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Information on EC 3.2.1.B26 - Sulfolobus solfataricus beta-glycosidase
for references in articles please use BRENDA:EC3.2.1.B26preliminary BRENDA-supplied EC number
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EC Tree
3.2.1.B26 Sulfolobus solfataricus beta-glycosidaseSpecify your search results
Word Map
- 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
The expected taxonomic range for this enzyme is: Saccharolobus solfataricus
Reaction Schemes
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, ssgh1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-D-glycosidase
beta-glycosidase
Bgl
bgly
GH1 beta-glycosidase
LACS
Sbeta-gly
Sbetagly
Ssbeta-Glc1
SsbetaG
SsbetaGly
SSO3019
Sbetagly
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
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.
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-
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-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl beta-D-glucopyranoside + H2O
2,4-dinitrophenol + beta-D-glucopyranose
-
-
-
-
?
2,4-dinitrophenyl beta-D-glucopyranoside + H2O
2,4-dinitrophenol + D-glucopyranose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranose
-
-
-
-
?
2-nitrophenyl beta-D-galactose + H2O
2-nitrophenol + beta-D-galactose
-
-
-
-
?
2-nitrophenyl beta-D-galactoside + H2O
2-nitrophenol + beta-D-galactose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylopyranose
-
-
-
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
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
-
i.e. ginsenoside Rb1
-
-
?
4-methylumbelliferyl beta-D-fucopyranoside + H2O
4-methylumbelliferone + beta-D-fucopyranose
-
-
-
-
?
4-methylumbelliferyl beta-D-fucoside + H2O
4-methylumbelliferol + D-fucose
-
-
-
?
4-methylumbelliferyl beta-D-fucoside + H2O
4-methylumbelliferone + beta-D-fucose
-
-
-
?
4-methylumbelliferyl beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
-
-
-
-
?
4-methylumbelliferyl beta-D-galacturonate + H2O
4-methylumbelliferone + beta-D-galacturonate
-
-
-
?
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucopyranose
-
-
-
-
?
4-methylumbelliferyl beta-D-glucuronic acid + H2O
4-methylumbelliferone + beta-D-glucuronic acid
-
-
-
-
?
4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferol + D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-mannopyranoside + H2O
4-methylumbelliferone + beta-D-mannopyranose
-
-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferol + D-mannose
-
-
-
?
4-methylumbelliferyl beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
-
-
-
-
?
4-methylumbelliferyl beta-D-xyloside + H2O
4-methylumbelliferol + D-xylose
-
-
-
?
4-methylumbelliferyl beta-D-xyloside + H2O
4-methylumbelliferone + beta-D-xylose
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl beta-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + D-fucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenyl + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-mannoside + H2O
4-nitrophenol + D-mannose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
-
?
ginsenoside C-O + H2O
ginsenoside C-K + D-glucose + L-arabinopyranose
-
-
-
?
ginsenoside C-Y + H2O
ginsenoside C-K + L-arabinopyranose
-
-
-
?
ginsenoside F2 + H2O
ginsenoside C-K + D-glucose
highest activity
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + D-glucose
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + D-glucose + L-arabinopyranose
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside Rd + L-arabinopyranose
-
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 C-K + D-glucose + L-arabinofuranose
-
-
-
?
ginsenoside Rc + H2O
ginsenoside Mc + L-arabinofuranose
-
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 C-K + D-glucose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside K + D-glucose
-
i.e. 3beta-[beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyloxy]-20-(beta-D-glucopyranosyloxy)dammar-24-en-12beta-ol
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
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
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
2-nitrophenyl beta-D-galactoside
2-nitrophenol + D-galactose
-
-
-
r
2-nitrophenyl beta-D-galactoside
2-nitrophenol + D-galactose
-
-
-
r
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
-
?
2-nitrophenyl beta-galactoside + H2O
2-nitrophenol + D-galactose
-
-
-
?
2-nitrophenyl beta-galactoside + H2O
2-nitrophenol + D-galactose
-
-
-
?
