Information on EC 3.2.1.B26 - Sulfolobus solfataricus beta-glycosidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.B26
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Sulfolobus solfataricus beta-glycosidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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.
show the reaction diagram
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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
2,4-dinitrophenyl beta-D-glucopyranoside + H2O
2,4-dinitrophenol + beta-D-glucopyranoside
show the reaction diagram
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-
-
-
?
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
2-nitrophenol + 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-glucopyranoside
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
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-
-
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
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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
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i.e. ginsenoside Rb1
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-
?
4-methylumbelliferyl beta-D-fucopyranoside + H2O
4-methylumbelliferone + beta-D-fucopyranose
show the reaction diagram
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-
-
-
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4-methylumbelliferyl beta-D-fucoside + H2O
4-methylumbelliferol + D-fucose
show the reaction diagram
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-
-
-
?
4-methylumbelliferyl beta-D-fucoside + H2O
4-methylumbelliferone + beta-D-fucose
show the reaction diagram
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-
-
-
?
4-methylumbelliferyl beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
show the reaction diagram
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-
-
-
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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
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-
-
-
?
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucopyranose
show the reaction diagram
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-
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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-glucuronic acid + H2O
4-methylumbelliferone + beta-D-glucuronic acid
show the reaction diagram
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-
-
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4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferol + D-glucose
show the reaction diagram
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-
-
-
?
4-methylumbelliferyl beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
show the reaction diagram
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-
-
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4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferol + D-mannose
show the reaction diagram
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-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferone + beta-D-mannose
show the reaction diagram
4-methylumbelliferyl beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
show the reaction diagram
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-
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4-methylumbelliferyl beta-D-xyloside + H2O
4-methylumbelliferol + D-xylose
show the reaction diagram
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-
-
-
?
4-methylumbelliferyl beta-D-xyloside + H2O
4-methylumbelliferone + beta-D-xylose
show the reaction diagram
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-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucopyranose
show the reaction diagram
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-
-
-
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
show the reaction diagram
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-
-
-
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
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-fucoside + H2O
4-nitrophenol + D-fucose
show the reaction diagram
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-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
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
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-glucopyranoside
show the reaction diagram
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-
-
-
?
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-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
4-nitrophenyl beta-D-glucoside
4-nitrophenol + beta-D-glucose
show the reaction diagram
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenyl + D-glucose
show the reaction diagram
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-
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?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucose
show the reaction diagram
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-
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?
4-nitrophenyl beta-D-mannoside + H2O
4-nitrophenol + D-mannose
show the reaction diagram
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-
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?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
show the reaction diagram
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-
-
-
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
show the reaction diagram
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-
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?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
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-
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?
4-nitrophenyl-beta-cellobioside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
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-
-
?
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
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-
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?
cellobiose + H2O
2 D-glucose
show the reaction diagram
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-
-
-
?
cellobiose + H2O
beta-D-glucose + beta-D-glucose
show the reaction diagram
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-
-
-
?
cellobiose + H2O
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
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-
-
-
?
cellotriose + H2O
?
show the reaction diagram
gentiobiose + H2O
2 beta-D-glucose
show the reaction diagram
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-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside Rd + L-arabinopyranose
show the reaction diagram
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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
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-
?
ginsenoside Rc + H2O
ginsenoside Mc + L-arabinofuranose
show the reaction diagram
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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
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-
?
ginsenoside Rd + H2O
ginsenoside K + D-glucose
show the reaction diagram
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i.e. 3beta-[beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyloxy]-20-(beta-D-glucopyranosyloxy)dammar-24-en-12beta-ol
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-
?
lactose + H2O
beta-D-glucose + beta-D-galactose
show the reaction diagram
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-
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?
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
laminaribiose + H2O
3 beta-D-glucose
show the reaction diagram
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-
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-
?
laminaribiose + H2O
?
show the reaction diagram
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-
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?
methyl beta-D-galactoside
methanol + D-galactose
show the reaction diagram
oleuropein + H2O
oleuropein aglycone + glucose
show the reaction diagram
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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 lowamount at the end of reaction
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?
additional information
?
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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
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
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laminaribiose
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?
