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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
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
no activity with alpha-L-arabinofuranoside linked to ginsenoside Rc
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
no activity with alpha-L-arabinofuranoside linked to ginsenoside Rc
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
the enzyme performs the transfer glucose, galactose and fucose from different donors
-
-
?
additional information
?
-
Saccharolobus solfataricus MT-4 / DSM 5833
-
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
?
-
-
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
?
-
the enzyme catalyzes the conversion of lactose to hexyl-beta-D-galactoside in hexanol (transgalactosylation reaction)
-
-
?
additional information
?
-
the enzyme has broad specificity, accommodating both gluco- and galacto-configured substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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+
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
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
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
tetrahydrofuran
-
5% (v/v), decreases activity with 4-nitrophenyl beta-D-galactopyranoside or 4-nitrophenyl beta-D-fucopyranoside
D-galactose
-
0.1 M, 21% inhibition of beta-galactoside hydrolysis, slight activation of beta-glucoside hydrolysis
D-glucose
-
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
additional information
-
soluble and immobilized enzyme show no inhibition by glucose
-
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
-
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
-
additional information
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
acetonitrile
-
maximal increase in enzyme activity at solvent concentrations of 15% (v/v) with 4-nitrophenyl beta-D-fucopyranoside as substrate
butan-2-one
-
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
-
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
-
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
-
the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme
methanol
-
the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme
Propanol
-
the liberation of aglycone from aryl beta-D-glucosides is stimulated by alcohols in a manner suggesting specific interaction between alcohol and enzyme
tetrahydrofuran
-
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
-
methyl acetate
-
5% (v/v), increases activity with 2-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside or 4-nitrophenyl beta-D-glucopyranoside
methyl acetate
-
highest activation at solvent concentrations of 5% (v/v) with 4-nitrophenyl beta-D-fucopyranoside as substrate
SDS
-
detergent activation, maximal activity in presence of 0.02% SDS. The SDS activation is marked at low temperature; specifically, at 10°C the SDS causes an activation of 140% with respect to the activity observed at the same temperature and in the absence of detergent. At 70°C the increase of enzyme activity is less than 10%. The enzyme activity is not affected by SDS concentration as high as 5% at each temperature
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Diabetic Angiopathies
Beta-glycosidases and diabetic microangiopathy. I. Decreases of beta-glycosidase activities in diabetic rat kidney.
Keratitis, Herpetic
[Use of tear enzyme assay to predict recurrent herpetic keratitis in children]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 65°C, wild-type enzyme
1.3
4-methylumbelliferyl beta-D-glucuronide
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
24.2
4-nitrophenyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
192
methyl beta-D-galactoside
release of methanol, pH 7.5, 80°C
0.95
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
0.95
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme R488A
0.99
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
1.47
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme R489A
1.5
2-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
1.53
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme E206Q
1.9
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme His489
1.97
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme delVal484-His489
1.99
2-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, native enzyme
3.9
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, recombinant enzyme
3.9
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, soluble enzyme
4
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, wild-type enzyme
4.1
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, soluble enzyme
5
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, enzyme immobilized on chitosan activated with glutaraldehyde
5.3
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, immobilized enzyme
1.1
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
0.5
2-nitrophenyl beta-D-glucopyranoside
-
wild-type, pH 6.5, 65°C, presence of 2 M formate
1.01
2-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 65°C, wild-type enzyme
1.01
2-nitrophenyl beta-D-glucopyranoside
-
wild-type, pH 6.5, 65°C
1.1
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 6.0, 65°C
1.17
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 6.5, 65°C, presence of 2 M formate
2.2
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 5.0, 65°C
4.9
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 4.0, 65°C
16.4
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 3.0, 65°C
0.03
2-Nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
1.01
2-Nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, wild-type enzyme
0.011
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, wild-type enzyme
0.023
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
0.34
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
0.41
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
0.011
4-methylumbelliferyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.011
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 80°C, wild-type enzyme
0.21
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 45°C, wild-type enzyme
0.34
4-methylumbelliferyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
0.34
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 80°C, mutant enzyme E432C
0.41
4-methylumbelliferyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
0.41
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 80°C, mutant enzyme W433C
18.6
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 45°C, mutant enzyme W433C
0.066
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, wild-type enzyme
0.083
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
0.47
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
2.2
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
0.066
4-methylumbelliferyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.066
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 80°C, wild-type enzyme
0.47
4-methylumbelliferyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
0.47
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 80°C, mutant enzyme E432C
0.57
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 45°C, wild-type enzyme
0.81
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 45°C, mutant enzyme E432C
2.2
4-methylumbelliferyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
2.2
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 80°C, mutant enzyme W433C
5.28
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 45°C, mutant enzyme W433C
1.3
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 80°C, wild-type enzyme
2.72
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 45°C, mutant enzyme W433C
3.46
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 45°C, mutant enzyme E432C
0.046
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, wild-type enzyme
0.068
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
0.34
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
1.61
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
0.046
4-methylumbelliferyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.046
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 80°C, wild-type enzyme
0.15
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 45°C, wild-type enzyme
0.34
4-methylumbelliferyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
0.34
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 80°C, mutant enzyme E432C
0.51
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 45°C, mutant enzyme E432C
1.61
4-methylumbelliferyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
1.61
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 80°C, mutant enzyme W433C
22.1
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 45°C, mutant enzyme W433C
1.3
4-methylumbelliferyl beta-D-glucuronic acid
-
pH 6.5, 80°C, wild-type enzyme
1.4
4-methylumbelliferyl beta-D-glucuronic acid
-
pH 6.5, 80°C, mutant enzyme M439C
0.036
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, wild-type enzyme
0.042
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
0.18
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
0.9
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
0.036
4-methylumbelliferyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.036
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, wild-type enzyme
0.18
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, mutant enzyme W433C
0.9
4-methylumbelliferyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
0.9
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, mutant enzyme E432C
24.2
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 45°C, wild-type enzyme
0.068
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
0.13
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, wild-type enzyme
0.59
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
