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Information on EC 3.2.1.B26 - Sulfolobus solfataricus beta-glycosidase and Organism(s) Saccharolobus solfataricus and UniProt Accession P22498

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Saccharolobus solfataricus
UNIPROT: P22498
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Saccharolobus solfataricus
Reaction Schemes
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Wide substrate specificity, active on aryl-beta-D-galactose, -alpha-L-fucose, -beta-D-glucose and -beta-D-xylose and on di- and oligosaccharides. D-Glucose dimers are hydrolysed in the order of decreasing efficiency: beta-(1,3), beta-(1,4), beta-(1,6). Exo-acting enzyme with a preference for cellotetraose.
Synonyms
beta-glycosidase, ssbetagly, beta-gly, sbetagly, sulfolobus solfataricus beta-glycosidase, sso1353, beta-d-glycosidase, ssbeta-gly, ssbetag, gh1 beta-glycosidase, more
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-galactoside
2-nitrophenol + D-galactose
show the reaction diagram
-
-
-
r
2-nitrophenyl beta-galactoside + H2O
2-nitrophenol + D-galactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-fucoside + H2O
4-methylumbelliferol + D-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-fucoside + H2O
4-methylumbelliferone + beta-D-fucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-galactoside + H2O
4-methylumbelliferone + beta-D-galactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-galacturonate + H2O
4-methylumbelliferone + beta-D-galacturonate
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + D-glucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferol + D-glucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferol + D-mannose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferone + beta-D-mannose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-xyloside + H2O
4-methylumbelliferol + D-xylose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-xyloside + H2O
4-methylumbelliferone + beta-D-xylose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + D-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-galactoside
4-nitrophenol + beta-D-galactose
show the reaction diagram
LacS shows 70% hydrolytic activity on nitrophenyl-beta-glucoside relative to the activity on nitrophenyl-beta-galactoside
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucoside
4-nitrophenol + beta-D-glucose
show the reaction diagram
LacS shows 70% hydrolytic activity on nitrophenyl-beta-glucoside relative to the activity on nitrophenyl-beta-galactoside
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenyl + D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-mannoside + H2O
4-nitrophenol + D-mannose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
show the reaction diagram
-
-
-
?
cellobiose + H2O
D-glucose + D-glucose
show the reaction diagram
-
-
-
?
ginsenoside C-Mc + H2O
?
show the reaction diagram
-
-
-
?
ginsenoside C-Mc1 + H2O
ginsenoside C-K + D-glucose + L-arabinofuranose
show the reaction diagram
-
-
-
?
ginsenoside C-O + H2O
ginsenoside C-K + D-glucose + L-arabinopyranose
show the reaction diagram
-
-
-
?
ginsenoside C-Y + H2O
ginsenoside C-K + L-arabinopyranose
show the reaction diagram
-
-
-
?
ginsenoside F2 + H2O
ginsenoside C-K + D-glucose
show the reaction diagram
highest activity
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + D-glucose
show the reaction diagram
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + D-glucose + L-arabinopyranose
show the reaction diagram
-
-
-
?
ginsenoside Rc + H2O
ginsenoside C-K + D-glucose + L-arabinofuranose
show the reaction diagram
-
-
-
?
ginsenoside Rd + H2O
ginsenoside C-K + ?
show the reaction diagram
-
-
-
?
ginsenoside Rd + H2O
ginsenoside C-K + D-glucose
show the reaction diagram
-
-
-
?
hesperidin + H2O
?
show the reaction diagram
-
-
-
?
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
methyl beta-D-galactoside
methanol + D-galactose
show the reaction diagram
-
-
-
r
naringin + H2O
?
show the reaction diagram
-
-
-
?
rebaudioside A + H2O
steviol + D-glucose
show the reaction diagram
negligible activity
-
-
?
rubusoside + H2O
steviol + D-glucose
show the reaction diagram
44.2% yield
-
-
?
stevioside + H2O
steviol + D-glucose
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl beta-D-glucopyranoside + H2O
2,4-dinitrophenol + beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl beta-D-glucopyranoside + H2O
2,4-dinitrophenol + D-glucopyranose
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 + beta-D-galactose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-galactose + H2O
2-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-galactoside + H2O
2-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylopyranose
show the reaction diagram
-
-
-
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
laminaribiose
-
?
3beta-[beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyloxy]-20-[beta-D-glucopyranosyl-(1->6)-beta-D-glucopyranosyloxy]dammar-24-en-12beta-ol + H2O
ginsenoside Rd + D-glucose
show the reaction diagram
-
i.e. ginsenoside Rb1
-
-
?
4-methylumbelliferyl beta-D-fucopyranoside + H2O
4-methylumbelliferone + beta-D-fucopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-glucuronic acid + H2O
4-methylumbelliferone + beta-D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
show the reaction diagram
-
14% of the activity compared to 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
show the reaction diagram
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
-
-
?
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
-
-
-
-
?
cellobiose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
cellobiose + H2O
beta-D-glucose + beta-D-glucose
show the reaction diagram
-
-
-
-
?
cellobiose + H2O
D-glucose + D-glucose
show the reaction diagram
-
-
-
-
?
cellotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
cellotetraose + H2O
cellotriose + D-glucose
show the reaction diagram
-
-
-
-
?
cellotriose + H2O
?
show the reaction diagram
-
-
-
-
?
gentiobiose + H2O
2 beta-D-glucose
show the reaction diagram
-
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside Rd + L-arabinopyranose
show the reaction diagram
-
i.e. 3beta-[beta-D-glucopyranosyl-(1->2)-beta-D glucopyranosyloxy]-20-[alpha-L-arabinopyranosyl-(1->6)-beta-D glucopyranosyloxy]dammar-24-en-12beta-ol
-
-
?
ginsenoside Rc + H2O
ginsenoside Mc + L-arabinofuranose
show the reaction diagram
-
i.e. 3beta-[beta-D-glucopyranosyl-(1->2)-beta-D glucopyranosyloxy]-20-[alpha-L-arabinofuranosyl-(1->6)-beta-D glucopyranosyloxy]dammar-24-en-12beta-ol
-
-
?
ginsenoside Rd + H2O
ginsenoside K + D-glucose
show the reaction diagram
-
i.e. 3beta-[beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyloxy]-20-(beta-D-glucopyranosyloxy)dammar-24-en-12beta-ol
-
-
?
lactose + H2O
beta-D-glucose + beta-D-galactose
show the reaction diagram
-
-
-
-
?
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
-
-
-
-
?
laminaribiose + H2O
3 beta-D-glucose
show the reaction diagram
-
-
-
-
?
laminaribiose + H2O
?
