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Information on EC 3.2.1.21 - beta-glucosidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9C8Y9

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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:
Arabidopsis thaliana
UNIPROT: Q9C8Y9
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
beta-glucosidase
-
amygdalase
-
-
-
-
amygdalinase
-
-
-
-
arbutinase
-
-
-
-
aryl-beta-glucosidase
-
-
-
-
beta-1,6-glucosidase
-
-
-
-
beta-D-glucosidase
-
-
-
-
beta-D-glucoside glucohydrolase
beta-glucosidase
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
4-MU-glucoside + H2O
?
show the reaction diagram
-
-
-
?
esculin + H2O
?
show the reaction diagram
-
-
-
?
scopolin + H2O
scopoletin + D-glucose
show the reaction diagram
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
show the reaction diagram
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferol + beta-D-glucopyranose
show the reaction diagram
163% relative activity
-
-
?
4-MU-glucoside + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
amygdalin + H2O
prunasin + D-glucose
show the reaction diagram
48% relative activity
-
-
?
beta-gentiobiose + H2O
?
show the reaction diagram
6.3% relative activity
-
-
?
D(+)cellobiose + H2O
?
show the reaction diagram
6.3% relative activity
-
-
?
DIMBOA-glucoside + H2O
?
show the reaction diagram
-
-
-
?
esculin + H2O
?
show the reaction diagram
-
-
-
?
n-decyl-beta-D-glucopyranoside + H2O
n-decanol + beta-D-glucopyranose
show the reaction diagram
11% relative activity
-
-
?
n-heptyl-beta-D-glucopyranoside + H2O
n-heptanol + beta-D-glucopyranose
show the reaction diagram
17% relative activity
-
-
?
n-octyl-beta-D-glucopyranoside + H2O
n-octanol + beta-D-glucopyranose
show the reaction diagram
7% relative activity
-
-
?
o-nitrophenyl-beta-D-fucopyranoside + H2O
o-nitrophenol + beta-D-fucopyranose
show the reaction diagram
117% relative activity
-
-
?
o-nitrophenyl-beta-D-galactopyranoside + H2O
o-nitrophenol + beta-D-galactopyranose
show the reaction diagram
17% relative activity
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucopyranose
show the reaction diagram
71% relative activity
-
-
?
prunasin + H2O
D-mandelonitrile + beta-D-glucose
show the reaction diagram
39% relative activity
-
-
?
salicin + H2O
?
show the reaction diagram
4.4% relative activity
-
-
?
scopolin + H2O
scopoletin + beta-D-glucose
show the reaction diagram
-
-
-
?
scopolin + H2O
scopoletin + 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
scopolin + H2O
scopoletin + D-glucose
show the reaction diagram
-
-
-
?
scopolin + H2O
scopoletin + beta-D-glucose
show the reaction diagram
-
-
-
?
scopolin + H2O
scopoletin + D-glucose
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
gluconolactone
competitively inhibits with p-nitrophenyl-beta-D-glucopyranoside, o-nitrophenyl-beta-D-glucopyranoside, and 4-methylumbelliferyl-beta-D-glucopyranoside as substrates
jacalin-related lectin
-
isoform Pyk10 is localized in ER bodies and has beta-D-glucosidase and beta-D-fucosidase activities. Jacalin-related lectins regulate the size of the active Pyk10 complexes, with two types of lectins working antagonistically
-
p-nitrophenyl-1-thio-beta-D-glucopyranoside
competitively inhibits with p-nitrophenyl-beta-D-glucopyranoside, o-nitrophenyl-beta-D-glucopyranoside, and 4-methylumbelliferyl-beta-D-glucopyranoside as substrates
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
protein PBPI
binding protein, interacts with beta-glucosidases and activates them
-
protein PBPII
binding protein, interacts with beta-glucosidases and activates them
-
jacalin-related lectin
-
isoform Pyk10 is localized in ER bodies and has beta-D-glucosidase and beta-D-fucosidase activities. Jacalin-related lectins regulate the size of the active Pyk10 complexes, with two types of lectins working antagonistically
-
protein PBPI
binding protein, interacts with beta-glucosidases and activates them
-
protein PBPII
binding protein, interacts with beta-glucosidases and activates them
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.8 - 9.7
esculin
0.73 - 0.81
scopolin
0.78
4-methylumbelliferyl-beta-D-glucopyranoside
-
5.8 - 9.7
esculin
2.1
o-nitrophenyl-beta-D-glucopyranoside
-
1.9
p-nitrophenyl-beta-D-glucopyranoside
-
0.73 - 0.81
scopolin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 4.7
gluconolactone
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.9
-
