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Information on EC 3.2.1.B33 - Sulfolobus shibatae beta-glycosidase
for references in articles please use BRENDA:EC3.2.1.B33preliminary BRENDA-supplied EC number
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3.2.1.B33 Sulfolobus shibatae beta-glycosidaseSpecify your search results
The expected taxonomic range for this enzyme is: Saccharolobus shibatae
Reaction Schemes
Hydrolysis of beta-glycosidic bonds with broad specificity. It prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
Synonyms
Sulfolobus shibatae beta-glycosidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Sulfolobus shibatae beta-glycosidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of beta-glycosidic bonds with broad specificity. It prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
-
-
-
-
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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
cellobiose + glycerol
beta-D-glucopyranosyl-(1->1)-D-glycerol + D-glucose
-
-
-
-
?
cellobiose + glycerol
beta-D-glucopyranosyl-(1->2)-D-glycerol + D-glucose
-
-
-
-
?
cellobiose + glycerol
beta-D-glucopyranosyl-(1->3)-D-glycerol + D-glucose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
rate of hydrolysis is 43.8% relative to 2-nitrophenyl-beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
rate of hydrolysis is 43.8% relative to 2-nitrophenyl-beta-D-galactopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
cellobiose + H2O
D-glucose + D-glucose
-
rate of hydrolysis is 25.4% relative to 2-nitrophenyl-beta-D-galactopyranoside
-
-
?
cellobiose + H2O
D-glucose + D-glucose
-
the enzyme prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
-
-
?
cellobiose + H2O
D-glucose + D-glucose
-
rate of hydrolysis is 25.4% relative to 2-nitrophenyl-beta-D-galactopyranoside
-
-
?
cellobiose + H2O
D-glucose + D-glucose
-
the enzyme prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
-
-
?
gentiobiose + H2O
D-glucose + D-glucose
-
the enzyme prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
-
-
?
gentiobiose + H2O
D-glucose + D-glucose
-
the enzyme prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
-
-
?
lactose + H2O
D-glucose + beta-D-galactose
-
strong intermolecular transglycosylation activity. Various intermolecular transfer products are formed, indicating that the enzyme prefers lactose as a good acceptor as well as a donor
-
-
?
lactose + H2O
D-glucose + beta-D-galactose
-
strong intermolecular transglycosylation activity. Various intermolecular transfer products are formed, indicating that the enzyme prefers lactose as a good acceptor as well as a donor
-
-
?
lactose + H2O
D-glucose + D-galactose
-
rate of hydrolysis is 15.7% relative to 2-nitrophenyl-beta-D-galactopyranoside
-
-
?
lactose + H2O
D-glucose + D-galactose
-
rate of hydrolysis is 15.7% relative to 2-nitrophenyl-beta-D-galactopyranoside
-
-
?
laminaribiose + H2O
D-glucose + D-glucose
-
the enzyme prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
-
-
?
laminaribiose + H2O
D-glucose + D-glucose
-
the enzyme prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
-
-
?
sophorose + H2O
D-glucose + D-glucose
-
the enzyme prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
-
-
?
sophorose + H2O
D-glucose + D-glucose
-
the enzyme prefers laminaribiose (beta1->3Glc), followed by sophorose (beta1->2Glc), gentiobiose (beta1->6Glc), and cellobiose (beta1->4Glc)
-
-
?
additional information
?
-
transglycosylation activity is tested with lactose as a donor and various sugars as acceptors. When sucrose is used as an acceptor beta-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-beta-D-fructofuranoside is formed
-
-
?
additional information
?
-
-
transglycosylation activity is tested with lactose as a donor and various sugars as acceptors. When sucrose is used as an acceptor beta-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-beta-D-fructofuranoside is formed
-
-
?
additional information
?