show the reaction diagram
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
show the reaction diagram
-
i.e. (4S,5E,6S)-4-[2-[2-(3,4-dihydroxyphenyl)ethoxy]-2-oxoethyl]-5-ethylidene-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)-2-tetrahydropyranyl]oxy]-4H-pyran-3-carboxylic acid methyl ester. The biotransformation produces unstable aglycone species formed by oleuropein hydrolysis that gives rise to the formation of hydroxytyrosol, at the operative temperatures of the bioreactor. The results of the biotransformation at 70°C showed that the main products are hydroxytyrosol, and glucose, being the oleuropein aglycone present in low amount at the end of reaction
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
laminaribiose
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
inhibits activity with 4-nitrophenyl beta-D-galactopyranoside
D-galactohydroximolactam
-
D-glucohydroximolactam
-
D-glucose
1,4-D-galactonolactone
-
0.1 M, 98% inhibition of beta-galactoside hydrolysis, 90% inhibition of beta-glucoside hydrolysis
1,4-dioxane
-
10% (v/v), decreases activity with 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-glucopyranoside or 4-nitrophenyl beta-D-fucopyranoside
1,5-D-gluconolactone
-
0.1 M, complete inhibition of beta-galactoside hydrolysis and beta-glucoside hydrolysis
2,4-dinitrophenyl-2-deoxy-2-fluoro-beta-D-glucoside
-
a mechanism-based inhibitor. 102fold molar excess, 80% inhibition of wild-type enzyme after 30 min and complete after overnight incubation. The E387G mutant enzyme is insensitive to the inhibitor
2,4-dinitrophenyl-beta-2-deoxy-2-fluoro-D-glucopyranoside
-
-
2-phenethyl glucoimidazole
-
-
4-nitrophenyl-beta-D-galactopyranoside
-
at low and intermediate temperatures (from 25°C to 50°C), the enzyme displays an inhibition by excess substrate and at high temperature (70 and 80°C) an activation, for 4-nitrophenyl-beta-D-galactopyranoside as substrate
Ba2+
-
the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
butan-2-one
-
10-20 (v/v)
Ca2+
-
the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
conduritol B epoxide
-
i.e. DL-1,2 anhydro-myo-inositol. The inhibitor is covalently bound to E387. Inhibitor-enzyme intermediate complex is formed more rapidly and hydrolyzed at a lower rate than it is for other glycosidases. One molecule of the inhibitor is covalently bound to each enzyme subunit
cyclophellitol
-
highly specific irreversible inhibitor of beta-glycosidases. Structural and dynamic aspects of beta-glycosidase from mesophilic and thermophilic bacteria by multitryptophanyl emission decay studies
D-arabinose
-
0.1 M, 64% inhibition of beta-galactoside hydrolysis, 20% inhibition of beta-glucoside hydrolysis
D-cellobiose
-
0.1 M, 79% inhibition of beta-galactoside hydrolysis, 25% inhibition of beta-glucoside hydrolysis
D-fucose
-
0.1 M, 58% inhibition of beta-galactoside hydrolysis, 23% inhibition of beta-glucoside hydrolysis
D-galactose
D-gluconic acid lactone
-
strong competitive inhibitor
D-glucose
-
0.1 M, 37% inhibition of beta-galactoside hydrolysis, slight activation of beta-glucoside hydrolysis
DL-1,2 anhydro-myo-inositol
-
the enzyme is fully inactivated at 65°C in presence of the inhibitor, according to pseudo-first-order kinetics. The process takes place through the formation of a stabilized inhibitor-enzyme intermediate. One molecule of the inhibitor is covalently bound to each enzyme subunit. The inhibitor iss covalently bound to E387
glucoimidazole
-
-
K+
-
the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
lactose
-
0.1 M, 41% inhibition of beta-galactoside hydrolysis, 18% inhibition of beta-glucoside hydrolysis
Li+
-
the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
Mg2+
-
the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
Na+
-
the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
Salicin
-
0.1 M, 97% inhibition of beta-galactoside hydrolysis, 92% inhibition of beta-glucoside hydrolysis
SDS
-
50°C, 30 min, 0.3% SDS, 40% loss of activity
tetrahydrofuran
-
5% (v/v), decreases activity with 4-nitrophenyl beta-D-galactopyranoside or 4-nitrophenyl beta-D-fucopyranoside
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-nitrophenyl-beta-D-galactopyranoside
-
at low and intermediate temperatures (from 25°C to 50°C), the enzyme displays an inhibition by excess substrate and at high temperature (70 and 80°C) an activation, for 4-nitrophenyl-beta-D-galactopyranoside as substrate
acetonitrile
-
maximal increase in enzyme activity at solvent concentrations of 15% (v/v) with 4-nitrophenyl beta-D-fucopyranoside as substrate
butan-2-one
-
maximum increase in enzyme activity (1.5fold compared to activity in buffer) is measured at 5% (v/v) solvent concentrations with 4-nitrophenyl beta-D-fucopyranoside as substrate
butanol
-
the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme
D-glucose
-
activated up to 2fold in the presence of D-glucose with respect to the maximum rate of glycosidic bond cleavage, measured with 2-nitrophenyl beta-D-galactoside as the substrate
ethanol
-
the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme
methanol
-
the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme
methyl acetate
Propanol
-
the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme
tetrahydrofuran
-
5% (v/v), increases activity with 2-nitrophenyl beta-D-galactopyranoside or 4-nitrophenyl beta-D-glucopyranoside
additional information
-
this enzyme appears to be activated by pressure between atmospheric pressure and 2.5 kbar with a maximal activity at 1.25 kbar. However, this enzyme still displayed the best catalytic efficiency at atmospheric pressure because of a Km value drastically increased by pressure
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
2.25
2-nitrophenyl beta-galactoside
at pH 6.0 and 80°C
0.011 - 18.6
4-methylumbelliferyl beta-D-fucoside
0.066 - 5.28
4-methylumbelliferyl beta-D-galactoside
1.3 - 3.46
4-methylumbelliferyl beta-D-galacturonate
0.046 - 22.1
4-methylumbelliferyl beta-D-glucoside
1.3
4-methylumbelliferyl beta-D-glucuronide
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.036 - 24.2
4-methylumbelliferyl beta-D-mannoside
0.13 - 13.7
4-methylumbelliferyl beta-D-xyloside
0.21 - 18.6
4-nitrophenyl beta-D-fucoside
1.57
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 70°C
0.57 - 5.28
4-nitrophenyl beta-D-galactoside
0.12 - 0.16
4-nitrophenyl beta-D-glucopyranoside
0.15 - 22.1
4-nitrophenyl beta-D-glucoside
24.2
4-nitrophenyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
5.1 - 13.7
4-nitrophenyl beta-D-xyloside
13.5
cellobiose
pH 5.0, 70°C
0.57 - 1.93
ginsenoside Rb1
0.52 - 1.59
ginsenoside Rd
15.82 - 196
lactose
192
methyl beta-D-galactoside
release of methanol, pH 7.5, 80°C
17.21
stevioside
at pH 6.0 and 80°C
0.17
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 65°C, wild-type enzyme
0.95 - 5.3
2-nitrophenyl beta-D-galactopyranoside
0.87
2-nitrophenyl beta-D-galactoside
-
pH 5.4, 75°C
0.5 - 16.4
2-nitrophenyl beta-D-glucopyranoside
0.03 - 1.01
2-Nitrophenyl beta-D-glucoside
3.9
2-nitrophenyl-beta-D-galactopyranoside
-
-
13
2-Nitrophenyl-beta-D-glucopyranoside
-
pH 5.5, 65°C
0.011 - 0.41
4-methylumbelliferyl beta-D-fucopyranoside
0.066 - 2.2
4-methylumbelliferyl beta-D-galactopyranoside
0.046 - 1.61
4-methylumbelliferyl beta-D-glucopyranoside
1.3 - 1.4