crude extract, at pH 5.5 and 50°C
148.5
-
after 164.5fold purification, at pH 5.5 and 50°C
20.34
21fold purified recombinant beta-glucosidase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
recombinant mutated beta-glucosidase
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
mutated recombinant beta-glucosidase
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoform Pyk10 is localized in ER bodies and has beta-D-glucosidase and beta-D-fucosidase activities. Jacalin-related lectins regulate the size of the active Pyk10 complexes, with two types of lectins working antagonistically
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BGL22_ARATH
524
0
59781
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59800
BGLU 22, calculated from seuqence
63000
SDS-PAGE, recombinant glycosylated protein
58000
-
SDS-PAGE
59700
60000
x * 60000, SDS-PAGE, recombinant mutated beta-glucosidase
63000
SDS-PAGE, recombinant glycosylated protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 60000, SDS-PAGE, recombinant mutated beta-glucosidase
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
mutated recombinant beta-glucosidase is fairly stable at pH 5.0 and 8.5, exhibiting 60 and 62% activities, respectively. It retains over 50% of the original activity between pH 4-7.5. Between pH values 6.0 and 7.2, it retains over 98% activity after incubation at 37°C for 2 h
696166
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
dramatical decrease of activity above 50°C
42
is fairly stable in 50 mM sodium acetate buffer, pH 5.6, at temperatures up to 42°C, while retaining only 48% of the original activity at 50°C for 10 min. It is completely inactivated upon incubation at 60°C for 10 min
50
dramatical decrease of activity above 50°C
60 - 90
-
about 50% activity at 60°C, about 30% activity at 70°C, about 10% activity at 80°C, no activity at 90°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Concanavalin A-Sepharose column chromatography, Shodex-phenyl HIC-814 column chromatography, and Sephacryl S-200 gel filtration
-
recombinant beta-glucosidase purified by gel filtration to apparent homogeneity, 21fold with an overall enzyme yield of 6.8%
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA is expressed in insect cells, Baculovirus expression system
cDNA expressed in insect cells, Baculovirus expression system
cDNA is expressed in insect cells, Baculovirus expression system
native and mutated cDNA sequences cloned into vector pPICZalphaB and expressed in Pichia pastoris
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
BGLU22 by cold and mannitol
BGLU22 by NaCl, 2,4-dichlorophenoxyacetate and methyl jasmonate
BGLU21 by cold, 2,4-dichlorophenoxyacetate and methyl jasmonate
BGLU23 by 2,4-dichlorophenoxyacetate and methyl jasmonate
BGLU23 by NaCl and mannitol
senescence-induced loss in photosynthesis enhances cell wall beta-glucosidase activity
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Turan, Y.
A pseudo-beta-glucosidase in Arabidopsis thaliana: correction by site-directed mutagenesis, heterologous expression, purification, and characterization
Biochemistry (Moscow)
73
912-919
2008
Arabidopsis thaliana (Q9SLA0), Arabidopsis thaliana
Manually annotated by BRENDA team
Nagano, A.J.; Fukao, Y.; Fujiwara, M.; Nishimura, M.; Hara-Nishimura, I.
Antagonistic jacalin-related lectins regulate the size of ER body-type beta-glucosidase complexes in Arabidopsis thaliana
Plant Cell Physiol.
49
969-980
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Sherameti, I.; Venus, Y.; Drzewiecki, C.; Tripathi, S.; Dan, V.M.; Nitz, I.; Varma, A.; Grundler, F.M.; Oelmueller, R.
PYK10, a beta-glucosidase located in the endoplasmatic reticulum, is crucial for the beneficial interaction between Arabidopsis thaliana and the endophytic fungus Piriformospora indica
Plant J.
54
428-439
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Mohapatra, P.K.; Patro, L.; Raval, M.K.; Ramaswamy, N.K.; Biswal, U.C.; Biswal, B.
Senescence-induced loss in photosynthesis enhances cell wall beta-glucosidase activity
Physiol. Plant.
138
346-355
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Ahn, Y.O.; Shimizu, B.; Sakata, K.; Gantulga, D.; Zhou, C.; Zhou, Z.; Bevan, D.R.; Esen, A.
Scopolin-hydrolyzing beta-glucosidases in roots of Arabidopsis
Plant Cell Physiol.
51
132-43
2010
Arabidopsis thaliana (Q9C525), Arabidopsis thaliana (Q9C8Y9), Arabidopsis thaliana (Q9SR37)
Manually annotated by BRENDA team