INHIBITORS
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
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inhibits activity with 4-nitrophenyl beta-D-galactopyranoside
1,4-D-galactonolactone
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0.1 M, 98% inhibition of beta-galactoside hydrolysis, 90% inhibition of beta-glucoside hydrolysis
1,4-dioxane
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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
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0.1 M, complete inhibition of beta-galactoside hydrolysis and beta-glucoside hydrolysis
2,4-dinitrophenyl-2-deoxy-2-fluoro-beta-D-glucoside
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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
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2-phenethyl glucoimidazole
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4-nitrophenyl-beta-D-galactopyranoside
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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+
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the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
butan-2-one
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10-20 (v/v)
Ca2+
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the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
conduritol B epoxide
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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
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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
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0.1 M, 64% inhibition of beta-galactoside hydrolysis, 20% inhibition of beta-glucoside hydrolysis
D-cellobiose
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0.1 M, 79% inhibition of beta-galactoside hydrolysis, 25% inhibition of beta-glucoside hydrolysis
D-fucose
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0.1 M, 58% inhibition of beta-galactoside hydrolysis, 23% inhibition of beta-glucoside hydrolysis
D-galactohydroximolactam
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D-galactose
D-glucohydroximolactam
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-
D-gluconic acid lactone
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strong competitive inhibitor
D-glucose
DL-1,2 anhydro-myo-inositol
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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
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K+
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the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
lactose
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0.1 M, 41% inhibition of beta-galactoside hydrolysis, 18% inhibition of beta-glucoside hydrolysis
Li+
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the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
Mg2+
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the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
Na+
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the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
Salicin
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0.1 M, 97% inhibition of beta-galactoside hydrolysis, 92% inhibition of beta-glucoside hydrolysis
SDS
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50°C, 30 min, 0.3% SDS, 40% loss of activity
tetrahydrofuran
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5% (v/v), decreases activity with 4-nitrophenyl beta-D-galactopyranoside or 4-nitrophenyl beta-D-fucopyranoside
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-nitrophenyl-beta-D-galactopyranoside
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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
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maximal increase in enzyme activity at solvent concentrations of 15% (v/v) with 4-nitrophenyl beta-D-fucopyranoside as substrate
butan-2-one
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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
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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
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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
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the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme
methanol
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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
