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Information on EC 3.2.1.B34 - Sulfolobus acidocaldarius beta-glycosidase and Organism(s) Sulfolobus acidocaldarius and UniProt Accession P14288

for references in articles please use BRENDA:EC3.2.1.B34
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Sulfolobus acidocaldarius
UNIPROT: P14288
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The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
The expected taxonomic range for this enzyme is: Sulfolobaceae
Reaction Schemes
hide
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
Synonyms
BgaS, LACS, Saci_1849, Sbetagly, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Saci_1849
locus name
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 + D-galactopyranose
show the reaction diagram
-
-
-
?
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
17% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
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
8% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
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
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
-
-
?
ginsenoside Rc + H2O
ginsenoside Mc + D-glucopyranose
show the reaction diagram
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
-
-
?
ginsenoside Rd + H2O
ginsenoside K + D-glucopyranose
show the reaction diagram
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
the enzyme does not convert compound Mc to compound K due to no activity for the alpha-L-arabinofuranose linkage in 20-O-alpha-L-arabinofuranosyl-(1->6)-beta-D-glucopyranose
-
?
ginsenoside Y + H2O
ginsenoside K + L-arabinopyranose
show the reaction diagram
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
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-galactose
endproduct inhibition, inhibition of enzymeactivity was stronger with glucose than galactose
D-glucose
endproduct inhibition, inhibition of enzyme activity is stronger with glucose than galactose
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butanol
-
maximal activation is induced by 80 mM 1-butanol (130%). The activation at 30"C becomes less with increasing temperature and at 75°C 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
-
alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
ethanol
-
alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
methanol
-
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
pH 5.5, 90°C
3.18
2-nitrophenyl beta-D-galactopyranoside
pH 5.5, 90°C
0.138
2-nitrophenyl beta-D-glucopyranoside
pH 5.5, 90°C
0.139
4-nitrophenyl beta-D-fucopyranoside
pH 5.5, 90°C
1.45
4-nitrophenyl beta-D-galactopyranoside
pH 5.5, 90°C
0.318
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 90°C
0.5 - 11
2-nitrophenyl beta-D-galactopyranoside
additional information
cellobiose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26.4
2-nitrophenyl beta-D-fucopyranoside
pH 5.5, 90°C
31.5
2-nitrophenyl beta-D-galactopyranoside
pH 5.5, 90°C
16.7
2-nitrophenyl beta-D-glucopyranoside
pH 5.5, 90°C
18.6
4-nitrophenyl beta-D-fucopyranoside
pH 5.5, 90°C
9.01
4-nitrophenyl beta-D-galactopyranoside
pH 5.5, 90°C
14.6
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 90°C
24 - 1450
2-nitrophenyl beta-D-galactopyranoside
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
228
2-nitrophenyl beta-D-fucopyranoside
pH 5.5, 90°C
9.9
2-nitrophenyl beta-D-galactopyranoside
pH 5.5, 90°C
121
2-nitrophenyl beta-D-glucopyranoside
pH 5.5, 90°C
134
4-nitrophenyl beta-D-fucopyranoside
pH 5.5, 90°C
6.2
4-nitrophenyl beta-D-galactopyranoside
pH 5.5, 90°C
46
4-nitrophenyl beta-D-glucopyranoside
pH 5.5, 90°C
24 - 330
2-nitrophenyl beta-D-galactopyranoside
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
173
mutant V212D, at 100 g/l lactose, pH 5.0, 50°C
189
wild-type, at 100 g/l cellobiose, pH 5.0, 50°C
262
mutant N211D, at 100 g/l lactose, pH 5.0, 50°C
278
wild-type, at 100 g/l lactose, pH 5.0, 50°C
321
mutant V212T, at 100 g/l cellobiose, pH 5.0, 50°C
383
mutant V212T, at 100 g/l lactose, pH 5.0, 50°C
40
mutant V212D, at 100 g/l cellobiose, pH 5.0, 50°C
62
mutant N211D, at 100 g/l cellobiose, pH 5.0, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.5
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
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80 - 100
80°C: about 70% of maximal activity, 100°C: about 40% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
114000
gel filtration
57000
2 * 57000, SDS-PAGE
57143
2 * 57143, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N211D
mutation changes the polarity close to the putative acid/base catalyst E209, leads to decrease in activity
V212D
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
92
mutant V212T, 30 min, 50% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable in the presence of detergents
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
enzyme is a potential producer of the rare ginsenosides compound K, compound Y, and compound Mc from the major ginsenosides Rb1, Rb2, Rc, and Rd
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, A.R.; Kim, H.J.; Lee, J.K.; Oh, D.K.
Hydrolysis and transglycosylation activity of a thermostable recombinant beta-glycosidase from Sulfolobus acidocaldarius
Appl. Biochem. Biotechnol.
160
2236-2247
2010
Sulfolobus acidocaldarius (P14288), Sulfolobus acidocaldarius DSM 639 (P14288)
Manually annotated by BRENDA team
D'Auria, S.; Nucci, R.; Rossi, M.; Bertoli, E.; Tanfani, F.; Gryczynski, I.; Malak, H.; Lakowicz, J.R.
beta-Glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: structure and activity in the presence of alcohols
J. Biochem.
126
545-552
1999
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Noh, K.H.; Oh, D.K.
Production of the rare ginsenosides compound K, compound Y, and compound Mc by a thermostable beta-glycosidase from Sulfolobus acidocaldarius
Biol. Pharm. Bull.
32
1830-1835
2009
Sulfolobus acidocaldarius (P14288), Sulfolobus acidocaldarius DSM 639 (P14288)
Manually annotated by BRENDA team
Anbarasan, S.; Timoharju, T.; Barthomeuf, J.; Pastinen, O.; Rouvinen, J.; Leisola, M.; Turunen, O.
Effect of active site mutation on pH activity and transglycosylation ofSulfolobus acidocaldarius beta-glycosidase
J. Mol. Catal. B
118
62-69
2015
Sulfolobus acidocaldarius (P14288), Sulfolobus acidocaldarius DSM 639 (P14288)
-
Manually annotated by BRENDA team