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
-
transglycosylation
- synthesis
- beta-d-galactoside
- beta-glucosides
- amygdalin
-
glycone
-
3.2.1.21
-
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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Subunits
Subunits on EC 3.2.1.B26 - Sulfolobus solfataricus beta-glycosidase
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monomer
tetramer
tetramer
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contains 17 tryptophanyl residues for each subunit. Molecular dynamic simulation studies performed on the multitryptophan subunit of the beta-glycosidase. The molecular dynamic trajectories obtained from the simulation provide information about the distances and mobility of solvent molecules and specific amino acid residues able to quench the tryptophanyl fluorescence in each tryptophan environment. From these data, the fluorescence lifetime for each tryptophan residue of Sbgly can be estimated using a modified Stern-Volmer expr. The results are in agreement with the emission decay of the enzyme experimentally detected