1.26
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
0.13
4-methylumbelliferyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.13
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 80°C, wild-type enzyme
0.59
4-methylumbelliferyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
0.59
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 80°C, mutant enzyme W433C
1.26
4-methylumbelliferyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
1.26
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 80°C, mutant enzyme E432C
5.1
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 45°C, wild-type enzyme
13.7
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 45°C, mutant enzyme E432C
0.4
4-nitrophenyl beta-D-fucopyranoside
-
pH and temperature not specified in the publication, native enzyme
0.45
4-nitrophenyl beta-D-fucopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
0.09
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
0.21
4-nitrophenyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
0.45
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 65°C, wild-type enzyme
0.7
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 75°C, recombinant enzyme
18.6
4-nitrophenyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
1.17
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
2.33
4-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, native enzyme
2.51
4-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
4.3
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, recombinant enzyme
4.7
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, wild-type enzyme
4.79
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme E206Q
0.57
4-nitrophenyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
0.81
4-nitrophenyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
5.28
4-nitrophenyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
0.45
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication, native enzyme
0.6
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
0.03
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
0.15
4-nitrophenyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
0.3
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, wild-type enzyme
0.5
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 75°C, recombinant enzyme
0.5
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 75°C, wild-type enzyme
0.51
4-nitrophenyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
22.1
4-nitrophenyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
5.1
4-nitrophenyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
13.7
4-nitrophenyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
0.55
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.0, 60°C, 1000 bar
0.86
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.0, 60°C, 1500 bar
20
cellobiose
-
pH 7.0, 75°C, enzyme immobilized on chitosan activated with glutaraldehyde
21.54
cellobiose
-
pH and temperature not specified in the publication, recombinant enzyme
21.6
cellobiose
-
pH and temperature not specified in the publication, immobilized enzyme
22.4
cellobiose
-
pH and temperature not specified in the publication, native enzyme
32.7
cellobiose
-
pH and temperature not specified in the publication, soluble enzyme
1.93
ginsenoside Rb1
mutant enzyme W361F, at pH 5.5 and 95°C
1.59
ginsenoside Rd
mutant enzyme W361F, at pH 5.5 and 95°C
131
lactose
-
pH 5.5, 70°C, enzyme immobilized on controlled pore glass
1.29
laminaribiose
-
pH and temperature not specified in the publication, native enzyme
1.4
laminaribiose
-
pH and temperature not specified in the publication, recombinant enzyme
additional information
additional information
-
kinetic studies of the reactions of galactosylated enzyme intermediates with a range of nucleophiles
-
additional information
additional information
-
KM increases with temperature: the increase is moderate at lower temperatures (from 30°C to 65°C) and more evident between 65°C and 85°C. Reactions with 4-nitrophenyl-beta-D-glucoside and 2-nitrophenyl-beta-D-glucoside show a biphasic behavior in LineweaverBurk plots, suggesting that transglycosylation reactions occur at higher substrate concentrations. Kinetic constants obtained at lower or higher substrate concentrations are calculated
-
additional information
additional information
-
kinetic constant values for soluble enzyme and for enzyme immobilized on chitosan activated with glutaraldehyde are comparable
-
additional information
additional information
-
kinetic constants for transglycosylation reactions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
275
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 65°C, wild-type enzyme
0.81
4-methylumbelliferyl beta-D-glucuronide
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
2.65
4-nitrophenyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
6.6
methyl beta-D-galactoside
release of methanol, pH 7.5, 80°C
34
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme E206Q
295
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
366
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme delVal484-His489
416
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme His489
427
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme R488A
498
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
611
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme R489A
1239
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, wild-type enzyme
1252
2-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
1416
2-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, native enzyme
1662
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, immobilized enzyme
1686
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, enzyme immobilized on chitosan activated with glutaraldehyde
1689
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, soluble enzyme
1713
2-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, recombinant enzyme
1713
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, soluble enzyme
1300
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
20.7
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 6.0, 65°C
52.9
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 5.0, 65°C
72.9
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 6.5, 65°C, presence of 2 M formate
309
2-nitrophenyl beta-D-glucopyranoside
-
wild-type, pH 6.5, 65°C
321.9
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 4.0, 65°C
439.8
2-nitrophenyl beta-D-glucopyranoside
-
wild-type, pH 6.5, 65°C, presence of 2 M formate
538
2-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 65°C, wild-type enzyme
901.4
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 3.0, 65°C
4.5
2-Nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
252
2-Nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, wild-type enzyme
18
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
31
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
80
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, wild-type enzyme
91
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
5.16
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 45°C, wild-type enzyme
9.43
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 45°C, mutant enzyme W433C
18
4-methylumbelliferyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
18
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 80°C, mutant enzyme E432C
31
4-methylumbelliferyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
31
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 80°C, mutant enzyme W433C
80
4-methylumbelliferyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
89
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 80°C, wild-type enzyme
5.4
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
14
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
94
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
98
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, wild-type enzyme
0.047
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 45°C, mutant enzyme E432C
0.08
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 45°C, mutant enzyme W433C
5.4
4-methylumbelliferyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
5.4
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 80°C, mutant enzyme E432C
7.2
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 45°C, wild-type enzyme
14.6
4-methylumbelliferyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
14.6
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 80°C, mutant enzyme W433C
98
4-methylumbelliferyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
98
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 80°C, wild-type enzyme
0.004
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 45°C, mutant enzyme E432C
0.004
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 45°C, mutant enzyme W433C
0.81
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 80°C, wild-type enzyme
5.1
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
33
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
140
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, wild-type enzyme
190
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
0.018
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 45°C, mutant enzyme E432C
2.72
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 45°C, mutant enzyme W433C
4.35
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 45°C, wild-type enzyme
5.1
4-methylumbelliferyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
5.1
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 80°C, mutant enzyme E432C
33
4-methylumbelliferyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
33
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 80°C, mutant enzyme W433C
140
4-methylumbelliferyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
