Any feedback?
Information on EC 3.2.1.21 - beta-glucosidase and Organism(s) Aspergillus oryzae and UniProt Accession Q2UUD6
for references in articles please use BRENDA:EC3.2.1.21Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.21 beta-glucosidaseIUBMB 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
Word Map
- 3.2.1.21
- cellobiose
- cellulase
- beta-galactosidase
- glycoside
- lysosomal
- alpha-glucosidase
- gaucher
- trichoderma
- aglycone
- endoglucanase
- glycosidases
-
cellulolytic
- almond
- xylanase
- reesei
- beta-xylosidase
-
saccharification
- alpha-mannosidase
- p-nitrophenyl
- alpha-galactosidase
-
lignocellulosic
- urease
- cellobiohydrolase
- avicel
-
cellulosic
- straw
- glucosylceramide
- cassava
- beta-n-acetylglucosaminidase
- xylan
- beta-d-glucopyranoside
- cmcase
- hemicellulose
-
microcrystalline
- beta-mannosidase
- arylamidase
- arbutin
- cellulomonas
-
transglucosylation
- stover
- alpha-l-fucosidase
- alpha-l-arabinofuranosidase
- cellotetraose
- bagasse
- azoreductase
- carboxymethylcellulase
- endo-beta-1,4-glucanase
- cellodextrins
- glucocerebroside
-
xylanolytic
- industry
- biofuel production
- medicine
- nutrition
- degradation
- analysis
- synthesis
- food industry
- molecular biology
- biotechnology
The taxonomic range for the selected organisms is: Aspergillus oryzae
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
-
-
-
-
additional information
-
the enzyme belongs to the glycosyl hydrolase family 3
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
W293 of the SDW segment, which is the residue next to the nucleophile D292 in family 3 BGL, is very important for hydrolytic reaction as a binder to a substrate. G294 of the SDWG sequence might play an important role in catalysis, interaction between the sugar rings and aromatic ring of W293 at the entrance of the catalytic pocket enhances the substrate recognition of beta-glucosidase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -
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
9001-22-3
-
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
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellotrioside + H2O
4-nitrophenol + D-cellotriose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
-
-
-
?
3-O-alpha-D-glucopyranosyl-D-glucose + H2O
alpha-D-glucose + D-glucose
-
nigerose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
4-nitrophenyl beta-D-cellobioside + 2 H2O
4-nitrophenol + 2 beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
low activity
-
?
4-nitrophenyl beta-L-arabinopyranoside + H2O
4-nitrophenol + beta-L-arabinopyranose
-
low activity
-
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
maltose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-xylopyranosyl-D-xylose + H2O
beta-D-xylose + D-xylose
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucose + H2O
alpha-D-glucose + D-glucose
-
isomaltose
-
?
daidzein 7-O-(6-O-acetyl-beta-D-glucoside) + H2O
daidzein + 6-O-acetyl-beta-D-glucose
-
-
-
?
daidzein-7-O-beta-D-glucopyranoside + H2O
daidzein + beta-D-glucose
-
-
-
?
genistein-7-O-beta-D-glucopyranoside + H2O
genistein + beta-D-glucose
-
-
-
?
genistein-7-O-beta-D-glucosyl-6''-O-acetate + H2O
genistein + 6-O-acetyl-beta-D-glucose
-
-
-
?
glycitein-7-O-beta-D-glucopyranoside + H2O
glycitein + beta-D-glucose
-
-
-
?
glycitein-7-O-beta-D-glucosyl-6''-O-acetate + H2O
glycitein + 6-O-acetyl-beta-D-glucose
-
-
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
high activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
less active than on cellobiose
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
low activity
-
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
cellobiose + H2O
2 beta-D-glucose
-
interaction between the sugar rings and aromatic ring of W293 at the entrance of the catalytic pocket enhances the substrate recognition of beta-glucosidase
-
-
?
piceid + H2O
resveratrol + beta-D-glucose
-
specific for, high activity
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl-alpha-L-arabinoside and 4-nitrophenyl-alpha-L-rhamnoside
-
-
?
additional information
?
-
low substrate specificity for isoflavones
-
-
?
additional information
?
-
low substrate specificity for isoflavones
-
-
?
additional information
?
-
-
low substrate specificity for isoflavones
-
-
?
NATURAL SUBSTRATE
NATURAL 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
3-O-alpha-D-glucopyranosyl-D-glucose + H2O
alpha-D-glucose + D-glucose
-
nigerose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
4-O-alpha-D-glucopyranosyl-D-glucose
alpha-D-glucose + D-glucose
-
maltose
-
?
4-O-beta-D-galactopyranosyl-D-glucose + H2O
beta-D-galactose + D-glucose
-
lactose
-
?
