Any feedback?
No. of entries
Information on EC 3.2.1.B34 - Sulfolobus acidocaldarius beta-glycosidase
for references in articles please use BRENDA:EC3.2.1.B34
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Old data from external sources may still be available.
Please check here for current data: EC unknown
Please check here for current data: EC unknown
preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.B34 Sulfolobus acidocaldarius beta-glycosidase
The expected taxonomic range for this enzyme is: Sulfolobaceae
Reaction Schemes
showhydrolytic 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, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BgaS
LACS
Saci_1849
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranose
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-galactoside
2-nitrophenol + beta-D-galactose
Substrates: -
Products: -
Products: -
r
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannopyranose
Substrates: 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
Products: -
Products: -
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
Substrates: 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
Products: -
Products: -
?
ginsenoside Rb2 + H2O
ginsenoside Y + D-glucopyranose
Substrates: 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
Products: -
Products: -
?
ginsenoside Rc + H2O
ginsenoside Mc + D-glucopyranose
Substrates: 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
Products: -
Products: -
?
ginsenoside Y + H2O
ginsenoside K + L-arabinopyranose
Substrates: 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
Products: -
Products: -
?
methyl beta-D-galactoside
methanol + beta-D-galactose
Substrates: -
Products: -
Products: -
r
2-nitrophenyl beta-D-fucopyranoside + H2O
2-nitrophenol + D-fucopyranose
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-fucopyranoside + H2O
2-nitrophenol + D-fucopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinoside + H2O
4-nitrophenol + L-arabinopyranose
Substrates: 17% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinoside + H2O
4-nitrophenol + L-arabinopyranose
Substrates: 17% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + D-fucopyranose
Substrates: 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
Products: -
Products: -
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + D-fucopyranose
Substrates: 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
Products: -
Products: -
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
Substrates: 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
Products: -
Products: -
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
Substrates: 28% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
Substrates: 28% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Substrates: 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
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Substrates: 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
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
Substrates: 8% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
Substrates: 8% of the activity compared to 4-nitrophenyl beta-D-glucopyranoside
Products: -
Products: -
?
cellobiose + H2O
2 D-glucose
Substrates: -
Products: -
Products: -
?
cellobiose + H2O
2 D-glucose
Substrates: -
Products: -
Products: -
?
ginsenoside Rb1 + H2O
ginsenoside Rd + ?
Substrates: -
Products: -
Products: -
?
ginsenoside Rb1 + H2O
ginsenoside Rd + ?
Substrates: -
Products: -
Products: -
?
ginsenoside Rd + H2O
ginsenoside K + D-glucopyranose
Substrates: -
Products: -
Products: -
?
ginsenoside Rd + H2O
ginsenoside K + D-glucopyranose
Substrates: -
Products: -
Products: -
?
ginsenoside Rd + H2O
ginsenoside K + D-glucopyranose
Substrates: 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
Products: 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
Products: 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
?
lactose + H2O
D-galactose + D-glucose
Substrates: -
Products: -
Products: -
?
lactose + H2O
D-galactose + D-glucose
Substrates: -
Products: -
Products: -
?
lactose + H2O
D-glucose + D-galactose
Substrates: -
Products: -
Products: -
r
lactose + H2O
D-glucose + D-galactose
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: enzyme shows low activity on the alpha-L-arabinofuranoside linkages in ginsenosides
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows low activity on the alpha-L-arabinofuranoside linkages in ginsenosides
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-galactose
endproduct inhibition, inhibition of enzymeactivity was stronger with glucose than galactose
D-glucose
endproduct inhibition, inhibition of enzyme activity is stronger with glucose than galactose
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-butanol
-
maximal activation is induced by 80 mM 1-butanol (130%). The activation at 30"C becomes less with increasing temperature and at 75°C is only 10%. Alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
1-propanol
-
alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
ethanol
-
alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
methanol
-
alcohol modifies the protein microenvironment, leading to a more flexible enzyme structure, which is probably responsible for the enhanced enzymatic activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
192
methyl beta-D-galactoside
relase, of methanol, pH 7.5, 80°C
0.5
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 30°C, presence of 80 mM 1-butanol
1
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 30°C, absence of 1-butanol
4
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 75°C, absence of 1-butanol
11
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 75°C, presence of 80 mM 1-butanol
additional information
cellobiose
wild-type, Km value 17 mg/ml, mutant V212T, 102 mg/ml, respectively, pH 5.0, 50°C
additional information
lactose
wild-type, Km value 101 mg/ml, mutant V212T, 75 mg/ml, respectively, pH 5.0, 50°C
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
1300
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
6.6
methyl beta-D-galactoside
relase, of methanol, pH 7.5, 80°C
24
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 30°C, absence of 1-butanol
55
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 30°C, presence of 80 mM 1-butanol
1320
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 75°C, absence of 1-butanol
1450
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 75°C, presence of 80 mM 1-butanol
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
1200
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
0.034
methyl beta-D-galactoside