140
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 80°C, wild-type enzyme
0.81
4-methylumbelliferyl beta-D-glucuronic acid
-
pH 6.5, 80°C, wild-type enzyme
1.3
4-methylumbelliferyl beta-D-glucuronic acid
-
pH 6.5, 80°C, mutant enzyme M439C
0.92
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
1.8
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, wild-type enzyme
2.3
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
2.8
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
0.92
4-methylumbelliferyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
0.92
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, mutant enzyme W433C
1.8
4-methylumbelliferyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
1.8
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, wild-type enzyme
2.65
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 45°C, wild-type enzyme
2.8
4-methylumbelliferyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
2.8
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, mutant enzyme E432C
1.5
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
2.8
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
3.8
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, wild-type enzyme
9.3
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
0.028
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 45°C, mutant enzyme E432C
1.5
4-methylumbelliferyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
1.5
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 80°C, mutant enzyme W433C
2.8
4-methylumbelliferyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
2.8
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 80°C, mutant enzyme E432C
3.8
4-methylumbelliferyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
3.8
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 80°C, wild-type enzyme
3.95
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 45°C, wild-type enzyme
427
4-nitrophenyl beta-D-fucopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
460
4-nitrophenyl beta-D-fucopyranoside
-
pH and temperature not specified in the publication, native enzyme
5.16
4-nitrophenyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
9.43
4-nitrophenyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
35
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
263
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 65°C, wild-type enzyme
503
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 75°C, recombinant enzyme
772
4-nitrophenyl beta-D-fucoside
-
pH 6.5, 75°C, wild-type enzyme
31
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, mutant enzyme E206Q
275
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 65°C, wild-type enzyme
930
4-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
1020
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, wild-type enzyme
1285
4-nitrophenyl beta-D-galactopyranoside
-
pH 6.5, 75°C, recombinant enzyme
1341
4-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, native enzyme
0.047
4-nitrophenyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
0.08
4-nitrophenyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
7.2
4-nitrophenyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
634
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
726
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication, native enzyme
0.018
4-nitrophenyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
2.72
4-nitrophenyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
4.35
4-nitrophenyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
4.4
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, mutant enzyme E206Q
240
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 65°C, wild-type enzyme
542
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 75°C, recombinant enzyme
542
4-nitrophenyl beta-D-glucoside
-
pH 6.5, 75°C, wild-type enzyme
0.028
4-nitrophenyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
3.95
4-nitrophenyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
547
cellobiose
-
pH and temperature not specified in the publication, recombinant enzyme
628
cellobiose
-
pH and temperature not specified in the publication, soluble enzyme
654
cellobiose
-
pH and temperature not specified in the publication, native enzyme
727
cellobiose
-
pH and temperature not specified in the publication, immobilized enzyme
746
cellobiose
-
pH 7.0, 75°C, enzyme immobilized on chitosan activated with glutaraldehyde
1343
ginsenoside Rb1
mutant enzyme W361F, at pH 5.5 and 95°C
1049
ginsenoside Rd
mutant enzyme W361F, at pH 5.5 and 95°C
524
laminaribiose
-
pH and temperature not specified in the publication, native enzyme
573
laminaribiose
-
pH and temperature not specified in the publication, recombinant enzyme
additional information
additional information
-
kcat increases exponentially with temperature. Reactions with 4-nitrophenyl-beta-D-glucoside and 2-nitrophenyl-beta-D-glucoside show a biphasic behavior in LineweaverBurk plots, suggesting that transglycosylation reactions occur at higher substrate concentrations. Kinetic constants obtained at lower or higher substrate concentrations are calculated
-
additional information
additional information
-
kinetic constants for transglycosylation reactions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1617
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 65°C, wild-type enzyme
0.034
methyl beta-D-galactoside
release of methanol, pH 7.5, 80°C
313.6
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, immobilized enzyme
337
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, soluble enzyme, enzyme immobilized on chitosan activated with glutaraldehyde
412
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, soluble enzyme
439
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.0, 75°C, soluble enzyme
712
2-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, native enzyme
844
2-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
1200
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
18.5
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 6.0, 65°C
23.8
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 5.0, 65°C
45
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 6.5, 65°C, presence of 2 M formate
55
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 3.0, 65°C
65.9
2-nitrophenyl beta-D-glucopyranoside
-
mutant E387G, pH 4.0, 65°C
533
2-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 65°C, wild-type enzyme
533
2-nitrophenyl beta-D-glucopyranoside
-
wild-type, pH 6.5, 65°C
850
2-nitrophenyl beta-D-glucopyranoside
-
wild-type, pH 6.5, 65°C, presence of 2 M formate
53
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
76
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
4000
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
7300
4-methylumbelliferyl beta-D-fucopyranoside
-
pH 6.5, 80°C, wild-type enzyme
0.053
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 80°C, mutant enzyme E432C
0.068
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 45°C, mutant enzyme E432C
0.076
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 80°C, mutant enzyme W433C
0.506
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 45°C, mutant enzyme W433C
2.5
4-methylumbelliferyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
7.3
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 80°C, wild-type enzyme
42.6
4-methylumbelliferyl beta-D-fucoside
pH 6.5, 45°C, wild-type enzyme
53
4-methylumbelliferyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
7300
4-methylumbelliferyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
6.3
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
11
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
1130
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
1490
4-methylumbelliferyl beta-D-galactopyranoside
-
pH 6.5, 80°C, wild-type enzyme
0.0063
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 80°C, mutant enzyme W433C
0.011
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 80°C, mutant enzyme E432C
0.015
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 45°C, mutant enzyme W433C
0.058
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 45°C, mutant enzyme E432C
0.6
4-methylumbelliferyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
1.49
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 80°C, wild-type enzyme
11
4-methylumbelliferyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
12.7
4-methylumbelliferyl beta-D-galactoside
pH 6.5, 45°C, wild-type enzyme
1490
4-methylumbelliferyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.0006
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 80°C, wild-type enzyme
0.001
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 45°C, mutant enzyme E432C
0.0013
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 45°C, mutant enzyme W433C
0.06
4-methylumbelliferyl beta-D-galacturonate
pH 6.5, 45°C, wild-type enzyme
15
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
20
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
2900
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
2900
4-methylumbelliferyl beta-D-glucopyranoside
-
pH 6.5, 80°C, wild-type enzyme
0.015
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 80°C, mutant enzyme E432C
0.02
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 80°C, mutant enzyme W433C
0.036
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 45°C, mutant enzyme E432C
0.123
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 45°C, mutant enzyme W433C
2.9
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 80°C, wild-type enzyme
6.3
4-methylumbelliferyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
15
4-methylumbelliferyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
29.8
4-methylumbelliferyl beta-D-glucoside
pH 6.5, 45°C, wild-type enzyme
2900