4-methylumbelliferyl beta-D-galactoside + H2O
4-methylumbelliferone + beta-D-galactose
-
-
-
?
4-methylumbelliferyl beta-D-galactoside + H2O
4-methylumbelliferone + beta-D-galactose
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferone + beta-D-mannose
-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferone + beta-D-mannose
-
-
-
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
14% of the activity compared to 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-fucopyranose
-
14% of the activity compared to 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
-
73% of the activity compared to 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucopyranose
-
73% of the activity compared to 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside
4-nitrophenol + beta-D-galactose
LacS shows 70% hydrolytic activity on nitrophenyl-beta-glucoside relative to the activity on nitrophenyl-beta-galactoside
-
-
?
4-nitrophenyl beta-D-galactoside
4-nitrophenol + beta-D-galactose
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
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
the enzyme shows constant donor selectivity (Vmax ratio of the 4-nitrophenyl-beta-D-glucoside and 4-nitrophenyl-beta-D-galactoside) as the temperature increased
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
52% of the activity compared to 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
52% of the activity compared to 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside
4-nitrophenol + beta-D-glucose
LacS shows 70% hydrolytic activity on nitrophenyl-beta-glucoside relative to the activity on nitrophenyl-beta-galactoside
-
-
?
4-nitrophenyl beta-D-glucoside
4-nitrophenol + beta-D-glucose
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 + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
the enzyme shows constant donor selectivity (Vmax ratio of the 4-nitrophenyl-beta-D-glucoside and 4-nitrophenyl-beta-D-galactoside) as the temperature increases
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
highest activity
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
highest activity
-
-
?
ginsenoside C-Mc1 + H2O
ginsenoside C-K + D-glucose + L-arabinofuranose
-
-
-
?
ginsenoside C-Mc1 + H2O
ginsenoside C-K + D-glucose + L-arabinofuranose
-
-
-
?
methyl beta-D-galactoside
methanol + D-galactose
-
-
-
r
rebaudioside A + H2O
steviol + D-glucose
negligible activity
-
-
?
rebaudioside A + H2O
steviol + D-glucose
negligible activity
-
-
?
rubusoside + H2O
steviol + D-glucose
44.2% yield
-
-
?
additional information
?
-
-
hydrolase with broad specificity and noticeable glucan 1 -> 4-beta-D-glucosidase activity
-
-
?
additional information
?
-
-
kinetic studies of the reactions of galactosylated enzyme intermediates with a range of nucleophiles
-
-
?
additional information
?
-
-
broad specificity and remarkable glucan-1,4-beta-D-glucosidase (exocellobiase) activity
-
-
?
additional information
?
-
-
the enzyme hydrolyzes a variety of low-molecular-weight, beta-linked glycosides. Chromogenic beta-D-galactosides and beta-D-glucosides are hydrolyzed at a common active site. beta-Glucosides and beta-fucosides represent the preferred substrates
-
-
?
additional information
?
-
-
wide substrate specificity. Active on aryl-beta-galactose, -fucose, -glucose and -xylose and on di- and oligosaccharides. Among glucose dimers are hydrolysed in the order of decreasing activity: beta-(1,3), beta-(1,4), beta-(1,6). Ssbeta-Gly is an exo-acting enzyme with a preference for cellotetraose
-
-
?
additional information
?
-
-
catalyzes transglycosylation reaction with with lactose as donor and N-acetyllactosamine as acceptor to synthesize beta-galactooligosaccharides at different temperatures. The main products are beta-D-Gal-1,6-D-GlcNAc, beta-D-Gal-1,4-D-GlcNAc and several oligosaccharides
-
-
?
additional information
?
-
-
collection of information on the global and local dynamics in view of a full understanding of topology and motion hierarchy in proteins by dynamic fluorescence and site-specific labeling EPR
-
-
?
additional information
?
