3.2.1.B26: Sulfolobus solfataricus beta-glycosidase
This is an abbreviated version!
For detailed information about Sulfolobus solfataricus beta-glycosidase, go to the full flat file.
Word Map on EC 3.2.1.B26
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3.2.1.B26
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transglycosylation
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synthesis
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beta-d-galactoside
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beta-glucosides
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amygdalin
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glycone
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3.2.1.21
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transgalactosylation
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prunasin
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beta-d-fucoside
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food industry
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analysis
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nutrition
- 3.2.1.B26
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transglycosylation
- synthesis
- beta-d-galactoside
- beta-glucosides
- amygdalin
-
glycone
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3.2.1.21
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transgalactosylation
- prunasin
- beta-d-fucoside
- food industry
- analysis
- nutrition
Reaction
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-D-glycosidase, beta-glucosidase, beta-Gly, beta-glycosidase, Bgl, bgly, EcSbgly, GH1 beta-glycosidase, LACS, Sbeta-gly, Sbetagly, Ss-beta-Gly, Ssbeta-Glc1, Ssbeta-Gly, SsbetaG, SsbetaGlc1, SsbetaGly, SsGH1, sso1353, SSO3019
ECTree
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Inhibitors
Inhibitors on EC 3.2.1.B26 - Sulfolobus solfataricus beta-glycosidase
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(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
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
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+
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
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
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
tetrahydrofuran
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5% (v/v), decreases activity with 4-nitrophenyl beta-D-galactopyranoside or 4-nitrophenyl beta-D-fucopyranoside
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0.1 M, 21% inhibition of beta-galactoside hydrolysis, slight activation of beta-glucoside hydrolysis
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0.1 M, 37% inhibition of beta-galactoside hydrolysis, slight activation of beta-glucoside hydrolysis
D-glucose
inhibits activity with 4-nitrophenyl beta-D-galactopyranoside
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soluble and immobilized enzyme show no inhibition by glucose
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additional information
the activities of the wild-type enzyme in 30% acetonitrile, butanone and acetone are higher than those in dimethyl sulfoxide, dimethylformamide and 1,4-dioxane. The low boiling point of acetone limits the application of this solvent in thermophilic enzyme reactions
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additional information
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the activities of the wild-type enzyme in 30% acetonitrile, butanone and acetone are higher than those in dimethyl sulfoxide, dimethylformamide and 1,4-dioxane. The low boiling point of acetone limits the application of this solvent in thermophilic enzyme reactions
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additional information
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cations can cause a strong attenuation of the ion pair interactions E474K72 and D473R402, with consequent partial dissociation of the tetrameric structure
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