4-methylumbelliferyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
0.6
4-methylumbelliferyl beta-D-glucuronic acid
-
pH 6.5, 80°C, wild-type enzyme
0.92
4-methylumbelliferyl beta-D-glucuronic acid
-
pH 6.5, 80°C, mutant enzyme M439C
0.6
4-methylumbelliferyl beta-D-glucuronide
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
5.1
4-methylumbelliferyl beta-D-glucuronide
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
3.2
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
5.1
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
50
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, wild-type enzyme
53
4-methylumbelliferyl beta-D-mannopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
0.001
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 45°C, mutant enzyme E432C
0.0032
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, mutant enzyme E432C
0.005
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 45°C, mutant enzyme W433C
0.0051
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, mutant enzyme W433C
0.05
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, wild-type enzyme
0.11
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 45°C, wild-type enzyme
3.2
4-methylumbelliferyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
50
4-methylumbelliferyl beta-D-mannoside
pH 6.5, 80°C, wild-type enzyme
76
4-methylumbelliferyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
2.2
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, mutant enzyme E432C
2.5
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, mutant enzyme W433C
30
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, wild-type enzyme
136
4-methylumbelliferyl beta-D-xylopyranoside
-
pH 6.5, 80°C, mutant enzyme M439C
0.002
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 45°C, mutant enzyme E432C
0.0022
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 80°C, mutant enzyme E432C
0.0025
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 80°C, mutant enzyme W433C
0.003
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 45°C, mutant enzyme W433C
0.03
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 80°C, wild-type enzyme
0.77
4-methylumbelliferyl beta-D-xyloside
pH 6.5, 45°C, wild-type enzyme
2.2
4-methylumbelliferyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme E432C
20
4-methylumbelliferyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 80°C, mutant enzyme W433C
30
4-methylumbelliferyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 80°C, wild-type enzyme
941
4-nitrophenyl beta-D-fucopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
1151
4-nitrophenyl beta-D-fucopyranoside
-
pH and temperature not specified in the publication, native enzyme
0.068
4-nitrophenyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
0.506
4-nitrophenyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
42.6
4-nitrophenyl beta-D-fucoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
370
4-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
576
4-nitrophenyl beta-D-galactopyranoside
-
pH and temperature not specified in the publication, native enzyme
0.015
4-nitrophenyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
0.058
4-nitrophenyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
12.7
4-nitrophenyl beta-D-galactoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
1058
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication, recombinant enzyme
1633
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication, native enzyme
0.036
4-nitrophenyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
0.123
4-nitrophenyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
29.8
4-nitrophenyl beta-D-glucoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
0.001
4-nitrophenyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
0.005
4-nitrophenyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
0.11
4-nitrophenyl beta-D-mannoside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
0.002
4-nitrophenyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme E432C
0.003
4-nitrophenyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 45°C, mutant enzyme W433C
0.77
4-nitrophenyl beta-D-xyloside
pH 6.5 (50 mM phosphate), 45°C, wild-type enzyme
1764
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.0, 60°C, 1500 bar
3356
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.0, 60°C, 1000 bar
11130
4-nitrophenyl-beta-D-glucopyranoside
-
pH 6.0, 60°C, 500 bar
19.2
cellobiose
-
pH and temperature not specified in the publication, soluble enzyme
25
cellobiose
-
pH and temperature not specified in the publication, recombinant enzyme
29
cellobiose
-
pH and temperature not specified in the publication, native enzyme
33.7
cellobiose
-
pH and temperature not specified in the publication, immobilized enzyme
37.3
cellobiose
-
pH 7.0, 75°C, enzyme immobilized on chitosan activated with glutaraldehyde
697
ginsenoside Rb1
mutant enzyme W361F, at pH 5.5 and 95°C
407
laminaribiose
-
pH and temperature not specified in the publication, native enzyme
410
laminaribiose
-
pH and temperature not specified in the publication, recombinant enzyme
additional information
additional information
-
the efficiency (kcat/KM) increases with temperature and reaches its maximal efficiency at 65°C. Reactions with 4-nitrophenyl-beta-D-glucoside and 2-nitrophenyl-beta-D-glucoside show a biphasic behavior in LineweaverBurk plots, suggesting that transglycosylation reactions occur at higher substrate concentrations. Kinetic constants obtained at lower or higher substrate concentrations are calculated
-
additional information
additional information
-
kinetic constants for transglycosylation reactions
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
46
D-glucose
pH 5.0, 70°C, substrate: 4-nitrophenyl beta-D-galactopyranoside
0.000053
glucoimidazole
-
pH 6.5, temperature not specified in the publication
additional information
2-phenethyl glucoimidazole
-
Ki is below 0.6 nM, pH 6.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0019
wild type enzyme, with ginsenoside C-Mc1 as substrate, at pH 5.5 and 95°C
0.0072
mutant enzyme W361F, with ginsenoside C-Mc as substrate, at pH 5.5 and 95°C
0.012
mutant enzyme W361F, with ginsenoside C-Mc1 as substrate, at pH 5.5 and 95°C
0.0126
wild type enzyme, with ginsenoside C-Mc1 as substrate, at pH 5.5 and 95°C
0.0154
wild type enzyme, with ginsenoside C-Mc as substrate, at pH 5.5 and 95°C
0.0201
wild type enzyme, with ginsenoside Rc as substrate, at pH 5.5 and 95°C
0.0233
mutant enzyme W361F, with ginsenoside Rc as substrate, at pH 5.5 and 95°C
0.0355
mutant enzyme W361F, with naringin as substrate, at pH 5.5 and 95°C
0.0391
wild type enzyme, with hesperidin as substrate, at pH 5.5 and 95°C
0.0567
mutant enzyme L213A, with ginsenoside C-Mc1 as substrate, at pH 5.5 and 95°C
0.0661
wild type enzyme, with ginsenoside C-Mc as substrate, at pH 5.5 and 95°C
0.0802
mutant enzyme L213A, with ginsenoside Rd as substrate, at pH 5.5 and 95°C
0.146
mutant enzyme L213A, with ginsenoside C-Mc as substrate, at pH 5.5 and 95°C
0.211
wild type enzyme, with ginsenoside Rd as substrate, at pH 5.5 and 95°C
0.233
wild type enzyme, with naringin as substrate, at pH 5.5 and 95°C
0.288
mutant enzyme W361F, with hesperidin as substrate, at pH 5.5 and 95°C
0.338
wild type enzyme, with ginsenoside Rd as substrate, at pH 5.5 and 95°C
0.52
wild type enzyme, with ginsenoside Rb2 as substrate, at pH 5.5 and 95°C
0.54
mutant enzyme L213A, with ginsenoside Rb2 as substrate, at pH 5.5 and 95°C
1.18
mutant enzyme L213A, with ginsenoside C-Y as substrate, at pH 5.5 and 95°C
1.347
mutant enzyme W361F, with ginsenoside C-Y as substrate, at pH 5.5 and 95°C
1.415
mutant enzyme W361F, with ginsenoside Rd as substrate, at pH 5.5 and 95°C
1.643
wild type enzyme, with ginsenoside Rb2 as substrate, at pH 5.5 and 95°C
1.74
wild type enzyme, with ginsenoside C-Y as substrate, at pH 5.5 and 95°C
127
-
mutant E387G, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
13.13
wild type enzyme, with ginsenoside F2 as substrate, at pH 5.5 and 95°C
13.227
mutant enzyme W361F, with ginsenoside F2 as substrate, at pH 5.5 and 95°C
13.65
mutant enzyme L213A, with ginsenoside Rb1 as substrate, at pH 5.5 and 95°C
15
-
mutant E387G, substrate 4-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
150
-
wild-type, substrate 4-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
166
19.1
-
wild-type, substrate 2-nitrophenyl beta-D-xylopyranoside, pH 3.0, 65°C
196
-
wild-type, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
2.031
mutant enzyme W361F, with ginsenoside C-O as substrate, at pH 5.5 and 95°C
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
219
-
wild-type, substrate 2-nitrophenyl beta-D-galactopyranoside, pH 3.0, 65°C
24.1
wild type enzyme, 1ith ginsenoside F2 as substrate, at pH 5.5 and 95°C
253
-
wild-type, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
3.213
mutant enzyme W361F, with ginsenoside Rb1 as substrate, at pH 5.5 and 95°C
33.4
mutant enzyme L213A, 1ith ginsenoside F2 as substrate, at pH 5.5 and 95°C
4.05
mutant enzyme L213A, with ginsenoside C-O as substrate, at pH 5.5 and 95°C
4.24
wild type enzyme, with ginsenoside C-O as substrate, at pH 5.5 and 95°C
4.388
wild type enzyme, with ginsenoside C-Y as substrate, at pH 5.5 and 95°C
5.082
wild type enzyme, with ginsenoside Rb1 as substrate, at pH 5.5 and 95°C
6.354
wild type enzyme, with ginsenoside C-O as substrate, at pH 5.5 and 95°C
63.3
-
mutant E387G, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
8.56
wild type enzyme, with ginsenoside Rb1 as substrate, at pH 5.5 and 95°C
9.077
mutant enzyme W361F, with ginsenoside Rb2 as substrate, at pH 5.5 and 95°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.5
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
7
-
in 50 mM sodium phosphate buffer, substrate: 2-nitrophenyl beta-D-galactopyranoside
7
-