4-O-beta-D-xylopyranosyl-D-xylose + H2O
beta-D-xylose + D-xylose
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucose + H2O
alpha-D-glucose + D-glucose
-
isomaltose
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
2-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
sophorose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no effect on piceid-beta-D-glucosidase by Ca2+, Mg2+, and Zn2+ ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
330
D-glucoheptose
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
130
D-glucuronamide
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
0.004
deoxynojirimycin
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
0.07
gluconolactone
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
440
myo-inositol
-
pH 5.0, 40°C, versus 4-nitrophenyl beta-D-glucopyranoside
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
176
-
purified enzyme, substrate 4-nitrophenyl beta-D-glucopyranoside, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
most effective induction of enzyme synthesis in medium containing quercetin
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G294A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294C
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294D
-
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
G294E
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294F
-
site-directed mutagenesis, the mutant shows 1.5fold higher activities for substrate recognition than the wild-type enzyme
G294H
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294I
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294K
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294L
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294M
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294N
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294P
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G294Q
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294R
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G294S
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G294T
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294V
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
G294W
-
site-directed mutagenesis, the mutant shows 1.5fold higher activities for substrate recognition than the wild-type enzyme
G294Y
-
site-directed mutagenesis, the mutant shows 1.6fold higher activities for substrate recognition than the wild-type enzyme
additional information
additional information
co-expression of beta-glucosidase and endoglucanase in Saccharomyces cerevisiae. Ethanol fermentation from 20 g per l barley beta-glucan with the co-displaying strain reaches 7.94 g per l ethanol after 24 h of fermentation. The conversion rate of ethanol is 69.6% of the theoretical ethanol concentration
additional information
-
co-expression of beta-glucosidase and endoglucanase in Saccharomyces cerevisiae. Ethanol fermentation from 20 g per l barley beta-glucan with the co-displaying strain reaches 7.94 g per l ethanol after 24 h of fermentation. The conversion rate of ethanol is 69.6% of the theoretical ethanol concentration
additional information
-
rapid construction of a library of mutant BGL1 from Aspergillus oryzae by yeast cell surface engineering
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
70
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native piceid-beta-D-glucosidase 12.6fold by ammonium sulfate fractionation, anion exchange chromatography, and freeze drying
-
purified 138.85fold by ammonium sulfate precipitation, DE-22 ion exchange and Sephadex G-150 gel filtration chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as fusion protein with alpha-agglutinin on surface of Saccharomyces cerevisiae cells
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha, display of the enzyme on the cell surface of Saccharomyces cerevisiae
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
co-expression of beta-glucosidase and endoglucanase in Saccharomyces cerevisiae. Ethanol fermentation from 20 g per l barley beta-glucan with the co-displaying strain reaches 7.94 g per l ethanol after 24 h of fermentation. The conversion rate of ethanol is 69.6% of the theoretical ethanol concentration
biotechnology
production of isoflavone aglycones by the enzyme. Isoform BGL1 shows broad substrate specificity to various isoflavone glycosides, the residual ratio is reached to 6.2% of the total amount of isoflavone glycosides and the hydrolysis reaction is almost finished within 48 h
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Riou, C.; Salmon, J.P.; Vallier, M.J.; Gunata, Z.; Barre, P.
Purification, characterization, and substrate specificity of a novel highly glucose-tolerant beta-glucosidase from Aspergillus oryzae
Appl. Environ. Microbiol.
64
3607-3614
1998
Aspergillus oryzae
Wiseman, A.
Fungal and other beta-D-glucosidases - their properties and applications
Enzyme Microb. Technol.
4
73-78
1982
Aspergillus niger, Aspergillus oryzae, Aspergillus wentii, Saccharomyces cerevisiae, Acetivibrio thermocellus, Pantoea agglomerans, Homo sapiens, Malus domestica, Rhizomucor miehei, Pyrus communis, Prunus dulcis, Trichoderma reesei
-
Langston, J.; Sheehy, N.; Xu, F.
Substrate specificity of Aspergillus oryzae family 3 beta-glucosidase
Biochim. Biophys. Acta
1764
972-978
2006
Aspergillus oryzae, Aspergillus oryzae GH3
Fukuda, T.; Kato-Murai, M.; Kadonosono, T.; Sahara, H.; Hata, Y.; Suye, S.; Ueda, M.
Enhancement of substrate recognition ability by combinatorial mutation of beta-glucosidase displayed on the yeast cell surface
Appl. Microbiol. Biotechnol.
76
1027-1033
2007
Aspergillus oryzae
Zhang, C.; Li, D.; Yu, H.; Zhang, B.; Jin, F.
Purification and characterization of piceid-beta-D-glucosidase from Aspergillus oryzae
Process Biochem.
42
83-88
2007
Aspergillus oryzae, Aspergillus oryzae FFCDL-100
-
Kaya, M.; Ito, J.; Kotaka, A.; Matsumura, K.; Bando, H.; Sahara, H.; Ogino, C.; Shibasaki, S.; Kuroda, K.; Ueda, M.; Kondo, A.; Hata, Y.
Isoflavone aglycones production from isoflavone glycosides by display of beta-glucosidase from Aspergillus oryzae on yeast cell surface
Appl. Microbiol. Biotechnol.
79
51-60
2008
Aspergillus oryzae (Q2UIR4), Aspergillus oryzae (Q2UL94), Aspergillus oryzae
Kotaka, A.; Bando, H.; Kaya, M.; Kato-Murai, M.; Kuroda, K.; Sahara, H.; Hata, Y.; Kondo, A.; Ueda, M.
Direct ethanol production from barley beta-glucan by sake yeast displaying Aspergillus oryzae beta-glucosidase and endoglucanase
J. Biosci. Bioeng.
105
622-627
2008
Aspergillus oryzae (Q2UUD6), Aspergillus oryzae
EXTERNAL LINKS (specific for EC-Number 3.2.1.21)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