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5% (v/v), increases activity with 2-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside or 4-nitrophenyl beta-D-glucopyranoside; highest activation at solvent concentrations of 5% (v/v) with 4-nitrophenyl beta-D-fucopyranoside as substrate
Propanol
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the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme
tetrahydrofuran
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17
2,4-dinitrophenyl beta-D-glucopyranoside
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pH 6.5, 65°C, wild-type enzyme
0.95 - 5.3
2-nitrophenyl beta-D-galactopyranoside
0.87 - 1.1
2-nitrophenyl beta-D-galactoside
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
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13
2-Nitrophenyl-beta-D-glucopyranoside
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pH 5.5, 65°C
0.011 - 0.41
4-methylumbelliferyl beta-D-fucopyranoside
0.011 - 18.6
4-methylumbelliferyl beta-D-fucoside
0.066 - 2.2
4-methylumbelliferyl beta-D-galactopyranoside
0.066 - 5.28
4-methylumbelliferyl beta-D-galactoside
1.3 - 3.46
4-methylumbelliferyl beta-D-galacturonate
0.046 - 1.61
4-methylumbelliferyl beta-D-glucopyranoside
0.046 - 22.1
4-methylumbelliferyl beta-D-glucoside
1.3 - 1.4
4-methylumbelliferyl beta-D-glucuronic acid
1.3
4-methylumbelliferyl beta-D-glucuronide
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pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.036 - 0.9
4-methylumbelliferyl beta-D-mannopyranoside
0.036 - 24.2
4-methylumbelliferyl beta-D-mannoside
0.068 - 1.26
4-methylumbelliferyl beta-D-xylopyranoside
0.13 - 13.7
4-methylumbelliferyl beta-D-xyloside
2.6
4-methylumbelliferyl-beta-D-glucopyranoside
-
pH 5.5, 65°C
1.2
4-methylumbelliferyl-beta-D-xylopyranoside
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pH 5.5, 65°C
0.095 - 0.45
4-nitrophenyl beta-D-fucopyranoside
0.09 - 18.6
4-nitrophenyl beta-D-fucoside
0.77 - 4.79
4-nitrophenyl beta-D-galactopyranoside
0.57 - 47
4-nitrophenyl beta-D-galactoside
0.095 - 0.6
4-nitrophenyl beta-D-glucopyranoside
0.03 - 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
0.3
4-nitrophenyl cellobioside
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pH 6.5, 75°C, recombinant enzyme; pH 6.5, 75°C, wild-type enzyme
0.7
4-nitrophenyl-beta-D-fucoside
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-
4.3
4-nitrophenyl-beta-D-galactopyranoside
-
-
0.085 - 54
4-nitrophenyl-beta-D-glucopyranoside
25
4-nitrophenyl-beta-D-xylopyranoside
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pH 5.5, 65°C
0.3
4-nitrophenyl-cellobioside
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-
13.5 - 32.7
cellobiose
37.9 - 196
lactose
1.29 - 1.4
laminaribiose
192
methyl beta-D-galactoside
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release of methanol, pH 7.5, 80°C
169 - 240.4
oleuropein
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
275
2,4-dinitrophenyl beta-D-glucopyranoside
Sulfolobus solfataricus
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pH 6.5, 65°C, wild-type enzyme
34 - 2437
2-nitrophenyl beta-D-galactopyranoside
1300 - 2400
2-nitrophenyl beta-D-galactoside
20.7 - 901.4
2-nitrophenyl beta-D-glucopyranoside
4.5 - 252
2-Nitrophenyl beta-D-glucoside
4.7
2-Nitrophenyl-beta-D-glucopyranoside
Sulfolobus solfataricus
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pH 5.5, 65°C
18 - 91
4-methylumbelliferyl beta-D-fucopyranoside
5.16 - 89
4-methylumbelliferyl beta-D-fucoside
5.4 - 98
4-methylumbelliferyl beta-D-galactopyranoside
0.047 - 98
4-methylumbelliferyl beta-D-galactoside
0.004 - 0.81
4-methylumbelliferyl beta-D-galacturonate
5.1 - 190
4-methylumbelliferyl beta-D-glucopyranoside
0.018 - 140
4-methylumbelliferyl beta-D-glucoside
0.81 - 1.3
4-methylumbelliferyl beta-D-glucuronic acid
0.81
4-methylumbelliferyl beta-D-glucuronide
Sulfolobus solfataricus
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pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.92 - 2.8
4-methylumbelliferyl beta-D-mannopyranoside
0.92 - 2.8
4-methylumbelliferyl beta-D-mannoside
1.5 - 9.3
4-methylumbelliferyl beta-D-xylopyranoside
0.028 - 3.95
4-methylumbelliferyl beta-D-xyloside
1.2
4-methylumbelliferyl-beta-D-glucopyranoside
Sulfolobus solfataricus
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pH 5.5, 65°C
0.8
4-methylumbelliferyl-beta-D-xylopyranoside