-
-
during lactose conversion at 70°C galactosyl transfer to acceptors other than water competes efficiently with complete hydrolysis of substrate. This process leads to transient formation of a range of new products, mainly disaccharides and trisaccharides, and shows a marked dependence on initial substrate concentration and lactose conversion. The molar ratio of trisaccharides to disaccharides is maximal at an early stage of reaction and decreases directly proportional to increasing substrate conversion. The major transgalactosylation products of SsbetaGl are beta-D-Galp-(1->3)-Glc and beta-D-Galp-(1->6)-Glc, and beta-D-Galp-(1->3)-lactose and beta-D-Galp-(1-->6)-lactose. The enzyme accumulates beta(1-->6)-linked glycosides, particularly allolactose, at a late stage of reaction
-
-
?
additional information
?
-
-
mutant enzyme E387G catalyzes transglycosylation reactions. In the transglycosylation reactions, 2-nitrophenyl beta-D-glucopyranoside is used as the donor and different aryl and alkyl mono- and disaccharide substrates containing alpha- and beta-glycosidic linkages are used as acceptors. The formation of the beta-1,3 linkage is observed with acceptors containing the 2-nitrophenyl group, while beta-1,6-disaccharides are predominant with 4-nitrophenyl beta-D-glucoside. When a beta linkage of the acceptor is between two sugars, as for the formation of trisaccharides, the beta-1,3 acceptors possess affinity for the donor active site and are also partially hydrolyzed. The beta-1,4-based acceptor furnish only linear trisaccharides, albeit in very poor yield. The presence of alpha linkages in the acceptors induces beta-1,6 glycosylation despite the nature ofthe aglycons. In these cases, the yield is higher with the increasing lipophilic nature of the aglycon; however, the yield depends on the dimensions and nature of this group. In fact, while maltose as free disaccharide givse very poor yields of trisaccharide products, 33% yield is reached with 4-nitrophenyl alpha-D-glucopyranoside
-
-
?
additional information
?
-
the enzyme catalyzes the conversion of lactose to hexyl-beta-D-galactoside in hexanol (transgalactosylation reaction)
-
-
?
additional information
?
-
-
the enzyme catalyzes the enzymatic synthesis of 2-beta-D-galactopyranosyloxyethyl methacrylate starting from 2-hydroxyethyl methacrylate and 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
additional information
?
-
the enzyme has broad specificity, accommodating both gluco- and galacto-configured substrates
-
-
?
additional information
?
-
-
the enzyme has broad specificity, accommodating both gluco- and galacto-configured substrates
-
-
?
additional information
?
-
-
the enzyme performs the transfer glucose, galactose and fucose from different donors
-
-
?
additional information
?
-
-
the transfer of the galactosyl group from lactose to acceptors such as lactose or D-glucose rather than water is significant for both enzymes and depends on the initial lactose concentration as well as the time-dependent substrate/product ratio during batchwise lactose conversion
-
-
?
additional information
?
-
-
the enzyme shows broad specificity for beta-D-gluco-, fuco- and galactosides. It hydrolyses a large number of beta-linked glycoside dimers and oligomers; chromogenic beta-glucosides and beta-fucosides are the preferred substrates, and kinetic analysis indicates that they bind to a common catalytic site. The order of catalytic efficiency is beta 1-3 > beta 1-4 > beta 1-6 and cellotetraose > cellotriose > cellobiose for glucose dimers and oliogomers respectively. The cleavage occurres at the non-reducing end of the oligosaccharide, and the enzyme shows noticeable specificity also for the aglycone part of substrates. The enzyme from Sulfolobus solfataricus strain MT-4 is defined as a true glycosyl hydrolase with remarkable exo-glucosidase activity
-
-
?