in 50 mM sodium phosphate buffer, substrate: 2-nitrophenyl-beta-D-galactopyranoside
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
additional information
-
activity dependence on pH at 65°C and 75°C on 5 mM 4-nitrophenyl beta-D-galactoside
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
80
95
75
-
the specific activity of the mutant increases with temperature up to 75°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
326274, 715512, 718769, 719097, 719558, 719756, 720221, 720966, 721006, 721007, 721008, 721315, 721362, 721468, 722128
-
-
brenda
-
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BGAL_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
489
0
56692
Swiss-Prot
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
240000
56690
quadrupole time-of-flight electrospray mass spectrometry
60000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
tetramer
-
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
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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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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)
E387Q
E432C
F222A
the mutant shows 105% activity towards ginsenoside Rd compared to the wild type enzyme
F359A
the mutant shows 84% activity towards ginsenoside Rd compared to the wild type enzyme
H342A
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
H489A
-
mutation produces faster enzyme inactivation, kcat/KM for 2-nitrophenyl beta-D-galactopyranoside is 85% of the wild-type value
K219R
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
L213A
L213Q
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
L213W
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
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
S220A
the mutant shows 92% activity towards ginsenoside Rd compared to the wild type enzyme
V209A
the mutant shows 170% activity towards ginsenoside Rd compared to the wild type enzyme
V209G
the mutant shows 60% activity towards ginsenoside Rd compared to the wild type enzyme
V209L
the mutant shows 10% activity towards ginsenoside Rd compared to the wild type enzyme
V209T
the mutant shows 80% activity towards ginsenoside Rd compared to the wild type enzyme
W361A
the mutant shows 241% activity towards ginsenoside Rd compared to the wild type enzyme
W361F
the mutant exhibits 4.2fold higher activity, 3.7fold higher catalytic efficiency, and 3.1fold lower binding energy for ginsenoside Rd than the wild type enzyme. The mutant completely converts ginsenoside Rb1 to compound K and shows also 7.4fold higher activity for hesperidin than the wild type enzyme
W361G
the mutant shows about 290% activity towards ginsenoside Rd compared to the wild type enzyme
W361L
the mutant shows about 40% activity towards ginsenoside Rd compared to the wild type enzyme
W361T
the mutant shows about 350% activity towards ginsenoside Rd compared to the wild type enzyme
W361Y
the mutant shows about 230% activity towards ginsenoside Rd compared to the wild type enzyme
W433C
F222A
-
the mutant shows 105% activity towards ginsenoside Rd compared to the wild type enzyme
-
F359A
-
the mutant shows 84% activity towards ginsenoside Rd compared to the wild type enzyme
-
K219R
-
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
-
L213A
L213W
-
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol)
-
S220A
-
the mutant shows 92% activity towards ginsenoside Rd compared to the wild type enzyme
-
W361A
-
the mutant shows 241% activity towards ginsenoside Rd compared to the wild type enzyme
-
E206Q
E432C
W433C
additional information
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
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 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
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
E432C
-
kcat/KM is reduced for 4-methylumbelliferyl beta-D-glucopyranoside is reduced 200fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-galactopyranoside is reduced 130fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-mannopyranoside is reduced 16fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-xylopyranoside is reduced 14fold
E432C
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
L213A
the mutant shows 110% activity with ginsenoside Rd compared to the wild type enzyme
L213A
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol). The variant enzyme converts ginsenosides Rc and C-Mc into C-K with molar conversions of 97%, which are 1.5 and 2fold higher, respectively, than those of the 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
W433C
-
kcat/KM is reduced for 4-methylumbelliferyl beta-D-glucopyranoside is reduced 140fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-galactopyranoside is reduced 230fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-mannopyranoside is reduced 10fold, kcat/KM is reduced for 4-methylumbelliferyl beta-D-xylopyranoside is reduced 12fold
W433C
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
L213A
-
the mutant with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to ginsenoside C-K (i.e. 20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol). The variant enzyme converts ginsenosides Rc and C-Mc into C-K with molar conversions of 97%, which are 1.5 and 2fold higher, respectively, than those of the wild type enzyme
-
L213A
-
the mutant shows 110% activity with ginsenoside Rd compared to the wild type enzyme
-
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
-
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 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
-
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
-
E432C
-
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
-
W433C
-
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
-
isolation of mutants with reduced expression of lacS. The mechanism of control occurs at the level of transcription. The mutations result in undetectable levels of lacS mRNA. The mechanism of reduction in lacS mRNA levels is unknown. It may result from events that act at the level of mRNA synthesis or mRNA degradation. Glycosyl hydrolase production in Sulfolobuis solfataricus requires a trans-acting factor for wild-type levels of expression. The trans-acting factor must recognize elements inherent to all target genes
additional information
generation of functional glycoside hydrolase hybrids by shuffling of the genes coding for Pyrococcus furiosus CelB and Sulfolobus solfataricus LacS. Generating of thermostable hybrid beta-glycosidases and isolating high-performance variants
additional information
-
isolation of mutants with reduced expression of lacS. The mechanism of control occurs at the level of transcription. The mutations result in undetectable levels of lacS mRNA. The mechanism of reduction in lacS mRNA levels is unknown. It may result from events that act at the level of mRNA synthesis or mRNA degradation. Glycosyl hydrolase production in Sulfolobuis solfataricus requires a trans-acting factor for wild-type levels of expression. The trans-acting factor must recognize elements inherent to all target genes
-
additional information
-
generation of functional glycoside hydrolase hybrids by shuffling of the genes coding for Pyrococcus furiosus CelB and Sulfolobus solfataricus LacS. Generating of thermostable hybrid beta-glycosidases and isolating high-performance variants
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
30 - 100
-
pH 6.5, no denaturation occurrs in the temperature range of 30 to 100°C for both the native and recombinant enzyme
5
-
after a storage greater than 40 h at atmospheric pressure, the residual activity decreases
60
70
75
80
85
90
additional information
75
-
5 h, enzyme immobilized on chitosan activated with glutaraldehyde, 15% loss of activity
75
-
90 min, 70% residual cell enzymatic activity in the aqueous phase
85
-
k(inact): 0.0000061 (wild-type enzyme), 0.00012 (mutant enzyme R488A), 0.00029 (mutant enzyme H489A), 0.00001 (mutant enzyme delHis489)
85
-
5 h, enzyme immobilized on chitosan activated with glutaraldehyde, 25% loss of activity
85
-
denaturation temperature. The temperature-induced denaturation of this tetrameric enzyme is a complex and irreversible process, in which subunit dissociation is coupled with unfolding, while unfolded polypeptide chains tend to associate in a nonspecific manner
90
-
low concentrations of the detergent (up to 0.02%) induce slight changes in the enzyme secondary structure, whereas high concentrations cause the alpha-helix content to increase at high temperatures and prevent protein aggregation
90
-
low concentrations of the SDS (up to 0.02%) induce slight changes in the enzyme secondary structure, whereas high concentrations cause the alpha-helix content to increase at high temperatures and prevent protein aggregation
additional information
-
an important role of the sequence segment present only in hyperthermophilic beta-glycosidases, in the thermal adaptation of archaea beta-glycosidases is hypothesized. The thermostabilization mechanism could occur as a consequence of numerous favorable ionic interactions of the 83124 sequence with the other part of protein matrix that becomes more rigid and less accessible to the insult of thermal-activated solvent molecules
additional information
-
the fluorescence emission is characterized by a bimodal lifetime distribution, suggesting that the enzyme structure contains rigid and flexible regions, properly located in the macromolecule. The enzyme activity and thermostability appear to be related to the dynamic properties of these regions as evidenced by perturbation studies of the enzyme structure at alkaline pH and by addition of detergents such as SDS. The pH increase affects the protein dynamics with a remarkable loss of thermal stability and activity; these changes occur without any significant variation in the secondary structure as revealed by far-UV dichroic measurements. In the presence of 0.02% (w/v) SDS at alkaline pH, the enzymatic activity and thermostability are recovered. Under these conditions, the conformational dynamics appear to be similar to that evidenced at neutral pH. Further inreases in SDS concentration, at alkaline pH, render the activity and thermostability of beta-glycosidase similar to those observed in the absence of detergent