-
transglycosylation activity is tested with lactose as a donor and various sugars as acceptors. When sucrose is used as an acceptor beta-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-beta-D-fructofuranoside is formed
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
-
no effect by 1-5 mM. Addition of 10 mM of MnCl2 enhances the hydrolysis activity of rSSG up to 23% whereas most metal ions do not show any considerable effect
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
5 mM, no inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 5% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
4-chloromercuribenzoate
-
5 mM, 94% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 90% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
Ba2+
-
1 mM, 5% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 6% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
Ca2+
-
1 mM, 5% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 6% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
Cd2+
-
no inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 12% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
Cu2+
-
1 mM, 81% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 36% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
Fe2+
-
1 mM, 1% inhibition of 2-nitrophenyl mbeta-D-galactopyranoside hydrolysis, 16% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
Hg2+
-
1 mM, complete inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis and 4-nitrophenyl beta-D-glucopyranoside hydrolysis
monoiodoacetate
-
5 mM, 3% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, no inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
Zn2+
-
1 mM, complete inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis and 4-nitrophenyl beta-D-glucopyranoside hydrolysis
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
-
pH 4.0: apout 5% of maximal activity, pH 5.0: maximal activity, pH 7.0: about 40% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
98
-
hydrolysis of 2-nitrophenyl beta-D-galactopyranoside or 4-nitrophenyl beta-D-glucopyranoside
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80 - 100
-
80°C: about 70% of maximal activity, 100°C: about 80% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
the enzyme retains 50% of the initial activity towards 2-nitrophenyl beta-D-galactopyranoside or 4-nitrophenyl beta-D-glucopyranoside after 146 h and 127 h of incubation in phosphate (pH 7.2) or acetate (pH 5.5) buffers. The half-lifes of the enzyme activity at this temperature are decreased after preincubation in acetate buffer (pH 5.5) up to 32 and 27 h, respectively
80
-
5 h, in 0.1 M acetate buffer (pH 5.5), the enzyme retained about 67% of the initial activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
synthesis
-
synthesis of beta-glucosylglycerol and its derivatives through the transglycosylation by Sulfolobus shibatae beta-glycosidase SSG and Deinococcus geothermalis amylosucrase DGAS. SSG catalyzes a transglycosylation reaction with glycerol as an acceptor and cellobiose as a donor to produce 56% of beta-D-glucopyranosyl-(1->1/3)-D-glycerol and beta-D-glucopyranosyl-(1->4)-D-glycerol. As a result, 61% of alpha-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->1/3)-D-glycerol and 28% of alpha-D-maltopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->1/3)-D-glycerol are synthesized as unnatural glucosylglycerols
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, N.Y.; Baek, N.I.; Cha, J.; Lee, S.B.; Auh, J.H.; Park, C.S.
Production of a new sucrose derivative by transglycosylation of recombinant Sulfolobus shibatae beta-glycosidase
Carbohydr. Res.
340
1089-1096
2005
Saccharolobus shibatae (P50388), Saccharolobus shibatae, Saccharolobus shibatae JCM 8931 (P50388)
brenda
Wolosowska, S.; Synowiecki, J.
Thermostable beta-glucosidase with a broad substrate specifity suitable for processing of lactose-containing products
Food Chem.
85
181-187
2004
Saccharolobus shibatae, Saccharolobus shibatae DSM 5389
-
brenda
Park, N.Y.; Cha, J.; Kim, D.O.; Park, C.S.
Enzymatic characterization and substrate specificity of thermostable beta-glycosidase from hyperthermophilic archaea, Sulfolobus shibatae, expressed in Escherichia coli
J. Microbiol. Biotechnol.
17
454-460
2007
Saccharolobus shibatae, Saccharolobus shibatae JCM 8931
brenda
Jung, D.H.; Seo, D.H.; Park, J.H.; Kim, M.J.; Baek, N.I.; Park, C.
Enzymatic synthesis of beta-glucosylglycerol and its unnatural glycosides via beta-glycosidase and amylosucrase
J. Microbiol. Biotechnol.
28
562-570
2019
Saccharolobus shibatae
brenda
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