Information on EC 3.2.1.B34 - Sulfolobus acidocaldarius beta-glycosidase

for references in articles please use BRENDA:EC3.2.1.B34
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The expected taxonomic range for this enzyme is: Sulfolobus

EC NUMBER
COMMENTARY hide
3.2.1.B34
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Sulfolobus acidocaldarius beta-glycosidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
show the reaction diagram
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-
-
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl beta-D-fucopyranoside + H2O
2-nitrophenol + D-fucopyranose
show the reaction diagram
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranose
show the reaction diagram
-
-
-
?
2-nitrophenyl beta-D-galactoside
2-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
r
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
show the reaction diagram
4-nitrophenyl alpha-L-arabinoside + H2O
4-nitrophenol + L-arabinopyranose
show the reaction diagram
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + D-fucopyranose
show the reaction diagram
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
show the reaction diagram
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannopyranose
show the reaction diagram
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
show the reaction diagram
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
-
-
?
4-nitrophenyl beta-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
show the reaction diagram
cellobiose + H2O
2 D-glucose
show the reaction diagram
ginsenoside Rb1 + H2O
ginsenoside Rd + ?
show the reaction diagram
ginsenoside Rb2 + H2O
ginsenoside Y + D-glucopyranose
show the reaction diagram
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hydrolysis of the 3-O-beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyl linkage in panaxadiol, activity is higher than hydrolysis of the 20-O-alpha-L-arabinopyranosyl-(1->6)-beta-D-glucopyranose linkage in ginsenoside Y
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-
?
ginsenoside Rc + H2O
ginsenoside Mc + D-glucopyranose
show the reaction diagram
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hydrolysis of the 3-O-beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyl linkage in panaxadiol, activity is higher than hydrolysis of the 20-O-alpha-L-arabinopyranosyl-(1->6)-beta-D-glucopyranose linkage in ginsenoside Y
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-
?
ginsenoside Rd + H2O
ginsenoside K + D-glucopyranose
show the reaction diagram
ginsenoside Y + H2O
ginsenoside K + L-arabinopyranose
show the reaction diagram
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hydrolysis of alpha-L-arabinopyranose linkage in 20-O-alpha-L-arabinopyranosyl-(1->6)-beta-D-glucopyranose, activity is lower than hydrolysis of the 3-O-beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyl linkage in panaxadiol
-
-
?
lactose + H2O
D-galactose + D-glucose
show the reaction diagram
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
-
-
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r
methyl beta-D-galactoside
methanol + beta-D-galactose
show the reaction diagram
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-
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r
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-galactose
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endproduct inhibition, inhibition of enzymeactivity was stronger with glucose than galactose
D-glucose
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endproduct inhibition, inhibition of enzyme activity is stronger with glucose than galactose
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butanol
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maximal activation is induced by 80 mM 1-butanol (130%). The activation at 30'C becomes less with increasing temperature and at 75C is only 10%. Alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
1-propanol
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alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
ethanol
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alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
methanol
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alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.116
2-nitrophenyl beta-D-fucopyranoside
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pH 5.5, 90C
0.5 - 11
2-nitrophenyl beta-D-galactopyranoside
1.1
2-nitrophenyl beta-D-galactoside
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release of 2-nitrophenol, pH 7.5, 80C
0.138
2-nitrophenyl beta-D-glucopyranoside
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pH 5.5, 90C
0.139
4-nitrophenyl beta-D-fucopyranoside
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pH 5.5, 90C
1.45
4-nitrophenyl beta-D-galactopyranoside
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pH 5.5, 90C
0.318
4-nitrophenyl beta-D-glucopyranoside
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pH 5.5, 90C
196
lactose
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release of D-glucose, pH 7.5, 80C
192
methyl beta-D-galactoside
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relase, of methanol, pH 7.5, 80C
additional information
cellobiose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26.4
2-nitrophenyl beta-D-fucopyranoside
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pH 5.5, 90C
24 - 1450
2-nitrophenyl beta-D-galactopyranoside
1300
2-nitrophenyl beta-D-galactoside
