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Information on EC 3.2.1.21 - beta-glucosidase and Organism(s) Caldicellulosiruptor saccharolyticus and UniProt Accession P10482

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EC Tree
IUBMB Comments
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
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This record set is specific for:
Caldicellulosiruptor saccharolyticus
UNIPROT: P10482
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Word Map
The taxonomic range for the selected organisms is: Caldicellulosiruptor saccharolyticus
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-glucosidase, linamarase, beta-glu, emulsin, bglu1, zm-p60.1, bgl1b, cel3a, novozyme 188, t-cell inhibitor, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYNbglA
thermophilic beta-glucosidase
amygdalase
-
-
-
-
amygdalinase
-
-
-
-
arbutinase
-
-
-
-
aryl-beta-glucosidase
-
-
-
-
beta-1,6-glucosidase
-
-
-
-
beta-D-glucosidase
-
-
-
-
beta-D-glucoside glucohydrolase
beta-glucoside hydrolase
-
-
-
-
BGA
-
-
-
-
cellobiase
-
-
-
-
elaterase
-
-
-
-
emulsin
-
-
-
-
gentiobiase
-
-
-
-
limarase
-
-
-
-
Novozyme 188
-
-
-
-
p-nitrophenyl beta-glucosidase
-
-
-
-
primeverosidase
-
-
-
-
salicilinase
-
-
-
-
T-cell inhibitor
-
-
-
-
vicianase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-glucoside glucohydrolase
Wide specificity for beta-D-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-22-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
show the reaction diagram
-
salicin
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
show the reaction diagram
-
-
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
sophorose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
laminaribiose
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
the enzyme catalysed both hydrolysis and transglycosylation
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + beta-D-lactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
show the reaction diagram
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
show the reaction diagram
-
lactose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
cellobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
gentiobiose
-
?
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
cellobiose + H2O
?
show the reaction diagram
highest specific activity
-
-
?
cellopentaose + H2O
?
show the reaction diagram
-
-
-
?
cellotetraose + H2O
?
show the reaction diagram
-
-
-
?
cellotriose + H2O
?
show the reaction diagram
-
-
-
?
gentiobiose + H2O
2 beta-D-glucose
show the reaction diagram
-
-
-
-
?
laminaribiose + H2O
2 beta-D-glucose
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
sophorose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
laminaribiose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
show the reaction diagram
-
lactose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
cellobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
gentiobiose
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-O-methyl-beta-D-glucose
-
competitive inhibition, Ki: 17.5 mM
Co2+
-
destabilizing effect
D-glucono-1,4-lactone
-
Ki: 1.6 mM
D-glucono-1,5-lactone
-
Ki: 0.09 mM
Hg2+
-
strong inactivation at 0.5 mM, reversal by addition of 10 mM beta-mercaptoethanol
La3+
-
rapid inactivation at 3 mM
N-ethylmaleimide
-
rapid loss of activity at 5 mM, reversal by addition of beta-mercaptoethanol
Ni2+
-
strong inhibition
SDS
-
complete inhibition at 1 mg/ml
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.12
2-nitrophenyl beta-D-galactopyranoside
-
-
0.29
2-nitrophenyl beta-D-glucopyranoside
-
-
0.44
4-nitrophenyl-beta-D-fucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
0.24
4-nitrophenyl-beta-D-fucoside
-
-
1.93 - 1.94
4-nitrophenyl-beta-D-galactopyranoside
0.51 - 0.67
4-nitrophenyl-beta-D-glucopyranoside
6.93
4-nitrophenyl-beta-D-xyloside
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
516
4-nitrophenyl-beta-D-fucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
82
4-nitrophenyl-beta-D-galactopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
387
4-nitrophenyl-beta-D-glucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1185
4-nitrophenyl-beta-D-fucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
42
4-nitrophenyl-beta-D-galactopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
579
4-nitrophenyl-beta-D-glucopyranoside
in 50 mM citrate buffer, at pH 5.5 and 70°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