4-methylumbelliferyl beta-D-glucuronic acid
0.036 - 0.9
4-methylumbelliferyl beta-D-mannopyranoside
0.068 - 1.26
4-methylumbelliferyl beta-D-xylopyranoside
2.6
4-methylumbelliferyl-beta-D-glucopyranoside
-
pH 5.5, 65°C
1.2
4-methylumbelliferyl-beta-D-xylopyranoside
-
pH 5.5, 65°C
0.095 - 0.45
4-nitrophenyl beta-D-fucopyranoside
0.09 - 1
4-nitrophenyl beta-D-fucoside
0.77 - 4.79
4-nitrophenyl beta-D-galactopyranoside
0.59 - 47
4-nitrophenyl beta-D-galactoside
0.095 - 0.6
4-nitrophenyl beta-D-glucopyranoside
0.03 - 21
4-nitrophenyl beta-D-glucoside
0.3
4-nitrophenyl cellobioside
0.7
4-nitrophenyl-beta-D-fucoside
-
-
4.3
4-nitrophenyl-beta-D-galactopyranoside
-
-
0.085 - 54
4-nitrophenyl-beta-D-glucopyranoside
25
4-nitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 65°C
0.3
4-nitrophenyl-cellobioside
-
-
20 - 32.7
cellobiose
44 - 131
lactose
1.29 - 1.4
laminaribiose
169 - 240.4
oleuropein
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1300
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
24
2-nitrophenyl beta-galactoside
at pH 6.0 and 80°C
5.16 - 89
4-methylumbelliferyl beta-D-fucoside
0.047 - 98
4-methylumbelliferyl beta-D-galactoside
0.004 - 0.81
4-methylumbelliferyl beta-D-galacturonate
0.018 - 140
4-methylumbelliferyl beta-D-glucoside
0.81
4-methylumbelliferyl beta-D-glucuronide
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.92 - 2.8
4-methylumbelliferyl beta-D-mannoside
0.028 - 3.95
4-methylumbelliferyl beta-D-xyloside
5.16 - 9.43
4-nitrophenyl beta-D-fucoside
165
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 70°C
0.047 - 7.2
4-nitrophenyl beta-D-galactoside
4.2 - 45
4-nitrophenyl beta-D-glucopyranoside
0.018 - 38.65
4-nitrophenyl beta-D-glucoside
2.65
4-nitrophenyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
0.028 - 3.95
4-nitrophenyl beta-D-xyloside
23.2
cellobiose
pH 5.0, 70°C
1343 - 2257
ginsenoside Rb1
92 - 1049
ginsenoside Rd
8.37 - 1500
lactose
6.6
methyl beta-D-galactoside
release of methanol, pH 7.5, 80°C
1.62
stevioside
at pH 6.0 and 80°C
275
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 65°C, wild-type enzyme
34 - 2437
2-nitrophenyl beta-D-galactopyranoside
2400
2-nitrophenyl beta-D-galactoside
-
pH 5.4, 75°C
20.7 - 901.4
2-nitrophenyl beta-D-glucopyranoside
4.5 - 252
2-Nitrophenyl beta-D-glucoside
4.7
2-Nitrophenyl-beta-D-glucopyranoside
-
pH 5.5, 65°C
18 - 91
4-methylumbelliferyl beta-D-fucopyranoside
5.4 - 98
4-methylumbelliferyl beta-D-galactopyranoside
5.1 - 190
4-methylumbelliferyl beta-D-glucopyranoside
0.81 - 1.3
4-methylumbelliferyl beta-D-glucuronic acid
0.92 - 2.8
4-methylumbelliferyl beta-D-mannopyranoside
1.5 - 9.3
4-methylumbelliferyl beta-D-xylopyranoside
1.2
4-methylumbelliferyl-beta-D-glucopyranoside
-
pH 5.5, 65°C
0.8
4-methylumbelliferyl-beta-D-xylopyranoside
-
pH 5.5, 65°C
427 - 462
4-nitrophenyl beta-D-fucopyranoside
35 - 772
4-nitrophenyl beta-D-fucoside
31 - 2374
4-nitrophenyl beta-D-galactopyranoside
56 - 4380
4-nitrophenyl beta-D-galactoside
634 - 940
4-nitrophenyl beta-D-glucopyranoside
4.4 - 542
4-nitrophenyl beta-D-glucoside
448 - 503
4-nitrophenyl cellobioside
4.9 - 542
4-nitrophenyl-beta-D-glucopyranoside
4.3
4-nitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 65°C
547 - 746
cellobiose
524 - 573
laminaribiose
274 - 350.8
oleuropein
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1200
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
10.67
2-nitrophenyl beta-galactoside
at pH 6.0 and 80°C
0.053 - 7300
4-methylumbelliferyl beta-D-fucoside
0.0063 - 1490
4-methylumbelliferyl beta-D-galactoside
0.0006 - 0.06
4-methylumbelliferyl beta-D-galacturonate
0.015 - 2900
4-methylumbelliferyl beta-D-glucoside
0.6 - 5.1
4-methylumbelliferyl beta-D-glucuronide
0.001 - 76
4-methylumbelliferyl beta-D-mannoside
0.002 - 30
4-methylumbelliferyl beta-D-xyloside
0.068 - 42.6
4-nitrophenyl beta-D-fucoside
105
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 70°C
0.015 - 12.7
4-nitrophenyl beta-D-galactoside
26.25 - 375
4-nitrophenyl beta-D-glucopyranoside
0.036 - 29.8
4-nitrophenyl beta-D-glucoside
0.001 - 0.11
4-nitrophenyl beta-D-mannoside
0.002 - 0.77
4-nitrophenyl beta-D-xyloside
1.72
cellobiose
pH 5.0, 70°C
697 - 3967
ginsenoside Rb1
178 - 660
ginsenoside Rd
0.53 - 7.7
lactose
0.034
methyl beta-D-galactoside
release of methanol, pH 7.5, 80°C
0.094
stevioside
at pH 6.0 and 80°C
1617
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 65°C, wild-type enzyme
313.6 - 2137
2-nitrophenyl beta-D-galactopyranoside
2700
2-nitrophenyl beta-D-galactoside
-
pH 5.4, 75°C
18.5 - 850
2-nitrophenyl beta-D-glucopyranoside
53 - 7300
4-methylumbelliferyl beta-D-fucopyranoside
6.3 - 1490
4-methylumbelliferyl beta-D-galactopyranoside
15 - 2900
4-methylumbelliferyl beta-D-glucopyranoside
0.6 - 0.92
4-methylumbelliferyl beta-D-glucuronic acid
3.2 - 53
4-methylumbelliferyl beta-D-mannopyranoside
2.2 - 136
4-methylumbelliferyl beta-D-xylopyranoside
941 - 4863
4-nitrophenyl beta-D-fucopyranoside
370 - 2860
4-nitrophenyl beta-D-galactopyranoside
1400
4-nitrophenyl beta-D-galactoside
-
pH 5.4, 75°C
1058 - 4700
4-nitrophenyl beta-D-glucopyranoside
1764 - 11910
4-nitrophenyl-beta-D-glucopyranoside
19.2 - 37.3
cellobiose
407 - 410
laminaribiose
1.46 - 1.62
oleuropein
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000084
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
pH 5.0, 70°C, substrate: 4-nitrophenyl beta-D-galactopyranoside
0.0011
D-galactohydroximolactam
pH 6.5, 37°C
0.001
D-glucohydroximolactam
pH 6.5, 37°C
46
D-glucose
pH 5.0, 70°C, substrate: 4-nitrophenyl beta-D-galactopyranoside
5.5
2,4-dinitrophenyl-beta-2-deoxy-2-fluoro-D-glucopyranoside
-
pH 5.5, 65°C
0.25
conduritol B epoxide
-
pH 6.5, 65°C
366
D-galactose
-
pH 5.5, 80°C
0.025
D-gluconic acid lactone
-
pH 6.5, 60°C
0.25
DL-1,2 anhydro-myo-inositol
-
pH 6.5, 75°C
0.000053
glucoimidazole
-
pH 6.5, temperature not specified in the publication
12 - 13
Mg2+
-
pH 7.5, 75°C
additional information
2-phenethyl glucoimidazole
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0019
wild type enzyme, with ginsenoside C-Mc1 as substrate, at pH 5.5 and 95°C
0.0072
mutant enzyme W361F, with ginsenoside C-Mc as substrate, at pH 5.5 and 95°C
0.012
mutant enzyme W361F, with ginsenoside C-Mc1 as substrate, at pH 5.5 and 95°C
0.0126
wild type enzyme, with ginsenoside C-Mc1 as substrate, at pH 5.5 and 95°C
0.0154
wild type enzyme, with ginsenoside C-Mc as substrate, at pH 5.5 and 95°C
0.0201
wild type enzyme, with ginsenoside Rc as substrate, at pH 5.5 and 95°C
0.0233
mutant enzyme W361F, with ginsenoside Rc as substrate, at pH 5.5 and 95°C
0.0355
mutant enzyme W361F, with naringin as substrate, at pH 5.5 and 95°C
0.0391
wild type enzyme, with hesperidin as substrate, at pH 5.5 and 95°C
0.0567
mutant enzyme L213A, with ginsenoside C-Mc1 as substrate, at pH 5.5 and 95°C
0.0661
wild type enzyme, with ginsenoside C-Mc as substrate, at pH 5.5 and 95°C
0.0802
mutant enzyme L213A, with ginsenoside Rd as substrate, at pH 5.5 and 95°C
0.146
mutant enzyme L213A, with ginsenoside C-Mc as substrate, at pH 5.5 and 95°C
0.211
wild type enzyme, with ginsenoside Rd as substrate, at pH 5.5 and 95°C
0.233
wild type enzyme, with naringin as substrate, at pH 5.5 and 95°C
0.288
mutant enzyme W361F, with hesperidin as substrate, at pH 5.5 and 95°C
0.338
wild type enzyme, with ginsenoside Rd as substrate, at pH 5.5 and 95°C
