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Information on EC 3.2.1.21 - beta-glucosidase and Organism(s) Homo sapiens and UniProt Accession Q9H227
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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.
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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: Homo sapiens
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 1
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
the two catalytic glutamate residues are located on strand 4, the acid/base Glu165, and on strand 7,the nucleophile Glu373
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
double replacement mechanism, retaining the configuration. A water molecule may be involved in the stabilization of transition states through a sugar 2-hydroxyl oxygen
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
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-L-arabinopyranoside + H2O
4-nitrophenol + beta-L-arabinopyranose
-
-
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
-
-
-
?
apigenin-7-O-beta-D-glucoside + H2O
apigenin + beta-D-glucose
high activity
-
-
?
quercetin 4'-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
best substrate, homology modelling revealed that hydrophobic interactions dominate the binding of the aglycone moiety, Val168, Trp345, Phe225, Phe179, Phe334 and Phe433 are especially important in determining substrate specificity
-
-
?
quercetin 7-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
high activity
-
-
?
17beta-estradiol 17-beta-D-glucoside + H2O
beta-D-glucose + 17beta-estradiol
-
-
-
?
17beta-estradiol-3'-beta-D-glucoside + H2O
beta-D-glucose + 17beta-estradiol
-
poor activity
-
?
2,4-dinitrophenyl-beta-D-galactoside + H2O
2,4-dinitrophenol + beta-D-galactose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl-alpha-L-arabinoside + H2O
2-nitrophenol + alpha-L-arabinose
-
very low activity
-
?
4-methylumbelliferyl alpha-L-arabinoside + H2O
4-methylumbelliferone + alpha-L-arabinose
-
-
-
-
?
4-methylumbelliferyl beta-D-fucoside + H2O
4-methylumbelliferone + beta-D-fucose
-
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-arabinopyranoside + H2O
4-methylumbelliferone + beta-D-arabinopyranose
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
daidzein 7-O-(6-O-malonyl-beta-D-glucoside) + H2O
daidzein + 6-O-malonyl-beta-D-glucopyranose
-
-
-
-
?
eriodicytol-7-beta-D-glucopyranoside + H2O
eriodicytol + beta-D-glucose
-
-
-
-
?
estrone-3-beta-D-glucoside + H2O
beta-D-glucose + estrone
-
poor activity
-
?
glucosyl ceramide + H2O
sphingosine + fatty acid + beta-D-glucose
-
involved in normal catabolism of glucosyl ceramides
-
?
luteolin-3',7-dibeta-D-glucopyranoside + H2O
luteolin + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-L-arabinopyranoside + H2O
p-nitrophenol + alpha-L-arabinose
-
-
-
-
?
p-nitrophenyl-beta-D-arabinopyranoside + H2O
p-nitrophenol + beta-D-arabinose
-
-
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucose
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactose
-
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
-
-
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylose
-
-
-
-
?
p-nitrophenyl-beta-L-arabinopyranoside + H2O
p-nitrophenol + beta-L-arabinose
-
-
-
-
?
phenylethyl-beta-D-galactoside + H2O
phenylethanol + beta-D-galactose
-
very poor substrate
-
?
quercetin 3,4'-O-di-beta-D-glucopyranoside + H2O
quercetin + 2 beta-D-glucose
-
-
-
-
?
quercetin 4'-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
-
-
-
-
?
quercetin 7-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
-
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
4-methylumbelliferone + beta-D-galactopyranose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
-
presence of sphingolipid binding site, possible role in glycosphingolipid metabolism
-
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
-
-
-
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
additional information
?
-
the human cytosolic beta-glucosidase is a xenobiotic-metabolizing enzyme that hydrolyses certain flavonoid glucosides, with specificity depending on the aglycone moiety, the type of sugar and the linkage between them, substrate specificity, overview
-
-
?
additional information
?
-
-
the human cytosolic beta-glucosidase is a xenobiotic-metabolizing enzyme that hydrolyses certain flavonoid glucosides, with specificity depending on the aglycone moiety, the type of sugar and the linkage between them, substrate specificity, overview
-
-
?
additional information
?