Sulfolobus solfataricus
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pH 5.5, 65°C
427 - 462
4-nitrophenyl beta-D-fucopyranoside
5.16 - 772
4-nitrophenyl beta-D-fucoside
31 - 2374
4-nitrophenyl beta-D-galactopyranoside
0.047 - 4380
4-nitrophenyl beta-D-galactoside
4.2 - 940
4-nitrophenyl beta-D-glucopyranoside
0.018 - 542
4-nitrophenyl beta-D-glucoside
2.65
4-nitrophenyl beta-D-mannoside
Sulfolobus solfataricus
-
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
0.028 - 3.95
4-nitrophenyl beta-D-xyloside
448 - 503
4-nitrophenyl cellobioside
4.9 - 542
4-nitrophenyl-beta-D-glucopyranoside
4.3
4-nitrophenyl-beta-D-xylopyranoside
Sulfolobus solfataricus
-
pH 5.5, 65°C
23.2 - 746
cellobiose
121 - 1500
lactose
524 - 573
laminaribiose
6.6
methyl beta-D-galactoside
Sulfolobus solfataricus
-
release of methanol, pH 7.5, 80°C
274 - 350.8
oleuropein
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1617
2,4-dinitrophenyl beta-D-glucopyranoside
Sulfolobus solfataricus
-
pH 6.5, 65°C, wild-type enzyme
7613
313.6 - 2137
2-nitrophenyl beta-D-galactopyranoside
880
1200 - 2700
2-nitrophenyl beta-D-galactoside
7995
18.5 - 850
2-nitrophenyl beta-D-glucopyranoside
1098
53 - 7300
4-methylumbelliferyl beta-D-fucopyranoside
8974
0.053 - 7300
4-methylumbelliferyl beta-D-fucoside
4192
6.3 - 1490
4-methylumbelliferyl beta-D-galactopyranoside
8973
0.0063 - 1490
4-methylumbelliferyl beta-D-galactoside
3279
0.0006 - 0.06
4-methylumbelliferyl beta-D-galacturonate
12259
15 - 2900
4-methylumbelliferyl beta-D-glucopyranoside
2122
0.015 - 2900
4-methylumbelliferyl beta-D-glucoside
1709
0.6 - 0.92
4-methylumbelliferyl beta-D-glucuronic acid
19800
0.6 - 5.1
4-methylumbelliferyl beta-D-glucuronide
15417
3.2 - 53
4-methylumbelliferyl beta-D-mannopyranoside
3787
0.001 - 76
4-methylumbelliferyl beta-D-mannoside
4923
2.2 - 136
4-methylumbelliferyl beta-D-xylopyranoside
4179
0.002 - 30
4-methylumbelliferyl beta-D-xyloside
4191
941 - 4863
4-nitrophenyl beta-D-fucopyranoside
5389
0.068 - 42.6
4-nitrophenyl beta-D-fucoside
2121
105 - 2860
4-nitrophenyl beta-D-galactopyranoside
999
0.015 - 1400
4-nitrophenyl beta-D-galactoside
1586
26.25 - 4700
4-nitrophenyl beta-D-glucopyranoside
510
0.036 - 29.8
4-nitrophenyl beta-D-glucoside
712
0.001 - 0.11
4-nitrophenyl beta-D-mannoside
19548
0.002 - 0.77
4-nitrophenyl beta-D-xyloside
3041
1764 - 11910
4-nitrophenyl-beta-D-glucopyranoside
237
1.72 - 37.3
cellobiose
82
3.19 - 7.7
lactose
114
407 - 410
laminaribiose
875
0.034
methyl beta-D-galactoside
Sulfolobus solfataricus
-
release of methanol, pH 7.5, 80°C
45669
1.46 - 1.62
oleuropein
10260
additional information
additional information
2
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
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
0.0011
D-galactohydroximolactam
-
pH 6.5, 37°C
366
D-galactose
-
pH 5.5, 80°C
0.001
D-glucohydroximolactam
-
pH 6.5, 37°C
0.025
D-gluconic acid lactone
-
pH 6.5, 60°C
46
D-glucose
-
pH 5.0, 70°C, substrate: 4-nitrophenyl beta-D-galactopyranoside
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
0.58
-
pH 6.5, 75°C, enzyme immobilized on XAD-4
0.59
-
pH 6.5, 75°C, enzyme immobilized on XAD-16
1.2
-
mutant E387G, substrate cellobiose, pH 3.0, 65°C
1.71
-
pH 6.5, 75°C, lyophilized enzyme
2.22
-
pH 6.5, 75°C, addition of 1% (w/v) SDS
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
3.53
-
pH 6.5, 75°C, enzyme immobilized on Celite
15
-
mutant E387G, 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
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
127
-
mutant E387G, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
150
-
wild-type, substrate 4-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
166
-
; pH 6.5, 75°C
196
-
wild-type, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, 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
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
30 - 95
-
barely active at 30°C, optimal activity over 95°C
additional information
-
activity dependence on pH at 65°C and 75°C on 5 mM 4-nitrophenyl beta-D-galactoside
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
-
4 * 56000
56690
-
quadrupole time-of-flight electrospray mass spectrometry
56692
-
x * 56692, calculated from sequence
57000
-
2 * 57000, SDS-PAGE
60000 - 65000
-
gel filtration
70000
-
x * 70000, SDS-PAGE
75910
-
MALDI-TOF
76000
-
gel filtration
220000
-
glycerol gradient centrifugation
240000
SUBUNITS
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