0.52
wild type enzyme, with ginsenoside Rb2 as substrate, at pH 5.5 and 95°C
0.54
mutant enzyme L213A, with ginsenoside Rb2 as substrate, at pH 5.5 and 95°C
0.58
pH 6.5, 75°C, enzyme immobilized on XAD-4
0.59
pH 6.5, 75°C, enzyme immobilized on XAD-16
1.18
mutant enzyme L213A, with ginsenoside C-Y as substrate, at pH 5.5 and 95°C
1.347
mutant enzyme W361F, with ginsenoside C-Y as substrate, at pH 5.5 and 95°C
1.415
mutant enzyme W361F, with ginsenoside Rd as substrate, at pH 5.5 and 95°C
1.643
wild type enzyme, with ginsenoside Rb2 as substrate, at pH 5.5 and 95°C
1.71
pH 6.5, 75°C, lyophilized enzyme
1.74
wild type enzyme, with ginsenoside C-Y as substrate, at pH 5.5 and 95°C
13.13
wild type enzyme, with ginsenoside F2 as substrate, at pH 5.5 and 95°C
13.227
mutant enzyme W361F, with ginsenoside F2 as substrate, at pH 5.5 and 95°C
13.65
mutant enzyme L213A, with ginsenoside Rb1 as substrate, at pH 5.5 and 95°C
2.031
mutant enzyme W361F, with ginsenoside C-O as substrate, at pH 5.5 and 95°C
2.22
pH 6.5, 75°C, addition of 1% (w/v) SDS
24.1
wild type enzyme, 1ith ginsenoside F2 as substrate, at pH 5.5 and 95°C
3.213
mutant enzyme W361F, with ginsenoside Rb1 as substrate, at pH 5.5 and 95°C
3.53
pH 6.5, 75°C, enzyme immobilized on Celite
33.4
mutant enzyme L213A, 1ith ginsenoside F2 as substrate, at pH 5.5 and 95°C
4.05
mutant enzyme L213A, with ginsenoside C-O as substrate, at pH 5.5 and 95°C
4.24
wild type enzyme, with ginsenoside C-O as substrate, at pH 5.5 and 95°C
4.388
wild type enzyme, with ginsenoside C-Y as substrate, at pH 5.5 and 95°C
5.082
wild type enzyme, with ginsenoside Rb1 as substrate, at pH 5.5 and 95°C
6.354
wild type enzyme, with ginsenoside C-O as substrate, at pH 5.5 and 95°C
8.56
wild type enzyme, with ginsenoside Rb1 as substrate, at pH 5.5 and 95°C
9.077
mutant enzyme W361F, with ginsenoside Rb2 as substrate, at pH 5.5 and 95°C
1.2
-
mutant E387G, substrate cellobiose, pH 3.0, 65°C
127
-
mutant E387G, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
15
-
mutant E387G, substrate 4-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
150
-
wild-type, substrate 4-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
19.1
-
wild-type, substrate 2-nitrophenyl beta-D-xylopyranoside, pH 3.0, 65°C
196
-
wild-type, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
2.5
-
mutant E387G, substrate 2-nitrophenyl beta-D-xylopyranoside, pH 3.0, 65°C
2.7
-
mutant E387G, substrate 2-nitrophenyl beta-D-galactopyranoside, pH 3.0, 65°C
219
-
wild-type, substrate 2-nitrophenyl beta-D-galactopyranoside, pH 3.0, 65°C
253
-
wild-type, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
61.9
-
wild-type, substrate cellobiose, pH 3.0, 65°C
63.3
-
mutant E387G, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6.5
-
at 65°C
5 - 5.5
-
at 75°C
5 - 6
-
soluble enzyme and immobilized enzymes
7 - 10
-
the increase of pH from 7.0 to 10.0 causes a strong reduction of the catalytic activity of Sbgly that becomes very low at alkaline pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
-
pH 4.0: about 60% of maximal activity at 75°C, pH 7.0: about 50% of maximal activity at 75°C
4.5 - 6.5
-
pH 4.5: about 80% of maximal activity, pH 6.5: about 70% of maximal activity
5.5 - 8.5
-
pH 5.5: about 50% of maximal activity, pH 8.5: about 50% of maximal activity
5.7 - 8
-
pH 5.6: about 45% of maximal activity, pH 8.0: about 55% of maximal activity
6 - 7.5
-
pH 6.0: about 45% of maximal activity, pH 7.0: optimum, pH 7.5: less than 10% of maximal activity
additional information
-
activity dependence on pH at 65°C and 75°C on 5 mM 4-nitrophenyl beta-D-galactoside
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 75
-
the specific activity of the mutant increases with temperature up to 75°C
30 - 80
-
enzyme immobilized on chitosan activated with glutaraldehyde shows an increase in the temperature range 30°C-80°C in 50 mM sodium phosphate buffer, pH 7.0
30 - 95
-
barely active at 30°C, optimal activity over 95°C
70 - 80
-
activity at 70°C is about 45% compared to the activity at 85°C. The temperatureactivity profiles of native and recombinant enzyme are almost indistinguishable using 2-nitrophenyl-beta-D-galactopyranoside
80 - 100
-
80°C: 65% of maximal activity, 100°C: 60% of maximal activity
80 - 120
-
80°C: about 40% of maximal activity, 110°C: 85% of maximal activity, 120°C: about 25% of maximal activity
95 - 145
-
95°C: about 45% of maximal activity, 145°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56690
quadrupole time-of-flight electrospray mass spectrometry
56692
x * 56692, calculated from sequence
220000
-
glycerol gradient centrifugation
240000
57000
-
2 * 57000, SDS-PAGE
60000
60000 - 65000
-
gel filtration
70000
-
x * 70000, SDS-PAGE
76000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 57000, SDS-PAGE
homotetramer
-
4 * 56000
monomer
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures, at approximately 2 A resolution, of the enzyme in complex with both covalently (derived from 2-fluoro-glycosides) and noncovalently (hydroximolactam) bound inhibitors
the crystal structure is determined using multiple isomorphous replacement assisted by solvent flattening, histogram equalisation and non-crystallographic symmetry averaging, and refined at 2.6 A resolution. the enzyme crystallises as a tetramer with 222 point group symmetry, one dyad of which is crystallographic, with a dimer in the asymmetric unit. Analysis of the structure reveals two features which differ significantly from mesophile proteins: (1) an unusually large proportion of surface ion-pairs involved in networks that cross-link sequentially separate structures on the protein surface, and (2) an unusually large number of solvent molecules buried in hydrophilic cavities between sequentially separate structures in the protein core. These factors suggest a model for hyperthermostability via resilience rather than rigidity
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E432C
F222A
the mutant shows 105% activity towards ginsenoside Rd compared to the wild type enzyme
F359A
the mutant shows 84% activity towards ginsenoside Rd compared to the wild type enzyme
G217A
the mutant converts ginsenoside Rc to ginsenoside Rd
G217N
the mutantconverts ginsenoside Rc to ginsenoside Rd
H342A
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
K219R
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
L213A
L213D
the mutant converts ginsenoside Rc to ginsenoside Rd
L213E
the mutant converts ginsenoside Rc to ginsenoside Rd
L213G
the mutant converts ginsenoside Rc to ginsenoside Rd
L213H
the mutant converts ginsenoside Rc to ginsenoside Rd
L213Q
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
L213S
the mutant converts ginsenoside Rc to ginsenoside Rd
L213W
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
S220A
the mutant shows 92% activity towards ginsenoside Rd compared to the wild type enzyme
V209A
the mutant shows 170% activity towards ginsenoside Rd compared to the wild type enzyme
V209G
the mutant shows 60% activity towards ginsenoside Rd compared to the wild type enzyme
V209L
the mutant shows 10% activity towards ginsenoside Rd compared to the wild type enzyme
V209T
the mutant shows 80% activity towards ginsenoside Rd compared to the wild type enzyme
W361A