-
-
enzyme deficiency causes the Gaucher's disease, the enzyme participates in degradation of glycosphingolipids
-
-
?
additional information
?
-
-
enzyme deficiency causes the Gaucher's disease, the enzyme participates in degradation of glycosphingolipids
-
-
?
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
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
cellobiose
-
?
eriodicytol-7-beta-D-glucopyranoside + H2O
eriodicytol + beta-D-glucose
-
-
-
-
?
glucosyl ceramide + H2O
sphingosine + fatty acid + beta-D-glucose
-
involved in normal catabolism of glucosyl ceramides
-
?
quercetin 4'-O-beta-D-glucopyranoside + H2O
quercetin + beta-D-glucose
-
-
-
-
?
additional information
?
-
-
enzyme deficiency causes the Gaucher's disease, the enzyme participates in degradation of glycosphingolipids
-
-
?
additional information
?
-
-
enzyme deficiency causes the Gaucher's disease, the enzyme participates in degradation of glycosphingolipids
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-dinitrophenyl-2-fluoro-2-deoxy-beta-D-glucopyranoside
-
0.001 mM, 64% inhibition after 30 min incubation
N-Bromoacetyl-beta-D-galactosylamine
-
inhibition of the glucosidase- and galactosidase-activities only above pH 8.0
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Gaucher spleen heat-stable factor
-
15fold increase for hydrolysis of 17beta-estradiol-17'-beta-D-glucoside
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
4-nitrophenyl-alpha-L-arabino-pyranoside
recombinant wild-type enzyme
2.97
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant N370S/L444P, Gaucher's disease patient
3.64
4-methylumbelliferyl beta-D-glucoside
-
pH 5.4, 37°C, Gaucher's disease enzyme from leukocytes
4.13
4-methylumbelliferyl beta-D-glucoside
-
pH 5.4, 37°C, healthy human enzyme from leukocytes
6.18
4-methylumbelliferyl beta-D-glucoside
-
pH 5.4, 37°C, healthy human enzyme from fibroblasts
7.18
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant N370S, heterozygote
12.37
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant N370S/N370S, Gaucher's disease patient
12.4
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant L444P, heterozygote
18.43
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant N370S and deletion mutation, Gaucher's disease patient
37.2
4-methylumbelliferyl beta-D-glucoside
-
pH 5.5, 37°C, mutant D409H, heterozygote
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.88
4-nitrophenyl-alpha-L-arabino-pyranoside
recombinant wild-type enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000055
7-(N-benzoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.0014
7-(N-benzoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.02
7-(N-benzoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.0003
7-(N-butylsulfonyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.0003
7-(N-butylsulfonyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.0025
7-(N-butylsulfonyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.00007
7-(N-pentoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.0002
7-(N-pentoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.0005
7-(N-pentoyl)-cyclophellitol aziridine
Homo sapiens
-
isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.000017
7-pentylcyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.0007
7-pentylcyclophellitol aziridine
Homo sapiens
-
isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.0007
7-pentylcyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.00035
cyclophellitol
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.002
cyclophellitol
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.1
cyclophellitol
Homo sapiens
-
IC50 above 0.1 mM, isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.0004
cyclophellitol aziridine
Homo sapiens
-
isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
0.0005
cyclophellitol aziridine
Homo sapiens
-
isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.1
cyclophellitol aziridine
Homo sapiens
-
IC50 above 0.1 mM, isoform GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.1
cyclophellitol thiirane
Homo sapiens
-
IC50 above 0.1 mM, GBA3, in 150 mM McIlvaine buffer, pH 6.0, at 37°C
0.1
cyclophellitol thiirane
Homo sapiens
-
IC50 above 0.1 mM, isoform GBA, in 150 mM McIlvaine buffer, pH 5.2, at 37°C
0.1
cyclophellitol thiirane
Homo sapiens
-
IC50 above 0.1 mM, isoform GBA2, in 150 mM McIlvaine buffer, pH 5.8, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.1
purified enzyme, substrate 4-nitrophenyl-alpha-L-arabinoopyranoside, recombinant wild-type enzyme
3.5
purified enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside, recombinant wild-type enzyme
3.6
purified enzyme, substrate 4-nitrophenyl-beta-D-fucopyranoside, recombinant wild-type enzyme
41.8
