Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.21 - beta-glucosidase

for references in articles please use BRENDA:EC3.2.1.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q51723
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The enzyme appears in 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
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-nitrophenyl beta-1,4-D-galactopyranoside 6-phosphate + H2O
?
show the reaction diagram
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
show the reaction diagram
-
-
?
2-nitrophenyl beta-D-galactopyranoside 6-phosphate + H2O
2-nitrophenol + beta-D-galactopyranose 6-phosphate
show the reaction diagram
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
show the reaction diagram
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
show the reaction diagram
-
-
-
?
4-nitrophenyl alpha-L-rhamnopyranoside + H2O
4-nitrophenol + alpha-L-rhamnopyranose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
show the reaction diagram
-
-
-
?
cellobiose + H2O
2 beta-D-glucose
show the reaction diagram
-
-
-
?
ginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
show the reaction diagram
-
ginsenoside Rg1 i.e. 6alpha,20-bis(beta-D-glucopyranosyl)oxy-dammar-24-en-3beta,12beta-diol
-
?
ginsenoside R2 + H2O
ginsenoside Rh1 + D-xylose
show the reaction diagram
-
-
-
?
ginsenoside Re + H2O
ginsenoside Rg1 + L-rhamnose
show the reaction diagram
ginsenoside Re i.e. 20-(beta-D-glucopyranosyl)oxy-6alpha-[alpha-L-rhamnopyranosyl-(1->2)-beta-D-glucopyranosyloxy]dammar-24-en-3beta,12beta-diol
ginsenoside Rg1 i.e. 6alpha,20-bis(beta-D-glucopyranosyl)oxy-dammar-24-en-3beta,12beta-diol
-
?
ginsenoside Rf + H2O
ginsenoside Rh1 + D-glucose
show the reaction diagram
-
-
-
?
ginsenoside Rg2 + H2O
ginsenoside Rh1 + L-rhamnose
show the reaction diagram
-
-
-
?
lactose + H2O
D-glucose + D-galactose
show the reaction diagram
preparation of lactose-free pasteurized milk with a recombinant thermostable beta-glucosidase
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-nitrophenol
the gelatin-immobilized enzyme is less sensitive than the native enzyme
Cu2+
1 mM, 22% inhibition, not significantly stimulated or inhibited by other divalent cations
D-glucose
the gelatin-immobilized enzyme is less sensitive than the native enzyme
phenol
the gelatin-immobilized enzyme is not sensitive in contrast to the native enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
at -20 to 40 °C no significant enzymatic activity is detected in the absence of microwave irradiation. However, a greater than 4 orders of magnitude increase in enzymatic activity of Pfu CelB is achieved with 300 W of microwave irradiation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3
2-nitrophenyl-beta-D-galactopyranoside
-
31
2-nitrophenyl-beta-D-galactopyranoside-6-phosphate
-
0.28
2-Nitrophenyl-beta-D-glucopyranoside
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
49
2-nitrophenyl beta-1,4-D-galactopyranoside 6-phosphate
-
2050
2-nitrophenyl-beta-D-galactopyranoside
-
860
2-Nitrophenyl-beta-D-glucopyranoside
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3700
2-nitrophenyl beta-D-galactopyranoside
-
pH 5.4, 75°C
12900
2-nitrophenyl beta-D-glucopyranoside
-
pH 5.4, 75°C
1000
4-nitrophenyl beta-D-galactopyranoside
-
pH 5.4, 75°C
7100
4-nitrophenyl beta-D-glucopyranoside
-
pH 5.4, 75°C
0.03 - 0.14
4-nitrophenyl beta-D-glucoside
4480
daidzin
-
pH 6.0, 95°C
12100
genistin
-
pH 6.0, 95°C
1840
glycitin
-
pH 6.0, 95°C
303
isoquercitrin
-
pH 5.0, 95°C
2.33
quercitrin
-
pH 5.0, 95°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
pH 5.5, 95°C, substrate: ginsenoside Rg2
0.06
pH 5.5, 95°C, substrate: ginsenoside R2
0.23
pH 5.5, 95°C, substrate: ginsenoside Re
0.6
pH 5.5, 95°C, substrate: 4-nitrophenyl-alpha-L-rhamnopyranoside
0.69
pH 5.5, 95°C, substrate: ginsenoside R1
117
pH 5.5, 95°C, substrate: 4-nitrophenyl-beta-D-xylopyranoside
12.5
pH 5.5, 95°C, substrate: 2-nitrophenyl-beta-D-xylopyranoside
1300
pH 5.5, 95°C, substrate: 4-nitrophenyl-beta-D-glucopyranoside
6.8
pH 5.5, 95°C, substrate: ginsenoside Rf
694.6
pH and temperature not specified in the publication
828
pH 5.5, 95°C, substrate: 2-nitrophenyl-beta-D-glucopyranoside