the mutant shows 241% activity towards ginsenoside Rd compared to the wild type enzyme
W361F
the mutant exhibits 4.2fold higher activity, 3.7fold higher catalytic efficiency, and 3.1fold lower binding energy for ginsenoside Rd than the wild type enzyme. The mutant completely converts ginsenoside Rb1 to compound K and shows also 7.4fold higher activity for hesperidin than the wild type enzyme
W361G
the mutant shows about 290% activity towards ginsenoside Rd compared to the wild type enzyme
W361L
the mutant shows about 40% activity towards ginsenoside Rd compared to the wild type enzyme
W361T
the mutant shows about 350% activity towards ginsenoside Rd compared to the wild type enzyme
W361Y
the mutant shows about 230% activity towards ginsenoside Rd compared to the wild type enzyme
W433C
D406G
-
inactive mutant
D458G
-
inactive mutant
D462G
-
inactive mutant. Addition of 1 mM NaN3 rescues enzymatic activity using 2-nitrophenyl-beta-D-glucopyranoside as substrate. Activity is 7fold lower compared to wild-type
delHis489
-
mutation produces faster enzyme inactivation, kcat/KM for 2-nitrophenyl beta-D-galactopyranoside is 45% of the wild-type value
delVal484-His489
-
clone DELTA6 lacks the last six amino acids (-Val-Lys-Pro-Leu-Arg-His-COOH) and has no additional mutations. Mutation produces faster enzyme inactivation, kcat/KM for 2-nitrophenyl beta-D-galactopyranoside is 37% of the wild-type value
E206Q
E335G
-
inactive mutant
E386G
-
mutation in nucleophile residue E387, mutation completely abolishes activity under statndard conditions. The addition of 2 M sodium formate as an external nucleophile leads to the recovery of 8.40% 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
E387A
-
inactive mutant enzyme of the catalytic nucleophile Glu387 is restored by externally added nucleophiles (sodium azide and sodium formate)
E387G
-
inactive mutant enzyme of the catalytic nucleophile Glu387 is restored by externally added nucleophiles (sodium azide and sodium formate)
E387Q
E432C
-
kcat/KM is reduced for 4-methylumbelliferyl beta-D-glucopyranoside is reduced 200fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-galactopyranoside is reduced 130fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-mannopyranoside is reduced 16fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-xylopyranoside is reduced 14fold
H489A
-
mutation produces faster enzyme inactivation, kcat/KM for 2-nitrophenyl beta-D-galactopyranoside is 85% of the wild-type value
M439C
-
shows almost identical values to wild-type for 4-methylumbelliferyl beta-D-glucopyranoside, 4-methylumbelliferyl beta-D-galactopyranoside or 4-methylumbelliferyl beta-D-mannopyranoside substrates. kcat/KM for 4-methylumbelliferyl beta-D-fucopyranoside is 1.8-fold lower than wild-type value and kcat/KM for 4-methylumbelliferyl beta-D-xylopyranoside is 4.7fold higher than wild-type
N97C
-
mutation causes some changes in the structural and dynamic properties as observed by circular dichroism in far- and near-UV light, as well as by frequency domain fluorometry, with a simultaneous loss of thermostability
R488A
-
mutation produces faster enzyme inactivation, kcat/KM for 2-nitrophenyl beta-D-galactopyranoside is 90% of the wild-type value
S101C
-
mutation causes some changes in the structural and dynamic properties as observed by circular dichroism in far- and near-UV light, as well as by frequency domain fluorometry, with a simultaneous loss of thermostability
W433C
-
kcat/KM is reduced for 4-methylumbelliferyl beta-D-glucopyranoside is reduced 140fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-galactopyranoside is reduced 230fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-mannopyranoside is reduced 10fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-xylopyranoside is reduced 12fold
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
when the enzyme is exposed at pH 10 its structure is affected to various extents. The perturbation occurs independently on thee probes used and is detectableby fluorescence, CD spectra in the far- and near-UV regions and infrared spectroscopy
724477
3.4
-
75°C, half-life is less than 5 min, irreversible aggregation
722214
6.5
-
no denaturation occurrs in the temperature range of 30 to 100°C for both the native and recombinant enzyme
722128
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
1.5 h, no residual activity
92
half-life: less than 3 min
100
-
investigation of the activity and conformational dynamics above 100°C. The data indicate a strong correlation between enzyme activity and protein flexibility. In particular, the time-resolved fluorescence data point out that some regions of the protein structure are very sensitive to the temperature increases, gaining a high flexibility degree with temperature. On the other hand, it is also possible to identify local environments of the enzyme structure that still possess a relatively high rigidity at 125°C
30 - 100
-
pH 6.5, no denaturation occurrs in the temperature range of 30 to 100°C for both the native and recombinant enzyme
5
-
after a storage greater than 40 h at atmospheric pressure, the residual activity decreases
97 - 98
-
Tm-value for recombinant enzyme
98 - 99
-
Tm-value for native enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
18.2% of the enzyme is inactivated in the immobilisation process on lyophilised chitosan matrix
-
chaotropes (I-, ClO4-, NO3- and Cs+) have a strong destabilising effect on the protein by perturbing hydrophobic interactions
-
denaturing effect of NaCl and Na2SO4
-
half-life times of the enzyme in hydrolysis of lactose is carried out at 70°C in a continuous stirred-tank reactor coupled to a 10000 Da cross-flow ultrafiltration module (to recycle the enzyme) is approximately 5 to 7 days
-
highly barostable enzyme
-
in Escherichia coli
-
N-epsilon-methylated beta-glycosidase from Sulfolobus solfataricus is characterized by a higher resistance to aggregation and denaturation at physiological pH, in comparison with the unmethylated form recombinantly expressed
-
stable in the presence of detergents
-
the enzyme can be immobilized with little loss of enzyme activity and catalytic efficiency by covalent coupling of the proteins via the surface amino groups to insoluble carriers
-
the stability of the bioreactor at the operative temperatures shows a t1/2 of 30 days at 70°C and a t1/2 of 56 days at 60°C
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
-
guanidine-induced denaturation is reversible when the protein concentration is lower than 0.01 mg/ml. In the range 2-4 M guanidine-HCl, there is an equilibrium among tetrameric, dimeric, and monomeric species. These findings indicate that the guanidine-induced denaturation is not a two-state transition with concomitant unfolding and dissociation of the four subunits. A mechanism involving a dimeric intermediate species is proposed and is able to fit the experimental fluorescence intensity transition profiles, allowing the estimation of the total denaturation Gibbs energy change at 25°C and pH 6.5
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 50 mM sodium phosphate buffer, pH 7.0, 50% glycerol, no appreciable loss of activity even after several months
-