additional information
-
the thermostable enzyme is an interesting model system for the study of protein adaptation to high temperatures. The largest ion-pair network of the enzyme is located at the tetrameric interface of the molecule
additional information
-
inactivation is coupled to irreversible aggregation
additional information
-
the conformational transitions of thermophilic beta-glycosidase from Sulfolobus solfataricus and the mechanism of its thermal and chemical activation are studied by electron paramagnetic resonance of nitroxide spin labels immobilized on the protein matrix
additional information
-
protein contains 68 tryptophans, two distinct classes of tryptophanyl residues that differ in microenvironmental characteristics. The conformational dynamics of the two classes of tryptophanyl residues is affected differently by temperature, suggesting that the protein regions in which they are located give different contributions to enzyme properties, such as flexibility, stability and function
additional information
-
the thermostability is affected by the nature and charge of the cations, reaching maximal effects for the case of Mg2+. Cations can cause a strong attenuation of the ion pair interactions E474K72 and D473R402, with consequent partial dissociation of the tetrameric structure
additional information
-
thermostability is not affected by the presence of Mg2+
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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
-
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
-
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
-
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
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
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
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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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Trap column chromatography, and Superdex 200 gel filtration
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
-
-
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression 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 in Escherichia coli
-
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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
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
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
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
-
-
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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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
nutrition
-
catalyst of lactose hydrolysis in dairy products in the food industry
synthesis
food industry
-
the enzyme suitable for hydrolysis of lactose at temperatures at 70-80°C
food industry
-
the immobilized enzyme is useful for the hydrolysis of lactose in whey or milk by using a packed-bed enzyme reactor operated at 70°C
synthesis
-
a continuous stirred-tank reactor charged with the enzyme and operated at steady-state conditions could be a useful reaction system for the production of galacto-oligosaccharides in which composition is narrower and more easily programmable, in terms of the individual components contained, as compared to the batchwise reaction
synthesis
-
development of a continuous cellobiose hydrolysis system for glucose production with a high degree of conversion by the enzyme immobilized on chitosan activated with glutaraldehyde
synthesis
-
enzymatic synthesis of 2-beta-D-galactopyranosyloxyethyl methacrylate starting from 2-hydroxyethyl methacrylate and 4-nitrophenyl-beta-D-galactopyranoside
synthesis
-
enzymatic synthesis of polyol- and masked polyol-glycosides. The enzyme performs the synthesis of glycosides in a competitive high yield compared with that obtained with mesophilic enzymes. It permits the use of a wide variety of acceptors including tetritol compounds and their masked or protected derivatives. The synthesis of glucosides of 2,3-isopropylidene protected pure enantiomers of threitol shows the possibility of obtaining reasonable yields of products in the presence of a scarce amount of the acceptor by adding aliquots of donor at time intervals, in such a way that a molar excess of acceptor was maintained, thus avoiding undesirable formation of glycosides of the donor or enzymatic hydrolysis of the product
synthesis
formation of mannosides and xylosides by transglycosylation
synthesis
-
high yield production of hydroxytyrosol from a commercially available oleuropein by using the immobilised recombinant EcSbgly from the hyperthermophilic archaeon Sulfolobus solfataricus on chitosan support
synthesis
-
industrial production of galactooligosaccharides, very efficient enzyme for the synthesis of beta-galactooligosaccharides because of its high product yields, transfer rates, substrate specificity, and thermostability
synthesis
optimization of hexyl-beta-D-glycoside synthesis from lactose in hexanol at low water activity and high temperature. Compared to other beta-glycosidases in lactose conversion into alkyl glycoside, the enzyme shows high activity in a hexanol one-phase system and synthesized high yields of both hexyl-beta-D-galactoside and hexyl-beta-D-glucoside. Using 32 g/l lactose (93 mM), the enzyme synthesizes yields of 41% galactoside (38.1 mM) and 29% glucoside (27.0 mM)
synthesis
-
synthesis of 2-deoxyglycosides and 2-deoxygalactosides from glucal or galactal as donors. The yields observed with alkyl acceptors confirms that the robustness of the biocatalyst is of great help in designing practical syntheses of pure beta-anomers of 2-deoxy derivatives of 4-penten-1-ol (obtained in 80% yield at 20 fold molar excess) and 3,4-dimethoxybenzyl alcohol (obtained in 19% yield at 3.3 fold molar excess). The attachment of 2-deoxyglyco units is performed on various pyranosidic acceptors (4-nitrophenyl alpha-D-glucopyranoside, 2-nitrophenyl 2-deoxy-N-acetyl-alpha-D-glucosamine and 4-nitrophenyl 2-deoxy-N-acetyl-beta-D-glucosamine). At low molecular excesses of the acceptors, satisfactory yields (20-40%) of chromophoric 2-deoxy di- and trisaccharides are obtained
synthesis
-
synthesis of ginsenoside K (20-O-beta-D-glucopyranosyl-20(S)-protopanaxadiol) by a recombinant enzyme. 20-O-beta-D-Glucopyranosyl-20(S)-protopanaxadiol has anti-tumor, anti-inflammatory, anti-allergic and hepatoprotective effects
synthesis
-
the immobilized enzyme is useful for the production of galactooligosaccharides by using a packed-bed enzyme reactor operated at 70°C
synthesis
application of the alpha-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus along with the beta-glycosidase from Sulfolobus solfataricus to yield ginsenoside compound K from the protopanaxadiol-type ginsenosides in red-ginseng extracts. The optimal reaction conditions are pH 6.0, 80°C, 2 U/ml beta-glucosidase, 3 U/ml alpha-L-arabinofuranosidase, and 7.5 g/l ginsenosides in red-ginseng extract. Under these optimized conditions 4.2 g/l ginsenoside compound K from 7.5 g/l protopanaxadiol-type ginsenosides is obtained in 12 h without other ginsenosides, with a molar yield of 100% and a productivity of 348 mg/l/h
synthesis
-
optimization of hexyl-beta-D-glycoside synthesis from lactose in hexanol at low water activity and high temperature. Compared to other beta-glycosidases in lactose conversion into alkyl glycoside, the enzyme shows high activity in a hexanol one-phase system and synthesized high yields of both hexyl-beta-D-galactoside and hexyl-beta-D-glucoside. Using 32 g/l lactose (93 mM), the enzyme synthesizes yields of 41% galactoside (38.1 mM) and 29% glucoside (27.0 mM)
-
synthesis
-
formation of mannosides and xylosides by transglycosylation
-
synthesis
-
application of the alpha-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus along with the beta-glycosidase from Sulfolobus solfataricus to yield ginsenoside compound K from the protopanaxadiol-type ginsenosides in red-ginseng extracts. The optimal reaction conditions are pH 6.0, 80°C, 2 U/ml beta-glucosidase, 3 U/ml alpha-L-arabinofuranosidase, and 7.5 g/l ginsenosides in red-ginseng extract. Under these optimized conditions 4.2 g/l ginsenoside compound K from 7.5 g/l protopanaxadiol-type ginsenosides is obtained in 12 h without other ginsenosides, with a molar yield of 100% and a productivity of 348 mg/l/h
-
synthesis
-
enzymatic synthesis of polyol- and masked polyol-glycosides. The enzyme performs the synthesis of glycosides in a competitive high yield compared with that obtained with mesophilic enzymes. It permits the use of a wide variety of acceptors including tetritol compounds and their masked or protected derivatives. The synthesis of glucosides of 2,3-isopropylidene protected pure enantiomers of threitol shows the possibility of obtaining reasonable yields of products in the presence of a scarce amount of the acceptor by adding aliquots of donor at time intervals, in such a way that a molar excess of acceptor was maintained, thus avoiding undesirable formation of glycosides of the donor or enzymatic hydrolysis of the product
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
D'Auria, S.; Morana, A.; Febbraio, F.; Vaccaro, C.; De Rosa, M.; Nucci, R.
Functional and structural properties of the homogeneous beta-glycosidase from the extreme thermoacidophilic archaeon Sulfolobus solfataricus expressed in Saccharomyces cerevisiae
Protein Expr. Purif.