crude extract, at 70°C
0.28
after 163fold purification, using 2-nitrophenyl-beta-D-galactopyranoside as substrate, at 70°C
0.3
after 163fold purification, using 2-nitrophenyl-beta-D-glucopyranoside as substrate, at 70°C
0.32
after 163fold purification, using 4-nitrophenyl-beta-D-xylopyranoside as substrate, at 70°C
0.75
after 163fold purification, using 4-nitrophenyl-beta-D-lactopyranoside as substrate, at 70°C
1.3
after 163fold purification, using 4-nitrophenyl-beta-D-cellobioside as substrate, at 70°C
10.8
after 163fold purification, using cellotetraose as substrate, at 70°C
13
after 163fold purification, using 4-nitrophenyl-beta-D-glucopyranoside as substrate, at 70°C
14.7
after 163fold purification, using 4-nitrophenyl-beta-D-fucopyranoside as substrate, at 70°C
16.2
after 163fold purification, using cellobiose as substrate, at 70°C
6.1
after 163fold purification, using 4-nitrophenyl-beta-D-galactopyranoside as substrate, at 70°C
6.8
after 163fold purification, using cellopentaose as substrate, at 70°C
9.5
after 163fold purification, using cellotriose as substrate, at 70°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BGLS_CALSA
455
0
53492
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 54000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 80
the half-lives of the enzyme at 60, 70, and 80°C are 250, 24.3, and 0.4 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable in the presence of cetyl-trimethylammonium bromide
-
stable in the presence of urea
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetrahydrofuran
-
unstable above 20%, v/v
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heat treatment and His-Trap affinity chromatography
to homogeneity, recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
a reporter gene for the localization of mammalian cells and transgenic tissues based on detection of the bglA (SYNbglA) gene of Caldocellum saccharolyticum that encodes a thermophilic beta-glucosidase is presented. SYNbglA expression can be localized in situ or detected quantitatively in colorimetric assays and can be co-localized with Escherichia coli beta-galactosidase. SYNbglA can be detected in tissue wholemounts and in frozen and wax embedded sections
industry
-
beta-glucosidase is a key enzyme involved in sugar-enzyme platform for fuel ethanol production from lignocellulosic biomass
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Plant, A.R.; Oliver, J.E.; Patchett, M.L.; Daniel, R.M.; Morgan, H.W.
Stability and substrate specificity of a beta-glucosidase from the thermophilic bacterium Tp8 cloned into Escherichia coli
Arch. Biochem. Biophys.
262
181-188
1988
Caldicellulosiruptor saccharolyticus
Manually annotated by BRENDA team
Hong, M.R.; Kim, Y.S.; Park, C.S.; Lee, J.K.; Kim, Y.S.; Oh, D.K.
Characterization of a recombinant beta-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus
J. Biosci. Bioeng.
108
36-40
2009
Caldicellulosiruptor saccharolyticus (A4XIG7), Caldicellulosiruptor saccharolyticus
Manually annotated by BRENDA team
McCutcheon, S.C.; Jones, K.; Cumming, S.A.; Kemp, R.; Ireland-Zecchini, H.; Saunders, J.C.; Houghton, C.A.; Howard, L.A.; Winton, D.J.
Characterization of a heat resistant beta-glucosidase as a new reporter in cells and mice
BMC Biol.
8
89
2010
Caldicellulosiruptor saccharolyticus (P10482), Caldicellulosiruptor saccharolyticus
Manually annotated by BRENDA team
Hansson, T.; Andersson, M.; Wehtje, E.; Adlercreutz, P.
Influence of water activity on the competition between beta-glycosidase-catalysed transglycosylation and hydrolysis in aqueous hexanol
Enzyme Microb. Technol.
29
527-534
2001
Caldicellulosiruptor saccharolyticus, Prunus dulcis, Pyrococcus furiosus
-
Manually annotated by BRENDA team
Singhania, R.R.; Patel, A.K.; Sukumaran, R.K.; Larroche, C.; Pandey, A.
Role and significance of beta-glucosidases in the hydrolysis of cellulose for bioethanol production
Biores. Technol.
127
500-507
2013
Aspergillus aculeatus, Aspergillus fumigatus, Aspergillus niger, Caldicellulosiruptor saccharolyticus, Thermochaetoides thermophila, Saccharomycopsis fibuligera, Humicola insolens, Penicillium citrinum, Talaromyces pinophilus, Rasamsonia emersonii, Neocallimastix patriciarum, Fomitopsis palustris, Penicillium decumbens, Trichoderma atroviride, Stachybotrys sp., Paecilomyces sp. 'thermophila', Penicillium janczewskii, Periconia sp., Schwanniomyces pseudopolymorphus, Fomitopsis sp. RCK2010, Fervidobacterium islandicum, Aspergillus fumigatus Z5
Manually annotated by BRENDA team