Information on EC 3.2.1.175 - beta-D-glucopyranosyl abscisate beta-glucosidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.175
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RECOMMENDED NAME
GeneOntology No.
beta-D-glucopyranosyl abscisate beta-glucosidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucopyranosyl abscisate + H2O = D-glucose + abscisate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
abscisic acid degradation by glucosylation
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Carotenoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
beta-D-glucopyranosyl abscisate glucohydrolase
The enzyme hydrolzes the biologically inactive beta-D-glucopyranosyl ester of abscisic acid to produce active abscisate. Abscisate is a phytohormone critical for plant growth, development and adaption to various stress conditions. The enzyme does not hydrolyse beta-D-glucopyranosyl zeatin [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Gerbel
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
abscisic acid is a phytohormone critical for plant growth. Dehydration rapidly induces polymerization of the beta-D-glucopyranosyl abscisate hydrolyzing enzyme AtBG1, resulting in a 4fold increase in enzymatic activity. Diurnal increases in abscisate levels are attributable to polymerization-mediated AtBG1 activation. Activation of inactive abscisate pools by polymerized AtBG1 is a mechanism by which plants rapidly adjust abscisate levels and respond to changing environmental cues
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
show the reaction diagram
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucose + abscisate
show the reaction diagram
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?
beta-D-glucopyranoyl abscisate + H2O
D-glucose + abscisate
show the reaction diagram
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?
Glc-conjugated abscisic acid + H2O
abscisic acid + D-glucose
show the reaction diagram
p-nitrophenyl-beta-D-glucopyranoside + H2O
beta-D-glucopyranose + p-nitrophenol
show the reaction diagram
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?
additional information
?
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the enzyme does not hydrolyze beta-D-glucopyranosyl zeatin
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-D-glucopyranosyl abscisate
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inhibits activity with p-nitrophenol-beta-D-glucopyranoside as substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41
beta-D-glucopyranosyl abscisate
pH 6.0, 35°C
1.8
p-nitrophenyl-beta-D-glucopyranoside
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pH 4.8, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
beta-D-glucopyranosyl abscisate
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pH 4.8, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.017
pH 6.0, 35°C, activity in control seedlings
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
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assay at
6
enzyme in crude extract
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6.5
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pH 4.5: about 50% of maximal activity, pH 6.5: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
10 * 60000, main peak of AtBG1 in dehydration-stressed plants. Dehydration rapidly induces polymerization of AtBG1, resulting in a 4fold increase in enzymatic activity. Diurnal increases in abscisate levels are attributable to polymerization-mediated AtBG1 activation
98000
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x * 98000, GFP-tagged enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
dehydration rapidly induces polymerization of the beta-D-glucopyranosyl abscisate hydrolyzing enzyme AtBG1, resulting in a 4fold increase in enzymatic activity. Assembly of AtBG1 into higher molecular weight forms upon dehydration stress occurs at a mild condition such as exposure to 30% relative humidity for 30 min, indicating that the response is very sensitive to dehydration stress
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant GFP-tagged enzyme from vacuoles by ultracentrifugation
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression in creeping bentgrass cv. Crenshaw via Agrobacterium tumefaciens strain EHA105 transformation system. the engineered plants shw increased abscisic acid levels, phenotype of transgenic plants
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transient expression of HA-tagged wild-type enzyme and mutant E426Q in protoplasts, expression of GFP-tagged enzyme in vacuoles; transient expression of HA-tagged wild-type enzyme BG1 in protoplasts
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
at the concentration of 100 mM beta-D-glucopyranosyl abscisate, the activity is 1.7fold greater than in controls, which suggests that beta-D-glucopyranosyl abscisate might cause enzyme induction
the recombinant enzyme is induced by Glc-conjugated abscisic acid; the recombinant enzyme is induced by Glc-conjugated abscisic acid
upregulated by salt stress
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAC105
a deletion mutant that lacks 105 residues at the C terminus. NO activity
E207Q
the amount of abscisate released by the mutant enzyme is reduced to 25% of that of the wild-type value, indicating that glutamic acid at position 207 is important for hydrolytic activity
additional information