7
299-308
1996
Saccharolobus solfataricus
brenda
Cobucci-Ponzano, B.; Aurilia, V.; Riccio, G.; Henrissat, B.; Coutinho, P.M.; Strazzulli, A.; Padula, A.; Corsaro, M.M.; Pieretti, G.; Pocsfalvi, G.; Fiume, I.; Cannio, R.; Rossi, M.; Moracci, M.
A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2
J. Biol. Chem.
285
20691-20703
2010
Saccharolobus solfataricus
brenda
D'Auria, S.; Barone, R.; Rossi, M.; Nucci, R.; Barone, G.; Fessas, D.; Bertoli, E.; Tanfani, F.
Effects of temperature and SDS on the structure of beta-glycosidase from the thermophilic archaeon Sulfolobus solfataricus
Biochem. J.
323
833-840
1997
Saccharolobus solfataricus
brenda
D'Auria, S.; Nucci, R.; Rossi, M.; Gryczynski, I.; Gryczynski, Z.; Lakowicz, J.R.
The beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: enzyme activity and conformational dynamics at temperatures above 100 degrees C
Biophys. Chem.
81
23-31
1999
Saccharolobus solfataricus
brenda
Haseltine, C.; Montalvo-Rodriguez, R.; Carl, A.; Bini, E.; Blum, P.
Extragenic pleiotropic mutations that repress glycosyl hydrolase expression in the hyperthermophilic archaeon Sulfolobus solfataricus
Genetics
152
1353-1361
1999
Saccharolobus solfataricus, Saccharolobus solfataricus 98/2
brenda
Petzelbauer, I.; Splechtna, B.; Nidetzky, B.
Galactosyl transfer catalyzed by thermostable beta-glycosidases from Sulfolobus solfataricus and Pyrococcus furiosus: kinetic studies of the reactions of galactosylated enzyme intermediates with a range of nucleophiles
J. Biochem.
130
341-349
2001
Saccharolobus solfataricus
brenda
Aguilar, C.F.
Sanderson, I.; Moracci, M.; Ciaramella, M.; Nucci, R.; Rossi, M.; Pearl, L.H.: Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability
J. Mol. Biol.
271
789-802
1997
Saccharolobus solfataricus
brenda
Moracci, M.; Capalbo, L.; Ciaramella, M.; Rossi, M.
Identification of two glutamic acid residues essential for catalysis in the beta-glycosidase from the thermoacidophilic archaeon Sulfolobus solfataricus
Protein Eng.
9
1191-1195
1996
Saccharolobus solfataricus, Saccharolobus solfataricus MT4
brenda
D'Auria, S.; Rossi, M.; Nucci, R.; Irace, G.; Bismuto, E.
Perturbation of conformational dynamics, enzymatic activity, and thermostability of beta-glycosidase from archaeon Sulfolobus solfataricus by pH and sodium dodecyl sulfate detergent
Proteins
27
71-79
1997
Saccharolobus solfataricus
brenda
Cobucci-Ponzano, B.; Moracci, M.; Lauro, B.; Ciaramella, M.; DAvino, R.; Rossi, M.
Ionic network at the C-terminus of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Functional role in the quaternary structure thermal stabilization
Proteins
48
98-106
2002
Saccharolobus solfataricus
brenda
Bismuto, E.; Febbraio, F.; Limongelli, S.; Briante, R.; Nucci, R.
Dynamic fluorescence studies of β-glycosidase mutants from Sulfolobus solfataricus: Effects of single mutations on protein thermostability
Proteins
51
10-20
2003
Saccharolobus solfataricus
brenda
Grogan, D.W.
Evidence that beta-galactosidase of Sulfolobus solfataricus is only one of several activities of a thermostable beta-D-glycosidase
Appl. Environ. Microbiol.
57
1644-1649
1991
Saccharolobus solfataricus, Saccharolobus solfataricus P2
brenda
Shames, A.I.; Nucci, R.; D'Auria, S.; Febbraio, F.; Vaccaro, C.; Lozinsky, E.; Rossi, M.; Likhtenshtein, G.I.
EPR spin labeling study of conformational transitions of beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus expressed in Escherichia coli
Appl. Magn. Reson.
18
515-526
2000
Saccharolobus solfataricus
-
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Cobucci-Ponzano, B., Perugino, G., Trincone, A., Mazzone, M., Di Lauro, B., Giordano, A., Rossi, M., Moracci, M.
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Saccharolobus solfataricus
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Expression and extensive characterization of a beta-glycosidase from the extreme thermoacidophilic archaeon Sulfolobus solfataricus in Escherichia coli: authenticity of the recombinant enzyme
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Saccharolobus solfataricus
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Petzelbauer, I.; Reiter, A.; Splechtna, B.; Kosma, P.; Nidetzky, B.
Transgalactosylation by thermostable beta-glycosidases from Pyrococcus furiosus and Sulfolobus solfataricus. Binding interactions of nucleophiles with the galactosylated enzyme intermediate make major contributions to the formation of new beta-glycosides
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Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617 (P22498)
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Extremophiles
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Saccharolobus solfataricus
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D'Auria, S.; Pellino, F.; La Cara, F.; Barone, R.; Rossi, M.; Nucci, R.
Immobilization on chitosan of a thermophilic beta-glycosidase expressed in Saccharomyces cerevisiae
Appl. Biochem. Biotechnol.
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Saccharolobus solfataricus
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Tricone, A.; Improta, R.; Gambacorta, A.
Enzymatic synthesis of polyol- and masked polyol-glycosides using beta-glycosidase of Sulfolobus
Biocatal. Biotransform.
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1995
Saccharolobus solfataricus, Saccharolobus solfataricus DSM 5833
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Huneke, F.-U.; Nucci, R.; Cowan, D.
Effect of water miscible organic solvents on kinetics of a thermostable beta-glycosidase
Biocatal. Biotransform.
17
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1999
Saccharolobus solfataricus
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brenda
Hansson, T.; Adlercreutz, P.
Enzymatic synthesis of hexyl glycosides from lactose at low water activity and high temperature using hyperthermostable beta-glycosidases
Biocatal. Biotransform.
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2002
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus P2 (P22498)
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Kaper, T.; Brouns, S.J.; Geerling, A.C.; De Vos, W.M.; Van der Oost, J.
DNA family shuffling of hyperthermostable beta-glycosidases
Biochem. J.
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2002
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus P2 (P22498)
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Febbraio, F.; Barone, R.; D'Auria, S.; Rossi, M.; Nucci, R.; Piccialli, G.; De Napoli, L.; Orru, S.; Pucci, P.
Identification of the active site nucleophile in the thermostable beta-glycosidase from the archaeon Sulfolobus solfataricus expressed in Escherichia coli
Biochemistry
36
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1997
Saccharolobus solfataricus
brenda
Catanzano, F.; Graziano, G.; De Paola, B.; Barone, G.; D'Auria, S.; Rossi, M.; Nucci, R.
Guanidine-induced denaturation of beta-glycosidase from Sulfolobus solfataricus expressed in Escherichia coli
Biochemistry
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1998
Saccharolobus solfataricus
brenda
Moracci, M.; Trincone, A.; Perugino, G.; Ciaramella, M.; Rossi, M.
