hexoses as substrates determined, 2,6-dichlorophenol indophenol as electron acceptor
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?
D-galactose + O2
?
show the reaction diagram
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hexoses as substrates determined
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?
D-galactose + O2
? + H2O2
show the reaction diagram
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-
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?
D-glucose + acceptor
?
show the reaction diagram
D-glucose + O2
? + H2O2
show the reaction diagram
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highest catalytic efficiency with D-glucose
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?
D-glucose + O2
D-glucono-1,5-lactone + H2O2
show the reaction diagram
D-mannose + O2
?
show the reaction diagram
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hexoses as substrates determined
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?
D-xylobiose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
D-xylose + 2,6-dichlorophenol indophenol
?
show the reaction diagram
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pentoses as substrates determined, 2,6-dichlorophenol indophenol as electron acceptor
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?
D-xylose + O2
?
show the reaction diagram
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pentoses as substrates determined
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?
D-xylose + O2
? + H2O2
show the reaction diagram
D-xylose + O2
D-xylono-1,5-lactone + H2O2
show the reaction diagram
debranched soluble oat spelt xylan + acceptor
?
show the reaction diagram
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?
glucomannan + O2
?
show the reaction diagram
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?
L-arabinose + 2,6-dichlorophenol indophenol
?
show the reaction diagram
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pentoses as substrates determined, 2,6-dichlorophenol indophenol as electron acceptor
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?
L-arabinose + O2
?
show the reaction diagram
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pentoses as substrates determined
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?
lactose + 2,6-dichlorophenol indophenol
?
show the reaction diagram
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substrate specificity for alpha-lactose and beta-lactose determined
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?
lactose + acceptor
?
show the reaction diagram
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?
lactose + O2
?
show the reaction diagram
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substrate specificity for alpha-lactose and beta-lactose determined
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?
malto-oligosaccharide + acceptor
?
show the reaction diagram
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?
maltohexaose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
maltopentaose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
maltose + 2,6-dichlorophenol indophenol
?
show the reaction diagram
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disaccharides as substrates determined, 2,6-dichlorophenol indophenol as electron acceptor
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?
maltose + acceptor
?
show the reaction diagram
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?
maltose + O2
?
show the reaction diagram
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disaccharides as substrates determined
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?
maltose + O2
? + H2O2
show the reaction diagram
maltose + O2
maltone-1,5-lactone + H2O2
show the reaction diagram
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?
maltotetraose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
maltotriose + O2
?
show the reaction diagram
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oligosaccharides as substrates determined
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?
N-acetyl-D-glucosamine + O2
? + H2O2
show the reaction diagram
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?
propoxylated wheat bran hemicellulose + O2
?
show the reaction diagram
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?
soluble oat spelt xylan + acceptor
?
show the reaction diagram
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?
wheat bran hemicellulose + O2
?
show the reaction diagram
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?
xylobiose + 2,6-dichlorophenol indophenol
?
show the reaction diagram
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disaccharides as substrates determined, 2,6-dichlorophenol indophenol as electron acceptor
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?
xylobiose + O2
?
show the reaction diagram
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disaccharides as substrates determined
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?
xylobiose + O2
? + H2O2
show the reaction diagram
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?
xylobiose + O2
xylobiono-1,5-lactone + H2O2
show the reaction diagram
xyloglucan + O2
?
show the reaction diagram
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?
xylohexaose + O2
xylohexaono-1,5-lactone + H2O2
show the reaction diagram
xylopentaose + O2
xylopentaono-1,5-lactone + H2O2
show the reaction diagram
xylotetraose + O2
xylotetraono-1,5-lactone + H2O2
show the reaction diagram
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?
xylotriose + O2
? + H2O2
show the reaction diagram
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?
xylotriose + O2
xylotriono-1,5-lactone + H2O2
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
cellobiose + O2
? + H2O2
show the reaction diagram
cellotriose + O2
? + H2O2
show the reaction diagram
D-galactose + O2
? + H2O2
show the reaction diagram
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-
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?
D-glucose + O2
? + H2O2
show the reaction diagram
-
highest catalytic efficiency with D-glucose
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?
D-xylose + O2
? + H2O2
show the reaction diagram
maltose + O2
? + H2O2
show the reaction diagram
N-acetyl-D-glucosamine + O2
? + H2O2
show the reaction diagram
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?
xylobiose + O2
? + H2O2
show the reaction diagram
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?