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
for 2-nitrophenyl-beta-1,4-D-galactopyranoside-6-phosphate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
pH 5.0: about 60% of maximal activity, pH 7.0: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 90
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 110
70°C: about 45% of maximal activity, 110°C: about 30% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q51723_9EURY
472
0
54665
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
136000
mutant enzyme R170A/R220A/Y227F, dimer, gel filtration
23600
wild-type enzyme tetramer, gel filtration
50000
mutant enzyme R170A/R220A/Y227F/R459G, monomer, gel filtration
54600
deduced from amino acid composition
55000
2 * 55000, SDS-PAGE after heating at 95°C,mutant enzyme R170A/R220A/Y227F
71000
mutant enzyme R170A/R220A/Y227F/R448E, monomer, gel filtration
96000
mutant enzyme R170A/R220A/Y227F/R449R, monomer, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 55000, SDS-PAGE after heating at 95°C,mutant enzyme R170A/R220A/Y227F
monomer
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3.3 A resolution
mutant enzyme R170A/R220A/Y227F, hanging-drop vapour-diffusion method, the structure is determined at 2.35 A resolution, stable homotetrameric structure, a dimeric form of the enzyme is constructed and its crystal structure is solved at a resolution of 1.70 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E417S
mutant with reduced pH optimum, increased Km and turnover number for 2-nitrophenyl-beta-1,4-D-glucopyranoside
F426Y
mutant with unchanged pH optimum, slight increased Km and slight reduced turnover number for 2-nitrophenyl-beta-1,4-D-glucopyranoside
M424K
mutant with increased pH optimum, slight increased Km and reduced turnover number for 2-nitrophenyl-beta-1,4-D-galactopyranoside
R170A/R220A/Y227F
mutant enzyme occurs as dimer
R170A/R220A/Y227F/R448E
mutant enzyme occurs as monomer, melting temperature is decreased form 110°C for the wild-type enzyme to 73-75°C for the mutant enzyme
R170A/R220A/Y227F/R449R
mutant enzyme occurs as monomer, melting temperature is decreased form 110°C for the wild-type enzyme to 73-75°C for the mutant enzyme
R170A/R220A/Y227F/R459G
mutant enzyme occurs as monomer, melting temperature is decreased form 110°C for the wild-type enzyme to 73-75°C for the mutant enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
37°C, 1 h incubation, the enzyme retains more than 80% of its maximum activity
724664
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
half life: 85 h
102
Tm-value of mutant enzyme R170A/R220A/Y227F
110
melting temperature of tetrameric wild-type enzyme
122
melting point at 50 MPa in Tris buffer, pH 7.5
30 - 120
the enzyme retains more than 80% of its maximum activity from 30°C to 120°C
70 - 80
mutant enzymes R170A/R220A/Y227F/R448E, R170A/R220A/Y227F/R449R or R170A/R220A/Y227F/R459G are immediately inactivated
73 - 75
melting temperature of mutant enzymes R170A/R220A/Y227F/R448E, R170A/R220A/Y227F/R449R or R170A/R220A/Y227F/R459G
80
no thermal unfolding at 200 MPa and 400 MPa
90
enzyme immobilized on gelatin, completely stable for one month
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is highly piezostable and thermostable, with increased enzyme inactivation at 25°C and pressures from 100 to 300 MPa. At a constant pressure of 400 MPa, no enzyme inactivation occurrs. Enzyme has an unfolding pressure of 800 MPa at 85°C. Two-step inactivation process due to pressure, which is most pronounced at low temperatures. An increase in pH from 5.5 to 6.5 has a stabilizing effect
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity, recombinant enzyme
wild-type and mutant enzyme R170A/R220A/Y227F
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in frame with the Saccharomyces cerecisiae a-factor secretory signal and expressed in Pichia pastoris strain X-33
expressed in Escherichia coli BL21
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
immobilization of the enzyme on gelatin, overview, the very stable gelatin-immobilized enzyme can be used in continuous synthesis of beta-glucosides by transglucosylation
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bauer, M.W.; Bylina, E.J.; Swanson, R.V.; Kelly, R.M.