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release of 2-nitrophenol, pH 7.5, 80C
16.7
2-nitrophenyl beta-D-glucopyranoside
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pH 5.5, 90C
18.6
4-nitrophenyl beta-D-fucopyranoside
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pH 5.5, 90C
9.01
4-nitrophenyl beta-D-galactopyranoside
-
pH 5.5, 90C
14.6
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.5, 90C
1500
lactose
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release of D-glucose, pH 7.5, 80C
6.6
methyl beta-D-galactoside
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relase, of methanol, pH 7.5, 80C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
228
2-nitrophenyl beta-D-fucopyranoside
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pH 5.5, 90C
9.9 - 330
2-nitrophenyl beta-D-galactopyranoside
1200
2-nitrophenyl beta-D-galactoside
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release of 2-nitrophenol, pH 7.5, 80C
121
2-nitrophenyl beta-D-glucopyranoside
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pH 5.5, 90C
134
4-nitrophenyl beta-D-fucopyranoside
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pH 5.5, 90C
6.2
4-nitrophenyl beta-D-galactopyranoside
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pH 5.5, 90C
46
4-nitrophenyl beta-D-glucopyranoside
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pH 5.5, 90C
7.7
lactose
-
release of D-glucose, pH 7.5, 80C
0.034
methyl beta-D-galactoside
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relase, of methanol, pH 7.5, 80C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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mutant V212D, at 100 g/l cellobiose, pH 5.0, 50C
62
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mutant N211D, at 100 g/l cellobiose, pH 5.0, 50C
173
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mutant V212D, at 100 g/l lactose, pH 5.0, 50C
189
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wild-type, at 100 g/l cellobiose, pH 5.0, 50C
262
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mutant N211D, at 100 g/l lactose, pH 5.0, 50C
278
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wild-type, at 100 g/l lactose, pH 5.0, 50C
321
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mutant V212T, at 100 g/l cellobiose, pH 5.0, 50C
383
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mutant V212T, at 100 g/l lactose, pH 5.0, 50C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.5
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pH 5.5: about 80% of maximal activity, pH 6.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84
-
mutant N211D, substrate cellobiose
92
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wild-type, mutant N211D and V212T, substrate lactose; wild-type, substrate cellobiose
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80 - 100
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80C: about 70% of maximal activity, 100C: about 40% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
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2 * 57000, SDS-PAGE
57143
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2 * 57143, calculated from sequence
114000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
half-lfe: 494 h
80
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half-lfe: 60 h
90
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half-lfe: 0.2 h
92
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mutant V212T, 30 min, 50% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable in the presence of detergents
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N211D
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mutation changes the polarity close to the putative acid/base catalyst E209, leads to decrease in activity
V212D
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mutation changes the polarity close to the putative acid/base catalyst E209, shifts the pH-activity profile towards acidic pH with both lactose and cellobiose as substrates and leads to decrease in activity
V212T
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mutation changes the polarity close to the putative acid/base catalyst E209, shifts the pH-activity profile towards acidic pH with both lactose and cellobiose as substrates. Although V212T increases 6fold the Kmvalue with cellobiose, the mutant shows higher specific activity in high substrate concentrations due to greatly reduced produc-tion of trisaccharide by V212T from cellobiose by transglycosylation
N211D
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mutation changes the polarity close to the putative acid/base catalyst E209, leads to decrease in activity
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V212D
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mutation changes the polarity close to the putative acid/base catalyst E209, shifts the pH-activity profile towards acidic pH with both lactose and cellobiose as substrates and leads to decrease in activity
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V212T
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mutation changes the polarity close to the putative acid/base catalyst E209, shifts the pH-activity profile towards acidic pH with both lactose and cellobiose as substrates. Although V212T increases 6fold the Kmvalue with cellobiose, the mutant shows higher specific activity in high substrate concentrations due to greatly reduced produc-tion of trisaccharide by V212T from cellobiose by transglycosylation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
synthesis