relase, of methanol, pH 7.5, 80°C
24
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 30°C, absence of 1-butanol
110
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 30°C, presence of 80 mM 1-butanol
131.9
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 75°C, presence of 80 mM 1-butanol
330
2-nitrophenyl beta-D-galactopyranoside
-
pH 7.4, 75°C, absence of 1-butanol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6.5
pH 5.5: about 80% of maximal activity, pH 6.5: about 60% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
90
92
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80 - 100
80°C: about 70% of maximal activity, 100°C: about 40% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
491
0
57143
Swiss-Prot
-
BGAL_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
489
0
56692
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N211D
mutation changes the polarity close to the putative acid/base catalyst E209, leads to decrease in activity
V212D
mutation changes the polarity close to the putative acid/base catalyst E209, shifts the pH-activity profile towards acidic pH with both lactose and cellobiose as substrates and leads to decrease in activity
V212T
mutation changes the polarity close to the putative acid/base catalyst E209, shifts the pH-activity profile towards acidic pH with both lactose and cellobiose as substrates. Although V212T increases 6fold the Kmvalue with cellobiose, the mutant shows higher specific activity in high substrate concentrations due to greatly reduced produc-tion of trisaccharide by V212T from cellobiose by transglycosylation
N211D
-
mutation changes the polarity close to the putative acid/base catalyst E209, leads to decrease in activity
-
V212D
-
mutation changes the polarity close to the putative acid/base catalyst E209, shifts the pH-activity profile towards acidic pH with both lactose and cellobiose as substrates and leads to decrease in activity
-
V212T
-
mutation changes the polarity close to the putative acid/base catalyst E209, shifts the pH-activity profile towards acidic pH with both lactose and cellobiose as substrates. Although V212T increases 6fold the Kmvalue with cellobiose, the mutant shows higher specific activity in high substrate concentrations due to greatly reduced produc-tion of trisaccharide by V212T from cellobiose by transglycosylation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
synthesis
biotechnology
construction of a series of Sulfolobus-Escherichia coli shuttle vectors based on the small multicopy plasmid pRN1 from Sulfolobus islandicus. The shuttle vectors do not integrate into the genome and do not rearrange. They allow functional overexpression of genes, and the beta-glycosidase (lacS) gene of ulfolobus solfataricus could function as selectable marker in Suldfolobus solfataricus
biotechnology
-
construction of a series of Sulfolobus-Escherichia coli shuttle vectors based on the small multicopy plasmid pRN1 from Sulfolobus islandicus. The shuttle vectors do not integrate into the genome and do not rearrange. They allow functional overexpression of genes, and the beta-glycosidase (lacS) gene of ulfolobus solfataricus could function as selectable marker in Suldfolobus solfataricus
-
synthesis
enzyme is a potential producer of the rare ginsenosides compound K, compound Y, and compound Mc from the major ginsenosides Rb1, Rb2, Rc, and Rd
synthesis
use of alpha-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus, EC 3.2.1.55, along with beta-glycosidase from Sulfolobus solfataricus to produce ginsenoside compound K from the protopanaxadiol-type ginsenosides in red-ginseng extract. The optimal reaction conditions are as follows: pH 6.0, 80°C, 2 U/ml Sulfolobus solfataricus enzyme, 3 U/ml Caldicellulosiruptor saccharolyticus enzyme, and 7.5 g/l protopanaxadiol-type ginsenosides. The enzymes produce 4.2 g/l ginsenoside compound K from 7.5 g/l ginsenosides in 12 h without other ginsenosides, with a molar yield of 100% and a productivity of 348 mg/l/h
synthesis
-
enzyme is a potential producer of the rare ginsenosides compound K, compound Y, and compound Mc from the major ginsenosides Rb1, Rb2, Rc, and Rd
-
synthesis
-
use of alpha-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus, EC 3.2.1.55, along with beta-glycosidase from Sulfolobus solfataricus to produce ginsenoside compound K from the protopanaxadiol-type ginsenosides in red-ginseng extract. The optimal reaction conditions are as follows: pH 6.0, 80°C, 2 U/ml Sulfolobus solfataricus enzyme, 3 U/ml Caldicellulosiruptor saccharolyticus enzyme, and 7.5 g/l protopanaxadiol-type ginsenosides. The enzymes produce 4.2 g/l ginsenoside compound K from 7.5 g/l ginsenosides in 12 h without other ginsenosides, with a molar yield of 100% and a productivity of 348 mg/l/h
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Eur. J. Biochem.
267
5055-5066
2000
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
brenda
Park, A.R.; Kim, H.J.; Lee, J.K.; Oh, D.K.
Hydrolysis and transglycosylation activity of a thermostable recombinant beta-glycosidase from Sulfolobus acidocaldarius
Appl. Biochem. Biotechnol.
160
2236-2247
2010
Sulfolobus acidocaldarius (P14288), Sulfolobus acidocaldarius DSM 639 (P14288)
brenda
D'Auria, S.; Nucci, R.; Rossi, M.; Bertoli, E.; Tanfani, F.; Gryczynski, I.; Malak, H.; Lakowicz, J.R.
beta-Glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: structure and activity in the presence of alcohols
J. Biochem.
126
545-552
1999
Sulfolobus acidocaldarius
brenda
Noh, K.H.; Oh, D.K.
Production of the rare ginsenosides compound K, compound Y, and compound Mc by a thermostable beta-glycosidase from Sulfolobus acidocaldarius
Biol. Pharm. Bull.
32
1830-1835
2009
Sulfolobus acidocaldarius (P14288), Sulfolobus acidocaldarius DSM 639 (P14288)
brenda
Shin, K.C.; Choi, H.Y.; Seo, M.J.; Oh, D.K.
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
Anbarasan, S.; Timoharju, T.; Barthomeuf, J.; Pastinen, O.; Rouvinen, J.; Leisola, M.; Turunen, O.
Effect of active site mutation on pH activity and transglycosylation ofSulfolobus acidocaldarius beta-glycosidase
J. Mol. Catal. B
118
62-69
2015
Sulfolobus acidocaldarius (P14288), Sulfolobus acidocaldarius DSM 639 (P14288)
-
brenda
Berkner, S.; Grogan, D.; Albers, S.V.; Lipps, G.
Small multicopy, non-integrative shuttle vectors based on the plasmid pRN1 for Sulfolobus acidocaldarius and Sulfolobus solfataricus, model organisms of the (cren-)archaea
Nucleic Acids Res.
35
e88
2007
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
brenda
EXTERNAL LINKS (specific for EC-Number 3.2.1.B34)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
