3.2.1.B34: Sulfolobus acidocaldarius beta-glycosidase
This is an abbreviated version!
For detailed information about Sulfolobus acidocaldarius beta-glycosidase, go to the full flat file.
Reaction
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside =
Synonyms
BgaS, LACS, Saci_1849, Sbetagly
ECTree
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Substrates Products
Substrates Products on EC 3.2.1.B34 - Sulfolobus acidocaldarius beta-glycosidase
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REACTION DIAGRAM
2-nitrophenyl beta-D-fucopyranoside + H2O
2-nitrophenol + D-fucopyranose
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?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
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-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranose
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-
-
?
2-nitrophenyl beta-D-galactoside
2-nitrophenol + beta-D-galactose
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-
-
r
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + D-fucopyranose
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannopyranose
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
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-
?
ginsenoside Rb2 + H2O
ginsenoside Y + D-glucopyranose
hydrolysis of the 3-O-beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyl linkage in panaxadiol, activity is higher than hydrolysis of the 20-O-alpha-L-arabinopyranosyl-(1->6)-beta-D-glucopyranose linkage in ginsenoside Y
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-
?
ginsenoside Rc + H2O
ginsenoside Mc + D-glucopyranose
hydrolysis of the 3-O-beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyl linkage in panaxadiol, activity is higher than hydrolysis of the 20-O-alpha-L-arabinopyranosyl-(1->6)-beta-D-glucopyranose linkage in ginsenoside Y
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-
?
ginsenoside Y + H2O
ginsenoside K + L-arabinopyranose
hydrolysis of alpha-L-arabinopyranose linkage in 20-O-alpha-L-arabinopyranosyl-(1->6)-beta-D-glucopyranose, activity is lower than hydrolysis of the 3-O-beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyl linkage in panaxadiol
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-
?
methyl beta-D-galactoside
methanol + beta-D-galactose
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r
2-nitrophenol + D-glucopyranose
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?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
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-
-
?
4-nitrophenol + L-arabinopyranose
17% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
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?
4-nitrophenyl alpha-L-arabinoside + H2O
4-nitrophenol + L-arabinopyranose
17% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
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-
?
4-nitrophenol + D-galactopyranose
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
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-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
28% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
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-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
28% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
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-
?
4-nitrophenol + D-glucopyranose
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-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
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-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
hydrolytic activity with 4-nitrophenyl substrates in the order of decreasing efficiency: 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-D-xylopyranoside
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-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
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-
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?
4-nitrophenol + L-arabinopyranose
8% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
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?
4-nitrophenyl beta-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
8% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
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-
?
ginsenoside K + D-glucopyranose
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?
ginsenoside Rd + H2O
ginsenoside K + D-glucopyranose
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?
ginsenoside Rd + H2O
ginsenoside K + D-glucopyranose
hydrolysis of the 3-O-beta-D-glucopyranosyl-(1->2)-beta-D-glucopyranosyl linkage in panaxadiol, activity is higher than hydrolysis of the 20-O-alpha-L-arabinopyranosyl-(1->6)-beta-D-glucopyranose linkage in ginsenoside Y
the enzyme does not convert compound Mc to compound K due to no activity for the alpha-L-arabinofuranose linkage in 20-O-alpha-L-arabinofuranosyl-(1->6)-beta-D-glucopyranose
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?
lactose + H2O
D-galactose + D-glucose
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?
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enzyme shows low activity on the alpha-L-arabinofuranoside linkages in ginsenosides
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?
additional information
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enzyme additionally catalyzes transglycosylation reactions, making new beta(1->3) and beta(1->6) glycosidic bonds by intermolecular as well as intramolecular transfer reactions. The intramolecular galactosyl transfer of CelB yields beta-D-Galp-(1->6)-D-glucose and beta-D-Galp-(1->3)-D-glucose in a molar ratio of about 1 : 2. Galactosyl transfer from CelB to D-glucose occurs with partitioning ratios, kNu /kwater, which are 170 times those for the reactions of the galactosylated enzyme with 2-propanol. Therefore, the binding interactions with nucleophiles contribute chiefly to formation of new beta-glycosides during lactose conversion. Likewise, noncovalent interactions with the glucose leaving group govern the catalytic efficiencies for the hydrolysis of lactose
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additional information
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enzyme additionally catalyzes transglycosylation reactions, making new beta(1->3) and beta(1->6) glycosidic bonds by intermolecular as well as intramolecular transfer reactions. The intramolecular galactosyl transfer of CelB yields beta-D-Galp-(1->6)-D-glucose and beta-D-Galp-(1->3)-D-glucose in a molar ratio of about 1 : 2. Galactosyl transfer from CelB to D-glucose occurs with partitioning ratios, kNu /kwater, which are 170 times those for the reactions of the galactosylated enzyme with 2-propanol. Therefore, the binding interactions with nucleophiles contribute chiefly to formation of new beta-glycosides during lactose conversion. Likewise, noncovalent interactions with the glucose leaving group govern the catalytic efficiencies for the hydrolysis of lactose
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?
additional information
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enzyme shows low activity on the alpha-L-arabinofuranoside linkages in ginsenosides
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?
additional information
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no activity toward aryl-alpha-glycosides or 4-nitrophenyl beta-L-arabinofuranoside. The enzyme exhibits transglycosylation activity with 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-glucopyranoside, and 4-nitrophenyl beta-D-fucopyranoside in decreasing order of activity, in the reverse order of its hydrolytic activity. The hydrolytic activity is higher toward cellobiose than toward lactose, but the transglycosylation activity is lower with cellobiose than with lactose
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additional information
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enzyme shows transglycosylation activity, producing close to 40% and 60% amounts of trisaccharide compared to the glucose in one h reaction with 100 and 200 g/l cellobiose, respectively
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?
additional information
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no activity toward aryl-alpha-glycosides or 4-nitrophenyl beta-L-arabinofuranoside. The enzyme exhibits transglycosylation activity with 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-glucopyranoside, and 4-nitrophenyl beta-D-fucopyranoside in decreasing order of activity, in the reverse order of its hydrolytic activity. The hydrolytic activity is higher toward cellobiose than toward lactose, but the transglycosylation activity is lower with cellobiose than with lactose
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?
additional information
?
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enzyme shows transglycosylation activity, producing close to 40% and 60% amounts of trisaccharide compared to the glucose in one h reaction with 100 and 200 g/l cellobiose, respectively
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?