purified enzyme, substrate apigenin-7-glucoside, recombinant wild-type enzyme
49.7
purified enzyme, substrate quercetin-4'-glucoside, recombinant wild-type enzyme
5.7
purified enzyme, substrate 4-nitrophenyl-beta-D-galactopyranoside, recombinant wild-type enzyme
additional information
additional information
substrate specificity of wild-type and mutant enzymes, overview
additional information
-
substrate specificity of wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). GBA3_HUMAN
469
0
53696
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53000
55000
-
1 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 1 * 57346, mass spectrometry
57346
-
1 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 1 * 57346, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
-
1 * 55000, recombinant His-tagged enzyme, SDS-PAGE, 1 * 57346, mass spectrometry
additional information
the main-chain fold of the enzyme belongs to the (beta/alpha)8 barrel structure, the active site is located at the bottom of a pocket formed by large surface loops, surrounding the C termini of the barrel of beta-strands
additional information
-
the main-chain fold of the enzyme belongs to the (beta/alpha)8 barrel structure, the active site is located at the bottom of a pocket formed by large surface loops, surrounding the C termini of the barrel of beta-strands
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
covalent intermediate of mutant E165P, in which glucose is bound to nucleophile E373. Structure confirms a double displacement mechanism
purified wild-type enzyme, 0.002 ml of protein solution containing 4 mg/ml protein in 20 mM MES, pH 6.0, are mixed with 0.001 ml of reservoir solution containing 0.2 M ammonium sulphate, MES buffer, pH 6.5, and 30% w/v polyethyleneglycol-monomethylether 5500, 20°C, several days, X-ray diffraction structure determination and anaylsis at 2.7 A resolution, molecular replacement method, modeling
purified recombinnat enzyme, hanging drop vapour diffusion method, micro-seeding, the protein crystallized in 1.6 M ammonium sulfate, 100 mM HEPES, pH 7.0, within 4 weeks, X-ray diffraction structure determination and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E165P
crystallization data of covalent intermediate with substrate, in which glucose is bound to nucleophile E373
M172L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, and altered substrate specificity
Q307N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, and altered substrate specificity
W345M
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, and altered substrate specificity
D409H
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, obligated GD heterozygotes
F225S
-
0.65% of wild-type specific activity with p-nitrophenyl-beta-D-glucopyranoside
L444P
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, obligated GD heterozygotes
N370S
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, obligated GD heterozygotes, and homozygote GD patients
N370S/D409H
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, homozygote GD patients
N370S/L444P
-
naturally occurring mutation involved in Gaucher's disease development with reduced enzyme activity, homozygote GD patients
V168Y
-
12% of wild-type specific activity with p-nitrophenyl-beta-D-glucopyranoside
Y308A
-
0.3% of wild-type specific activity with p-nitrophenyl-beta-D-glucopyranoside
Y308F
-
6% of wild-type specific activity with p-nitrophenyl-beta-D-glucopyranoside
additional information
-
naturally occurring deletion mutantions involved in Gaucher's disease development with reduced enzyme activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
60
50
-
half-life: 22-24 min, 2fold enhanced stability of Gaucher disease liver enzyme compared to control liver
60
-
half-life of the healthy leukocyte enzyme is 3.5 min, of the healthy fibroblast 3 min, and half-life of the Gaucher's disease enzyme from leukocyte is about 6 min, and from fibroblast 3 min, thermostability, overview
60
-
heat stability of wild-type and mutant enzymes at 60°C, overview, the wild-type enzyme is inactivated within 1 min, homozygote mutants are inactive after 2 min, heterozygotes after 2-4 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 12fold in a two-step process involving hydrophobic interaction chromatography, with an additional anion exchange chromatography step
native CBG, cation-exchange chromatography, Octyl-Sepharose, chromatofocusing, gel filtration, recombinant CBG, Octyl-Sepharose
-
recombinant N-terminally His6-tagged cytosolic isozyme from Sf9 insect cells by nickel affinity and ion exchange chromatography to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of N-terminally His6-tagged cytosolic isozyme in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
LaMarco, K.L.; Glew, R.H.
