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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

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

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.B26 Sulfolobus solfataricus beta-glycosidase

Inhibitors

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

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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
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-galactohydroximolactam
-
D-galactose
D-glucohydroximolactam
-
D-gluconic acid lactone
-
strong competitive inhibitor
D-glucose
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
-