4°C, enzyme immobilized on chitosan activated with glutaraldehyde, stable for 2 months, 20% loss of activity after 4 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Trap column chromatography, and Superdex 200 gel filtration
Ni-Sepharose column chromatography
His6-tagged mutant enzyme
-
purification of mutant proteins E206Q and E387Q to homogeneity using the Schistosoma japonicum glutathione S-transferase fusion system
-
purification of mutant proteins E206Q and E387Q to homogeneity using the Schistosoma japonicum glutathione-S-transferase fusion system
-
purification of the expressed beta-glycosidase by cell autolysis and thermal precipitation of extracts
-
to homogeneity, recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli Rosetta BL21(DE3)pLyS cells
expressed in Escherichia coli strain ER2566
expression in Escherichia coli
wild-type and mutated sequences are expressed in Escherichia coli with a His7-tag to allow one-step chromatographic purification
wild-type enzyme and mutant enzymes E432C and W433C are expressed in Escherichia coli with a His7-tag to allow one-step chromatographic purification
cloned and expressed in Saccharomyces cerevisiae
-
expressed in Escherichia coli
-
expressed in Saccharomyces cerevisiae
-
expression in Escherichia coli BL21
-
expression in Saccharomyces cerevisiae
-
mutant S101C is expressed in Escherichia coli
-
overexpressed in Escherichia coli
-
wild-type and mutant enzymes are ontained by expression as fusions of glutathione S-transferase in Escherichia coli
-
wild-type, mutant E432C, mutant W433C and mutant M439C enzymes are expressed in Escherichia coli as recombinant proteins containing an N-terminal His6-tag
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induction when cells which were maintained in sucrose minimal medium with yeast extract are down shifted to sucrose minimal medium without yeast extract addtion. An increase is evident after 2 h of incubation and reaches maximum levels 6 h after the shift. An active mechanism is employed for induction of lacS expression. Levels of lacS mRNA are reduced 20fold as a consequence of yeast extract medium supplementation to sucrose minimal medium. A passive mechanism involving cell dilution is used to repress lacS expression
levels of lacS mRNA are reduced 20fold as a consequence of yeast extract medium supplementation to sucrose minimal medium. A passive mechanism involving cell dilution is used to repress lacS expression
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
guanidine-induced denaturation is reversible when the protein concentration is lower than 0.01 mg/ml. In the range 2-4 M guanidine-HCl, there is an equilibrium among tetrameric, dimeric, and monomeric species. These findings indicate that the guanidine-induced denaturation is not a two-state transition with concomitant unfolding and dissociation of the four subunits. A mechanism involving a dimeric intermediate species is proposed and is able to fit the experimental fluorescence intensity transition profiles, allowing the estimation of the total denaturation Gibbs energy change at 25°C and pH 6.5
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
analysis
-
reporter genes in molecular biology
food industry
nutrition
-
catalyst of lactose hydrolysis in dairy products in the food industry
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
D'Auria, S.; Morana, A.; Febbraio, F.; Vaccaro, C.; De Rosa, M.; Nucci, R.
Functional and structural properties of the homogeneous beta-glycosidase from the extreme thermoacidophilic archaeon Sulfolobus solfataricus expressed in Saccharomyces cerevisiae
Protein Expr. Purif.
7
299-308
1996
Saccharolobus solfataricus
Manually annotated by BRENDA team
Cobucci-Ponzano, B.; Aurilia, V.; Riccio, G.; Henrissat, B.; Coutinho, P.M.; Strazzulli, A.; Padula, A.; Corsaro, M.M.; Pieretti, G.; Pocsfalvi, G.; Fiume, I.; Cannio, R.; Rossi, M.; Moracci, M.
A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2
J. Biol. Chem.
285
20691-20703
2010
Saccharolobus solfataricus
Manually annotated by BRENDA team
D'Auria, S.; Barone, R.; Rossi, M.; Nucci, R.; Barone, G.; Fessas, D.; Bertoli, E.; Tanfani, F.
Effects of temperature and SDS on the structure of beta-glycosidase from the thermophilic archaeon Sulfolobus solfataricus
Biochem. J.
323
833-840
1997
Saccharolobus solfataricus
Manually annotated by BRENDA team
D'Auria, S.; Nucci, R.; Rossi, M.; Gryczynski, I.; Gryczynski, Z.; Lakowicz, J.R.
The beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: enzyme activity and conformational dynamics at temperatures above 100 degrees C
Biophys. Chem.
81
23-31
1999
Saccharolobus solfataricus
Manually annotated by BRENDA team
Haseltine, C.; Montalvo-Rodriguez, R.; Carl, A.; Bini, E.; Blum, P.
Extragenic pleiotropic mutations that repress glycosyl hydrolase expression in the hyperthermophilic archaeon Sulfolobus solfataricus
Genetics
152
1353-1361
1999
Saccharolobus solfataricus, Saccharolobus solfataricus 98/2
Manually annotated by BRENDA team
Petzelbauer, I.; Splechtna, B.; Nidetzky, B.
Galactosyl transfer catalyzed by thermostable beta-glycosidases from Sulfolobus solfataricus and Pyrococcus furiosus: kinetic studies of the reactions of galactosylated enzyme intermediates with a range of nucleophiles
J. Biochem.
130
341-349
2001
Saccharolobus solfataricus
Manually annotated by BRENDA team
Aguilar, C.F.
Sanderson, I.; Moracci, M.; Ciaramella, M.; Nucci, R.; Rossi, M.; Pearl, L.H.: Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability
J. Mol. Biol.
271
789-802
1997
Saccharolobus solfataricus
Manually annotated by BRENDA team
Moracci, M.; Capalbo, L.; Ciaramella, M.; Rossi, M.
Identification of two glutamic acid residues essential for catalysis in the beta-glycosidase from the thermoacidophilic archaeon Sulfolobus solfataricus
Protein Eng.
9
1191-1195
1996
Saccharolobus solfataricus, Saccharolobus solfataricus MT4
Manually annotated by BRENDA team
D'Auria, S.; Rossi, M.; Nucci, R.; Irace, G.; Bismuto, E.
Perturbation of conformational dynamics, enzymatic activity, and thermostability of beta-glycosidase from archaeon Sulfolobus solfataricus by pH and sodium dodecyl sulfate detergent
Proteins
27
71-79
1997
Saccharolobus solfataricus
Manually annotated by BRENDA team
Cobucci-Ponzano, B.; Moracci, M.; Lauro, B.; Ciaramella, M.; DAvino, R.; Rossi, M.
Ionic network at the C-terminus of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Functional role in the quaternary structure thermal stabilization
Proteins
48
98-106
2002
Saccharolobus solfataricus
Manually annotated by BRENDA team
Bismuto, E.; Febbraio, F.; Limongelli, S.; Briante, R.; Nucci, R.
Dynamic fluorescence studies of β-glycosidase mutants from Sulfolobus solfataricus: Effects of single mutations on protein thermostability
Proteins
51
10-20
2003
Saccharolobus solfataricus
Manually annotated by BRENDA team
Grogan, D.W.
Evidence that beta-galactosidase of Sulfolobus solfataricus is only one of several activities of a thermostable beta-D-glycosidase
Appl. Environ. Microbiol.
57
1644-1649
1991
Saccharolobus solfataricus, Saccharolobus solfataricus P2
Manually annotated by BRENDA team
Shames, A.I.; Nucci, R.; D'Auria, S.; Febbraio, F.; Vaccaro, C.; Lozinsky, E.; Rossi, M.; Likhtenshtein, G.I.
EPR spin labeling study of conformational transitions of beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus expressed in Escherichia coli
Appl. Magn. Reson.