additional information
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enzyme additionally catalyzes transglycosylation reactions, making new beta(1->3) and beta(1->6) glycosidic bonds by intermolecular as well as intramolecular transfer reactions. The intramolecular galactosyl transfer of CelB yields beta-D-Galp-(1->6)-D-glucose and beta-D-Galp-(1->3)-D-glucose in a molar ratio of about 1 : 2. Galactosyl transfer from CelB to D-glucose occurs with partitioning ratios, kNu /kwater, which are 170 times those for the reactions of the galactosylated enzyme with 2-propanol. Therefore, the binding interactions with nucleophiles contribute chiefly to formation of new beta-glycosides during lactose conversion. Likewise, noncovalent interactions with the glucose leaving group govern the catalytic efficiencies for the hydrolysis of lactose
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additional information
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enzyme additionally catalyzes transglycosylation reactions, making new beta(1->3) and beta(1->6) glycosidic bonds by intermolecular as well as intramolecular transfer reactions. The intramolecular galactosyl transfer of CelB yields beta-D-Galp-(1->6)-D-glucose and beta-D-Galp-(1->3)-D-glucose in a molar ratio of about 1 : 2. Galactosyl transfer from CelB to D-glucose occurs with partitioning ratios, kNu /kwater, which are 170 times those for the reactions of the galactosylated enzyme with 2-propanol. Therefore, the binding interactions with nucleophiles contribute chiefly to formation of new beta-glycosides during lactose conversion. Likewise, noncovalent interactions with the glucose leaving group govern the catalytic efficiencies for the hydrolysis of lactose
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additional information
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no activity with alpha-L-arabinofuranoside linked to ginsenoside Rc
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additional information
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the specific hydrolytic activity for the wild type enzyme follows the order ginsenoside F2 > Rb1 > C-O > C-Y > Rb2 > Rd > C-Mc> C-Mc1
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additional information
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no activity with alpha-L-arabinofuranoside linked to ginsenoside Rc
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additional information
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the specific hydrolytic activity for the wild type enzyme follows the order ginsenoside F2 > Rb1 > C-O > C-Y > Rb2 > Rd > C-Mc> C-Mc1
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additional information
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enzyme additionally catalyzes transglycosylation reactions, making new beta(1->3) and beta(1->6) glycosidic bonds by intermolecular as well as intramolecular transfer reactions. The intramolecular galactosyl transfer of CelB yields beta-D-Galp-(1->6)-D-glucose and beta-D-Galp-(1->3)-D-glucose in a molar ratio of about 1 : 2. Galactosyl transfer from CelB to D-glucose occurs with partitioning ratios, kNu /kwater, which are 170 times those for the reactions of the galactosylated enzyme with 2-propanol. Therefore, the binding interactions with nucleophiles contribute chiefly to formation of new beta-glycosides during lactose conversion. Likewise, noncovalent interactions with the glucose leaving group govern the catalytic efficiencies for the hydrolysis of lactose
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the enzyme performs the transfer glucose, galactose and fucose from different donors
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Saccharolobus solfataricus MT-4 / DSM 5833
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the enzyme shows broad specificity for beta-D-gluco-, fuco- and galactosides. It hydrolyses a large number of beta-linked glycoside dimers and oligomers; chromogenic beta-glucosides and beta-fucosides are the preferred substrates, and kinetic analysis indicates that they bind to a common catalytic site. The order of catalytic efficiency is beta 1-3 > beta 1-4 > beta 1-6 and cellotetraose > cellotriose > cellobiose for glucose dimers and oliogomers respectively. The cleavage occurres at the non-reducing end of the oligosaccharide, and the enzyme shows noticeable specificity also for the aglycone part of substrates. The enzyme from Sulfolobus solfataricus strain MT-4 is defined as a true glycosyl hydrolase with remarkable exo-glucosidase activity
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the enzyme hydrolyzes a variety of low-molecular-weight, beta-linked glycosides. Chromogenic beta-D-galactosides and beta-D-glucosides are hydrolyzed at a common active site. beta-Glucosides and beta-fucosides represent the preferred substrates
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the enzyme catalyzes the conversion of lactose to hexyl-beta-D-galactoside in hexanol (transgalactosylation reaction)
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additional information
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the enzyme has broad specificity, accommodating both gluco- and galacto-configured substrates
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