after a storage greater than 40 h at atmospheric pressure, the residual activity decreases
30 - 100
-
pH 6.5, no denaturation occurrs in the temperature range of 30 to 100°C for both the native and recombinant enzyme
92
-
half-life: less than 3 min
97 - 98
-
Tm-value for recombinant enzyme
98 - 99
-
Tm-value for native enzyme
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
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
; to homogeneity, recombinant enzyme
-
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Saccharomyces cerevisiae
-
expressed in Escherichia coli
-
expressed in Escherichia coli; expression in Escherichia coli
-
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae
-
expression in Escherichia coli BL21
-
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 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
-
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
mutant shows 10- and 60-fold reduced activities on aryl-galacto and aryl-glucosides, respectively, when compared with the wild type. Significant decrease in Km-value with 4-nitrophenyl beta-D-glucoside or 2-nitrophenyl beta-D-glucoside. The residual activity of the mutant loses the typical pH dependence shown by the wild type. These data suggest that Glu206 acts as the general acid/base catalyst in the hydrolysis reaction; mutant shows 10- and 60-fold reduced activities on aryl-galacto and aryl-glucosides, respectively, when compared with the wild type. Significant decrease in Km-value with 4-nitrophenyl beta-D-glucoside or 2-nitrophenyl betaD-glucoside. The residual activity of the mutant loses the typical pH dependence shown by the wild type. These data suggest that Glu206 acts as the general acid/base catalyst in the hydrolysis reaction
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)
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
E206Q
-
mutant shows 10- and 60-fold reduced activities on aryl-galacto and aryl-glucosides, respectively, when compared with the wild type. Significant decrease in Km-value with 4-nitrophenyl beta-D-glucoside or 2-nitrophenyl beta-D-glucoside. The residual activity of the mutant loses the typical pH dependence shown by the wild type. These data suggest that Glu206 acts as the general acid/base catalyst in the hydrolysis reaction; mutant shows 10- and 60-fold reduced activities on aryl-galacto and aryl-glucosides, respectively, when compared with the wild type. Significant decrease in Km-value with 4-nitrophenyl beta-D-glucoside or 2-nitrophenyl betaD-glucoside. The residual activity of the mutant loses the typical pH dependence shown by the wild type. These data suggest that Glu206 acts as the general acid/base catalyst in the hydrolysis reaction
-
E387Q
-
mutant shows no detectable activity
-
E432C
-
kcat/KM for 4-methylumbelliferyl beta-D-glucoside is reduced 200fold, kcat/KM for 4-methylumbelliferyl beta-D-galactoside is reduced 130fold, kcat/KM for 4-methylumbelliferyl beta-D-xyloside is reduced 1.5fold, kcat/KM for 4-methylumbelliferyl beta-D-fucoside is reduced 2900fold, kcat/KM for 4-methylumbelliferyl beta-D-mannoside is ibcreased 1.5fold; the kcat/KM for 4-methylumbelliferyl beta-D-glucoside is reduced 200fold, and 4-methylumbelliferyl beta-D-galactoside is reduced 130fold. Although the activities with 4-methylumbelliferyl beta-D-mannoside and 4-methylumbelliferyl beta-D-xyloside are also reduced in the mutant, this is to a much smaller extent. The mutant enzyme shows remarkably broader specificity than wild-type enzyme
-
W433C
-
kcat/KM for 4-methylumbelliferyl beta-D-glucoside is reduced 140fold, kcat/KM for 4-methylumbelliferyl beta-D-galactoside is reduced 230fold, kcat/KM for 4-methylumbelliferyl beta-D-xyloside is reduced 14fold, kcat/KM for 4-methylumbelliferyl beta-D-fucoside is reduced 138fold, kcat/KM for 4-methylumbelliferyl beta-D-mannoside is reduced 16fold; the kcat/KM for 4-methylumbelliferyl beta-D-glucoside is reduced 140fold, and 4-methylumbelliferyl beta-D-galactoside is reduced 230fold. Although the activities with 4-methylumbelliferyl beta-D-mannoside and 4-methylumbelliferyl beta-D-xyloside are also reduced in the mutant, this is to a much smaller extent. The mutant enzyme shows remarkably broader specificity than wild-type enzyme
-
additional information
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
analysis
-
reporter genes in molecular biology
food industry
nutrition
-
catalyst of lactose hydrolysis in dairy products in the food industry
synthesis