18
515-526
2000
Saccharolobus solfataricus
-
Manually annotated by BRENDA team
Cobucci-Ponzano, B., Perugino, G., Trincone, A., Mazzone, M., Di Lauro, B., Giordano, A., Rossi, M., Moracci, M.
Applications in biocatalysis of glycosyl hydrolases from the hyperthermophilic archaeon Sulfolobus solfataricus
Biocatal. Biotransform.
21
215-221
2003
Saccharolobus solfataricus
-
Manually annotated by BRENDA team
Moracci, M.; Nucci, R.; Febbraio, F.; Vaccaro, C.; Vespa, N.; La Cara, F.; Rossi, M.
Expression and extensive characterization of a beta-glycosidase from the extreme thermoacidophilic archaeon Sulfolobus solfataricus in Escherichia coli: authenticity of the recombinant enzyme
Enzyme Microb. Technol.
17
992-997
1995
Saccharolobus solfataricus
Manually annotated by BRENDA team
Petzelbauer, I.; Reiter, A.; Splechtna, B.; Kosma, P.; Nidetzky, B.
Transgalactosylation by thermostable beta-glycosidases from Pyrococcus furiosus and Sulfolobus solfataricus. Binding interactions of nucleophiles with the galactosylated enzyme intermediate make major contributions to the formation of new beta-glycosides
Eur. J. Biochem.
267
5055-5066
2000
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617 (P22498)
Manually annotated by BRENDA team
Pouwels, J.; Moracci, M.; Cobucci-Ponzano, B.; Perugino, G.; van der Oost, J.; Kaper, T.; Lebbink, J.H.; de Vos, W.M.; Ciaramella, M.; Rossi, M.
Activity and stability of hyperthermophilic enzymes: a comparative study on two archaeal beta-glycosidases
Extremophiles
4
157-164
2000
Saccharolobus solfataricus
Manually annotated by BRENDA team
D'Auria, S.; Pellino, F.; La Cara, F.; Barone, R.; Rossi, M.; Nucci, R.
Immobilization on chitosan of a thermophilic beta-glycosidase expressed in Saccharomyces cerevisiae
Appl. Biochem. Biotechnol.
61
157-166
1996
Saccharolobus solfataricus
Manually annotated by BRENDA team
Tricone, A.; Improta, R.; Gambacorta, A.
Enzymatic synthesis of polyol- and masked polyol-glycosides using beta-glycosidase of Sulfolobus
Biocatal. Biotransform.
12
77-88
1995
Saccharolobus solfataricus, Saccharolobus solfataricus DSM 5833
-
Manually annotated by BRENDA team
Huneke, F.-U.; Nucci, R.; Cowan, D.
Effect of water miscible organic solvents on kinetics of a thermostable beta-glycosidase
Biocatal. Biotransform.
17
251-267
1999
Saccharolobus solfataricus
-
Manually annotated by BRENDA team
Hansson, T.; Adlercreutz, P.
Enzymatic synthesis of hexyl glycosides from lactose at low water activity and high temperature using hyperthermostable beta-glycosidases
Biocatal. Biotransform.
20
167-178
2002
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus P2 (P22498)
-
Manually annotated by BRENDA team
Kaper, T.; Brouns, S.J.; Geerling, A.C.; De Vos, W.M.; Van der Oost, J.
DNA family shuffling of hyperthermostable beta-glycosidases
Biochem. J.
368
461-470
2002
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus P2 (P22498)
Manually annotated by BRENDA team
Febbraio, F.; Barone, R.; D'Auria, S.; Rossi, M.; Nucci, R.; Piccialli, G.; De Napoli, L.; Orru, S.; Pucci, P.
Identification of the active site nucleophile in the thermostable beta-glycosidase from the archaeon Sulfolobus solfataricus expressed in Escherichia coli
Biochemistry
36
3068-3075
1997
Saccharolobus solfataricus
Manually annotated by BRENDA team
Catanzano, F.; Graziano, G.; De Paola, B.; Barone, G.; D'Auria, S.; Rossi, M.; Nucci, R.
Guanidine-induced denaturation of beta-glycosidase from Sulfolobus solfataricus expressed in Escherichia coli
Biochemistry
37
14484-14490
1998
Saccharolobus solfataricus
Manually annotated by BRENDA team
Moracci, M.; Trincone, A.; Perugino, G.; Ciaramella, M.; Rossi, M.
Restoration of the activity of active-site mutants of the hyperthermophilic beta-glycosidase from Sulfolobus solfataricus: dependence of the mechanism on the action of external nucleophiles
Biochemistry
37
17262-17270
1998
Saccharolobus solfataricus
Manually annotated by BRENDA team
Gloster, T.M.; Roberts, S.; Ducros, V.M.; Perugino, G.; Rossi, M.; Hoos, R.; Moracci, M.; Vasella, A.; Davies, G.J.
Structural studies of the beta-glycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors
Biochemistry
43
6101-6109
2004
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P22498)
Manually annotated by BRENDA team
Gloster, T.M.; Roberts, S.; Perugino, G.; Rossi, M.; Moracci, M.; Panday, N.; Terinek, M.; Vasella, A.; Davies, G.J.
Structural, kinetic, and thermodynamic analysis of glucoimidazole-derived glycosidase inhibitors
Biochemistry
45
11879-11884
2006
Saccharolobus solfataricus
Manually annotated by BRENDA team
Hamon, V.; Dallet, S.; Legoy, M.D.
The pressure-dependence of two beta-glucosidases with respect to their thermostability
Biochim. Biophys. Acta
1294
195-203
1996
Saccharolobus solfataricus
Manually annotated by BRENDA team
D'Auria, S.; Moracci, M.; Febbraio, F.; Tanfani, F.; Nucci, R.; Rossi, M.
Structure-function studies on beta-glycosidase from Sulfolobus solfataricus. Molecular bases of thermostability
Biochimie
80
949-957
1989
Saccharolobus solfataricus
Manually annotated by BRENDA team
Noh, K.H.; Son, J.W.; Kim, H.J., Oh, D.K.
Ginsenoside compound K production from ginseng root extract by a thermostable beta-glycosidase from Sulfolobus solfataricus
Biosci. Biotechnol. Biochem.
73
316-321
2009
Saccharolobus solfataricus
Manually annotated by BRENDA team
Morana, A.; Moracci, M.; Ottombrino, A.; Ciaramella, M.; Rossi, M.; De Rosa, M.
Industrial-scale production and rapid purification of an archaeal beta-glycosidase expressed in Saccharomyces cerevisiae
Biotechnol. Appl. Biochem.
22
261-268
1995
Saccharolobus solfataricus
Manually annotated by BRENDA team
Santin, M.; Rosso, F.; Sada, A.; Peluso, G.; Improta, R.; Trincone, A.
Enzymatic synthesis of 2-beta-D-galactopyranosyloxy ethyl methacrylate (GalEMA) by the thermophilic archeon Sulfolobus solfataricus
Biotechnol. Bioeng.
49
217-222
1996
Saccharolobus solfataricus
Manually annotated by BRENDA team
Petzelbauer, I.; Nidetzky, B.; Haltrich, D.; Kulbe, K.D.
Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable beta-glycosidases
Biotechnol. Bioeng.
64
322-332
1999
Saccharolobus solfataricus
Manually annotated by BRENDA team
Petzelbauer, I.; Zeleny, R.; Reiter, A.; Kulbe, K.D.; Nidetzky, B.
Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose: II. Oligosaccharide formation by two thermostable beta-glycosidases
Biotechnol. Bioeng.
69
140-149
2000
Saccharolobus solfataricus
Manually annotated by BRENDA team
Petzelbauer, I.; Splechtna, B.; Nidetzky, B.
Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. III. Utilization of two thermostable beta-glycosidases in a continuous ultrafiltration membrane reactor and galacto-oligosaccharide formation under steady-state conditions
Biotechnol. Bioeng.