Comparison of a beta-glucosidase and a beta-mannosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Purification, characterization, gene cloning, and sequence analysis
J. Biol. Chem.
271
23749-23755
1996
Pyrococcus furiosus (Q51723), Pyrococcus furiosus
Manually annotated by BRENDA team
Kaper, T.; Lebbink, J.H.G.; Pouwels, J.; Kopp, J.; Schulz, G.E.; van der Oost, J.; de Vos, W.M.
Comparative structural analysis and substrate specificity engineering of the hyperthermostable beta-glucosidase CelB from Pyrococcus furiosus
Biochemistry
39
4963-4970
2000
Pyrococcus furiosus (Q51723), Pyrococcus furiosus
Manually annotated by BRENDA team
Nagatomo, H.; Matsushita, Y.; Sugamoto, K.; Matsui, T.
Preparation and properties of gelatin-immobilized beta-glucosidase from Pyrococcus furiosus
Biosci. Biotechnol. Biochem.
69
128-136
2005
Pyrococcus furiosus (Q51723), Pyrococcus furiosus
Manually annotated by BRENDA team
Bruins, M.E.; Meersman, F.; Janssen, A.E.; Heremans, K.; Boom, R.M.
Increased susceptibility of beta-glucosidase from the hyperthermophile Pyrococcus furiosus to thermal inactivation at higher pressures
FEBS J.
276
109-117
2009
Pyrococcus furiosus (Q51723), Pyrococcus furiosus
Manually annotated by BRENDA team
Nakabayashi, M.; Kataoka, M.; Mishima, Y.; Maeno, Y.; Ishikawa, K.
Structural analysis of beta-glucosidase mutants derived from a hyperthermophilic tetrameric structure
Acta Crystallogr. Sect. D
70
877-888
2014
Pyrococcus furiosus (Q51723), Pyrococcus furiosus
Manually annotated by BRENDA team
Oh, H.J.; Shin, K.C.; Oh, D.K.
Production of ginsenosides Rg1 and Rh1 by hydrolyzing the outer glycoside at the C-6 position in protopanaxatriol-type ginsenosides using beta-glucosidase from Pyrococcus furiosus
Biotechnol. Lett.
36
113-119
2013
Pyrococcus furiosus (Q51723)
Manually annotated by BRENDA team
Li, B.; Wang, Z.; Li, S.; Donelan, W.; Wang, X.; Cui, T.; Tang, D.
Preparation of lactose-free pasteurized milk with a recombinant thermostable beta-glucosidase from Pyrococcus furiosus
BMC Biotechnol.
13
73
2013
Pyrococcus furiosus (Q51723), Pyrococcus furiosus
Manually annotated by BRENDA team
Young, D.D.; Nichols. J.; Kelly, R.M.; Deiters, A.
Microwave activation of enzymatic catalysis
J. Am. Chem. Soc.
130
10048-10049
2008
Prunus dulcis, Pyrococcus furiosus (Q51723)
Manually annotated by BRENDA team