Galactosylsphingosine inhibition of the broad-specificity cytosolic beta-glucosidase of human liver
Arch. Biochem. Biophys.
236
669-676
1985
Homo sapiens
Maret, A.; Salvayre, R.; Negre, A.; Douste-Blazy, L.
Substrate specificity of the human splenic non-specific soluble beta-glucosidase
Eur. J. Biochem.
133
283-287
1983
Homo sapiens
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
-
Daniels, L.B.; Coyle, P.J.; Chiao, Y.B.; Glew, R.H.
Purification and characterization of a cytosolic broad specificity beta-glucosidase from human liver
J. Biol. Chem.
256
13004-13013
1981
Homo sapiens
Meisler, M.H.
Inhibition of human liver beta-galactosidases and beta-glucosidase by N-bromoacetyl-beta-D-galactosylamine
Biochim. Biophys. Acta
410
347-353
1975
Homo sapiens
Berrin, J.G.; Czjzek, M.; Kroon, P.A.; McLauchlan, W.R.; Puigserver, A.; Williamson, G.; Juge, N.
Substrate (aglycone) specificity of human cytosolic beta-glucosidase
Biochem. J.
373
41-48
2003
Homo sapiens
Berrin, J.G.; McLauchlan, W.R.; Needs, P.; Williamson, G.; Puigserver, A.; Kroon, P.A.; Juge, N.
Functional expression of human liver cytosolic beta-glucosidase in Pichia pastoris. Insights into its role in the metabolism of dietary glucosides
Eur. J. Biochem.
269
249-258
2002
Homo sapiens
Michelin, K.; Wajner, A.; Goulart, L.d.S.; Fachel, A.A.; Pereira, M.L.; de Mello, A.S.; Souza, F.T.; Pires, R.F.; Giugliani, R.; Coelho, J.C.
Biochemical study on beta-glucosidase in individuals with Gaucher's disease and normal subjects
Clin. Chim. Acta
343
145-153
2004
Homo sapiens
Michelin, K.; Wajner, A.; Bock, H.; Fachel, A.; Rosenberg, R.; Pires, R.F.; Pereira, M.L.; Giugliani, R.; Coelho, J.C.
Biochemical properties of beta-glucosidase in leukocytes from patients and obligated heterozygotes for Gaucher disease carriers
Clin. Chim. Acta
362
101-109
2005
Homo sapiens
Tribolo, S.; Berrin, J.G.; Kroon, P.A.; Czjzek, M.; Juge, N.
The crystal structure of human cytosolic beta-glucosidase unravels the substrate aglycone specificity of a family 1 glycoside hydrolase
J. Mol. Biol.
370
964-975
2007
Homo sapiens (Q9H227), Homo sapiens
Fleury, D.; Domaingue, P.; Gillard, C.; Touitou, R.; Mollat, P.
Expression, purification, characterization and crystallization of a recombinant human cytosolic beta-glucosidase produced in insect cells
Protein Expr. Purif.
52
96-103
2007
Homo sapiens
Noguchi, J.; Hayashi, Y.; Baba, Y.; Okino, N.; Kimura, M.; Ito, M.; Kakuta, Y.
Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase
Biochem. Biophys. Res. Commun.
374
549-552
2008
Homo sapiens (Q9H227), Homo sapiens
Li, K.Y.; Jiang, J.; Witte, M.D.; Kallemeijn, W.W.; Donker-Koopman, W.E.; Boot, R.G.; Aerts, J.M.; Codee, J.D.; van der Marel, G.A.; Overkleeft, H.S.
Exploring functional cyclophellitol analogues as human retaining beta-glucosidase inhibitors
Org. Biomol. Chem.
12
7786-7791
2014
Homo sapiens
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