77
394-404
2002
Saccharolobus solfataricus
Manually annotated by BRENDA team
Petzelbauer, I.; Kuhn, B.; Splechtna, B.; Kulbe, K.D.; Nidetzky, B.
Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable beta-glycosidases and optimization of a packed-bed reactor for lactose conversion
Biotechnol. Bioeng.
77
619-631
2002
Saccharolobus solfataricus
Manually annotated by BRENDA team
Hansson, T.; Adlercreutz, P.
The temperature influences the ratio of glucosidase and galactosidase activities of beta-glycosidases
Biotechnol. Lett.
24
1465-1471
2002
Saccharolobus solfataricus
-
Manually annotated by BRENDA team
Trincone, A.; Giordano, A.; Perugino, G.; Rossi, M.; Moracci, M.
Highly productive autocondensation and transglycosylation reactions with Sulfolobus solfataricus glycosynthase
Chembiochem
6
1431-1437
2005
Saccharolobus solfataricus
Manually annotated by BRENDA team
Hancock, S.M.; Corbett, K.; Fordham-Skelton, A.P.; Gatehouse, J.A.; Davis, B.G.
Developing promiscuous glycosidases for glycoside synthesis: residues W433 and E432 in Sulfolobus solfataricus beta-glycosidase are important glucoside- and galactoside-specificity determinants
Chembiochem
6
866-875
2005
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P22498)
Manually annotated by BRENDA team
Reuter, S.; Rusborg Nygaard, A.; Zimmermann, W.
beta-Galactooligosaccharide synthesis with beta-galactosidases from Sulfolobus solfataricus, Aspergillus oryzae, and Escherichia coli
Enzyme Microb. Technol.
25
509-516
1999
Saccharolobus solfataricus
-
Manually annotated by BRENDA team
Bismuto, E.; Nucci, R.; Febbraio, F.; Tanfani, F.; Gentile, F.; Briante, R.; Scire, A.; Bertoli, E.; Amodeo, P.
Effects induced by mono- and divalent cations on protein regions responsible for thermal adaptation in beta-glycosidase from Sulfolobus solfataricus
Eur. Biophys. J.
33
38-49
2004
Saccharolobus solfataricus
Manually annotated by BRENDA team
Bismuto, E.; Irace, G.; D'Auria, S.; Rossi, M.; Nucci, R.
Multitryptophan-fluorescence-emission decay of beta-glycosidase from the extremely thermophilic archaeon Sulfolobus solfataricus
Eur. J. Biochem.
244
53-58
1997
Saccharolobus solfataricus
Manually annotated by BRENDA team
Corbett, K.; Fordham-Skelton, A.P.; Gatehouse, J.A.; Davis, B.G.
Tailoring the substrate specificity of the beta-glycosidase from the thermophilic archaeon Sulfolobus solfataricus
FEBS Lett.
509
355-360
2001
Saccharolobus solfataricus
Manually annotated by BRENDA team
Haseltine, C.; Montalvo-Rodriguez, R.; Bini, E.; Carl, A.; Blum, P.
Coordinate transcriptional control in the hyperthermophilic archaeon Sulfolobus solfataricus
J. Bacteriol.
181
3920-3927
1999
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P22498)
Manually annotated by BRENDA team
D'Auria, S.; Rossi, M.; Barone, G.; Catanzano, F.; Del Vecchio, P.; Graziano, G.; Nucci, R.
Temperature-induced denaturation of beta-glycosidase from the archaeon Sulfolobus solfataricus
J. Biochem.
120
292-300
1996
Saccharolobus solfataricus, Saccharolobus solfataricus MT4
Manually annotated by BRENDA team
Febbraio, F.; Andolfo, A.; Tanfani, F.; Briante, R.; Gentile, F.; Formisano, S.; Vaccaro, C.; Scire, A.; Bertoli, E.; Pucci, P.; Nucci, R.
Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon the N-epsilon-methylation of specific lysyl residues: critical role of in vivo post-translational modifications
J. Biol. Chem.
279
10185-10194
2003
Saccharolobus solfataricus, Saccharolobus solfataricus MT4
Manually annotated by BRENDA team
Briante, R.; La Cara, F.; Febbraio, F.; Barone, R.; Piccialli, G.; Carolla, R.; Mainolfi, P.; De Napoli, L.; Patumi, M.; Fontanazza, G.; Nucci, R.
Hydrolysis of oleuropein by recombinant beta-glycosidase from hyperthermophilic archaeon Sulfolobus solfataricus immobilised on chitosan matrix
J. Biotechnol.
77
275-286
2000
Saccharolobus solfataricus
Manually annotated by BRENDA team
Lozinsky, E.; Febbraio, F.; Shames, A.I.; Likhtenshtein, G.I.; Bismuto, E.; Nucci, R.
Heterogeneity in the structural dynamics of Sulfolobus solfataricus beta-glycosidase revealed by electron paramagnetic resonance and frequency domain fluorometry
Protein Sci.
11
2535-2544
2002
Saccharolobus solfataricus
Manually annotated by BRENDA team
Bismuto, E.; Martelli, P.L.; Casadio, R.; Irace, G.
Tryptophanyl fluorescence lifetime distribution of hyperthermophilic beta-glycosidase from molecular dynamics simulation: a comparison with the experimental data
Protein Sci.
9
1730-1742
2000
Saccharolobus solfataricus
Manually annotated by BRENDA team
Bismuto, E.; Nucci, R.; Rossi, M.; Irace, G.
Structural and dynamic aspects of beta-glycosidase from mesophilic and thermophilic bacteria by multitryptophanyl emission decay studies
Proteins
35
163-172
1999
Saccharolobus solfataricus
Manually annotated by BRENDA team
Tricone, A.M.; Pagnotta, E.; Rossi, M.; Mazzone, M.; Moracci., M.
Enzymatic synthesis of 2-deoxy-beta-glucosides and stereochemistry of beta-glycosidase from Sulfolobus solfataricus on glucal
Tetrahedron Asymmetry
12
2783-2787
2001
Saccharolobus solfataricus
-
Manually annotated by BRENDA team
Nucci, R.; Moracci, M.; Vaccaro, C.; Vespa, N.; Rossi, M.
Exo-glucosidase activity and substrate specificity of the beta-glycosidase isolated from the extreme thermophile Sulfolobus solfataricus
Biotechnol. Appl. Biochem.
17
239-250
1993
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
-
Manually annotated by BRENDA team
Perugino, G.; Trincone, A.; Giordano, A.; van der Oost, J.; Kaper, T.; Rossi, M.; Moracci, M.
Activity of hyperthermophilic glycosynthases is significantly enhanced at acidic pH
Biochemistry
42
8484-8493
2003
Saccharolobus solfataricus
Manually annotated by BRENDA team
Shin, K.C.; Choi, H.Y.; Seo, M.J.; Oh, D.K.
Improved conversion of ginsenoside Rb to compound K by semi-rational design of Sulfolobus solfataricus beta-glycosidase
AMB Express
7
186
2017
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
Manually annotated by BRENDA team
Nguyen, T.T.; Kim, S.B.; Kim, N.M.; Kang, C.; Chung, B.; Park, J.S.; Kim, D.
Production of steviol from steviol glucosides using beta-glycosidase from Sulfolobus solfataricus
Enzyme Microb. Technol.
93-94
157-165
2016
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
Manually annotated by BRENDA team
Choi, J.H.; Shin, K.C.; Oh, D.K.
An L213A variant of beta-glycosidase from Sulfolobus solfataricus with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to compound K
PLoS ONE
13
e0191018
2018
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
Manually annotated by BRENDA team
Shin, K.; Choi, H.; Seo, M.; Oh, D.
Compound K production from red ginseng extract by beta-glycosidase from Sulfolobus solfataricus supplemented with alpha-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus
PLoS ONE
10
e0145876
2015
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
Manually annotated by BRENDA team