xylotriose + O2
? + H2O2
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H2O2
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about 40% inhibition at 200 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
4-O-methyl-alpha-D-glucopyranosyl uronic acid-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose
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wild type enzyme, at pH 8.0 and 37°C
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52 - 75
6-deoxy-D-glucose
0.078 - 0.09
alpha-L-arabinofuranosyl-(1->2)-[alpha-L-arabinofuranosyl-(1->3)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose
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0.052 - 0.059
alpha-L-arabinofuranosyl-(1->3)-beta-D-xylopyranosyl-(1->4)-D-xylose
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0.039 - 0.4
cellobiose
0.06 - 0.16
cellohexaose
0.03 - 0.15
Cellopentaose
0.06 - 0.26
Cellotetraose
0.05 - 0.44
cellotriose
36.1 - 132
D-galactose
3.11 - 31
D-glucose
2 - 288
D-xylose
47 - 85
L-arabinose
0.11 - 0.19
lactose
13 - 30
maltohexaose
11 - 32
maltopentaose
2.81 - 19.6
maltose
12 - 30
maltotetraose
18 - 30
maltotriose
56 - 950
N-acetyl-D-glucosamine
0.05 - 5.11
xylobiose
0.005 - 0.1
xylohexaose
0.05 - 0.104
xylopentaose
0.067 - 0.11
xylotetraose
0.08 - 4.3
xylotriose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
4-O-methyl-alpha-D-glucopyranosyl uronic acid-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose
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wild type enzyme, at pH 8.0 and 37°C
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0.45 - 0.81
6-deoxy-D-glucose
9 - 13.5
alpha-L-arabinofuranosyl-(1->2)-[alpha-L-arabinofuranosyl-(1->3)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose
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8.8 - 12.3
alpha-L-arabinofuranosyl-(1->3)-beta-D-xylopyranosyl-(1->4)-D-xylose
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0.22 - 13.7
cellobiose
1.1 - 13.2
cellohexaose
1.1 - 12.7
Cellopentaose
1.4 - 12.8
Cellotetraose
1.5 - 13.7
cellotriose
0.25 - 13.3
D-galactose
0.46 - 13.2
D-glucose
0.58 - 12.4
D-xylose
0.73 - 1.1
L-arabinose
4.4 - 6.3
lactose
0.35 - 0.57
maltohexaose
0.9 - 1.8
maltopentaose
0.76 - 10.4
maltose
2.3 - 2.6
maltotetraose
2.2 - 2.3
maltotriose
7.8 - 12.8
N-acetyl-D-glucosamine
3 - 14.8
xylobiose
7.8 - 15.2
xylohexaose
8.8 - 15.2
xylopentaose
8.1 - 16
xylotetraose
7.9 - 14.5
xylotriose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
36.5
4-O-methyl-alpha-D-glucopyranosyl uronic acid-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose
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wild type enzyme, at pH 8.0 and 37°C
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115 - 150
alpha-L-arabinofuranosyl-(1->2)-[alpha-L-arabinofuranosyl-(1->3)]-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylose
-
148.3 - 233.3
alpha-L-arabinofuranosyl-(1->3)-beta-D-xylopyranosyl-(1->4)-D-xylose
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30 - 306.7
cellobiose
66.7 - 150
cellohexaose
78.3 - 216.7
Cellopentaose
56.7 - 233.3
Cellotetraose
23.3 - 250
cellotriose
0.06 - 0.18
D-galactose
0.18 - 3.6
D-glucose
0.02 - 0.36
D-xylose
0.53 - 2.13
maltose
0.008 - 0.2
N-acetyl-D-glucosamine
2.48 - 300
xylobiose
73.3 - 300
xylohexaose
85 - 283.3
xylopentaose
73.3 - 233.3
xylotetraose
2.83 - 183.3
xylotriose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme purified and characterized, identified as a carbohydrate-acceptor oxidoreductase according to its molecular and structural properties and according to its specificity for electron donors and acceptors
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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most active at pH 5.5 if O2 is used as electron acceptor
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 7
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stable in a pH range of 2.0-7.0 at 30°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
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gel filtration, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
and wild-type proteins are 1.9 M, 2.4 M, 2.6 M, and 3.2 M, respectively.
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and wild-type proteins are 48°C, 52°C, 46°C, and 56°C, respectively.
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The melting temperatures for the H70A, C130A, H70A/C130A,
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the presence of the xylan-binding module CBM22A of Clostridium thermocellum fused to the N-terminal of the enzyme increases its catalytic activity on mono- and oligo-saccharides by 2-3fold while not affecting binding affinity to these substrates, does not alter the thermostability of the enzyme or reduces substrate inhibition
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The [guanidine HCl]1/2 values for the H70A, C130A, H70A/C130A,
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration, SDS-PAGE
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Ni-NTA resin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as fusion protein with carbohydrate binding modules CBM3, CBM11, and CBM44 from Clostridium thermocellum in Pichia pastoris GS115 cells
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expressed in Pichia pastoris KM71H
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expressed in Pichia pastoris strain GS115
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expressed in Pichia pastoris strain KM71H
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A38V
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the mutation significantly increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
A38V/S388N
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the mutation increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
C130A
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FAD binding site, FAD covalently attached
E247A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
H70A
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FAD binding site, FAD covalently attached
H70A/C130A
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no activity, lack of essential FAD cofactor
Q353A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q353N
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q384A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q384N
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
W351A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme; the mutation increases Km values by up to 2 orders of magnitude while also increasing kcat up to 3fold on cello- and xylo-oligosaccharides and showing no substrate inhibition compared to the wild type enzyme
W351F
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the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates
Y300N
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the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
Y310A
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larger amount of carbohydrates
Y72A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Y72F
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
A38V
-
the mutation significantly increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
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E247A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
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Q384A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
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W351F
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the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates
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Y300A
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the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
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Y300N
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the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
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Y72A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
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Y72F
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
-