Restoration of the activity of active-site mutants of the hyperthermophilic beta-glycosidase from Sulfolobus solfataricus: dependence of the mechanism on the action of external nucleophiles
Biochemistry
37
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1998
Saccharolobus solfataricus
brenda
Gloster, T.M.; Roberts, S.; Ducros, V.M.; Perugino, G.; Rossi, M.; Hoos, R.; Moracci, M.; Vasella, A.; Davies, G.J.
Structural studies of the beta-glycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors
Biochemistry
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Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P22498)
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Structural, kinetic, and thermodynamic analysis of glucoimidazole-derived glycosidase inhibitors
Biochemistry
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Saccharolobus solfataricus
brenda
Hamon, V.; Dallet, S.; Legoy, M.D.
The pressure-dependence of two beta-glucosidases with respect to their thermostability
Biochim. Biophys. Acta
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1996
Saccharolobus solfataricus
brenda
D'Auria, S.; Moracci, M.; Febbraio, F.; Tanfani, F.; Nucci, R.; Rossi, M.
Structure-function studies on beta-glycosidase from Sulfolobus solfataricus. Molecular bases of thermostability
Biochimie
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1989
Saccharolobus solfataricus
brenda
Noh, K.H.; Son, J.W.; Kim, H.J., Oh, D.K.
Ginsenoside compound K production from ginseng root extract by a thermostable beta-glycosidase from Sulfolobus solfataricus
Biosci. Biotechnol. Biochem.
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Saccharolobus solfataricus
brenda
Morana, A.; Moracci, M.; Ottombrino, A.; Ciaramella, M.; Rossi, M.; De Rosa, M.
Industrial-scale production and rapid purification of an archaeal beta-glycosidase expressed in Saccharomyces cerevisiae
Biotechnol. Appl. Biochem.
22
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1995
Saccharolobus solfataricus
brenda
Santin, M.; Rosso, F.; Sada, A.; Peluso, G.; Improta, R.; Trincone, A.
Enzymatic synthesis of 2-beta-D-galactopyranosyloxy ethyl methacrylate (GalEMA) by the thermophilic archeon Sulfolobus solfataricus
Biotechnol. Bioeng.
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217-222
1996
Saccharolobus solfataricus
brenda
Petzelbauer, I.; Nidetzky, B.; Haltrich, D.; Kulbe, K.D.
Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable beta-glycosidases
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Saccharolobus solfataricus
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Petzelbauer, I.; Zeleny, R.; Reiter, A.; Kulbe, K.D.; Nidetzky, B.
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Saccharolobus solfataricus
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Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. III. Utilization of two thermostable beta-glycosidases in a continuous ultrafiltration membrane reactor and galacto-oligosaccharide formation under steady-state conditions
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Saccharolobus solfataricus
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Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable beta-glycosidases and optimization of a packed-bed reactor for lactose conversion
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Saccharolobus solfataricus
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Chembiochem
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Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P22498)
brenda
Reuter, S.; Rusborg Nygaard, A.; Zimmermann, W.
beta-Galactooligosaccharide synthesis with beta-galactosidases from Sulfolobus solfataricus, Aspergillus oryzae, and Escherichia coli
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Saccharolobus solfataricus
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Bismuto, E.; Nucci, R.; Febbraio, F.; Tanfani, F.; Gentile, F.; Briante, R.; Scire, A.; Bertoli, E.; Amodeo, P.
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Saccharolobus solfataricus
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Bismuto, E.; Irace, G.; D'Auria, S.; Rossi, M.; Nucci, R.
Multitryptophan-fluorescence-emission decay of beta-glycosidase from the extremely thermophilic archaeon Sulfolobus solfataricus
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Saccharolobus solfataricus
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Corbett, K.; Fordham-Skelton, A.P.; Gatehouse, J.A.; Davis, B.G.
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Saccharolobus solfataricus
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Saccharolobus solfataricus (P22498), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P22498)
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Saccharolobus solfataricus, Saccharolobus solfataricus MT4
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Thermal stability and aggregation of Sulfolobus solfataricus beta-glycosidase are dependent upon the N-epsilon-methylation of specific lysyl residues: critical role of in vivo post-translational modifications
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Saccharolobus solfataricus, Saccharolobus solfataricus MT4
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Briante, R.; La Cara, F.; Febbraio, F.; Barone, R.; Piccialli, G.; Carolla, R.; Mainolfi, P.; De Napoli, L.; Patumi, M.; Fontanazza, G.; Nucci, R.
Hydrolysis of oleuropein by recombinant beta-glycosidase from hyperthermophilic archaeon Sulfolobus solfataricus immobilised on chitosan matrix
J. Biotechnol.
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Saccharolobus solfataricus
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Lozinsky, E.; Febbraio, F.; Shames, A.I.; Likhtenshtein, G.I.; Bismuto, E.; Nucci, R.
Heterogeneity in the structural dynamics of Sulfolobus solfataricus beta-glycosidase revealed by electron paramagnetic resonance and frequency domain fluorometry
Protein Sci.
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Saccharolobus solfataricus
brenda
Bismuto, E.; Martelli, P.L.; Casadio, R.; Irace, G.
Tryptophanyl fluorescence lifetime distribution of hyperthermophilic beta-glycosidase from molecular dynamics simulation: a comparison with the experimental data
Protein Sci.
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2000
Saccharolobus solfataricus
brenda
Bismuto, E.; Nucci, R.; Rossi, M.; Irace, G.
Structural and dynamic aspects of beta-glycosidase from mesophilic and thermophilic bacteria by multitryptophanyl emission decay studies
Proteins
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1999
Saccharolobus solfataricus
brenda
Tricone, A.M.; Pagnotta, E.; Rossi, M.; Mazzone, M.; Moracci., M.
Enzymatic synthesis of 2-deoxy-beta-glucosides and stereochemistry of beta-glycosidase from Sulfolobus solfataricus on glucal
Tetrahedron Asymmetry
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2001
Saccharolobus solfataricus
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Nucci, R.; Moracci, M.; Vaccaro, C.; Vespa, N.; Rossi, M.
Exo-glucosidase activity and substrate specificity of the beta-glycosidase isolated from the extreme thermophile Sulfolobus solfataricus
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1993
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
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Perugino, G.; Trincone, A.; Giordano, A.; van der Oost, J.; Kaper, T.; Rossi, M.; Moracci, M.
Activity of hyperthermophilic glycosynthases is significantly enhanced at acidic pH
Biochemistry
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2003
Saccharolobus solfataricus
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Shin, K.C.; Choi, H.Y.; Seo, M.J.; Oh, D.K.
Improved conversion of ginsenoside Rb to compound K by semi-rational design of Sulfolobus solfataricus beta-glycosidase
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Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
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Nguyen, T.T.; Kim, S.B.; Kim, N.M.; Kang, C.; Chung, B.; Park, J.S.; Kim, D.
Production of steviol from steviol glucosides using beta-glycosidase from Sulfolobus solfataricus
Enzyme Microb. Technol.
93-94
157-165
2016
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
brenda
Choi, J.H.; Shin, K.C.; Oh, D.K.
An L213A variant of beta-glycosidase from Sulfolobus solfataricus with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to compound K
PLoS ONE
13
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2018
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
brenda
Shin, K.; Choi, H.; Seo, M.; Oh, D.
Compound K production from red ginseng extract by beta-glycosidase from Sulfolobus solfataricus supplemented with alpha-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus
PLoS ONE
10
e0145876
2015
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
brenda
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