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Information on EC 3.2.1.175 - beta-D-glucopyranosyl abscisate beta-glucosidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SE50
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3.2.1.175 beta-D-glucopyranosyl abscisate beta-glucosidaseIUBMB Comments
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 .
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
atbg1, aba-beta-d-glucosidase, beta-glucosidase homolog 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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].
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
Glc-conjugated abscisic acid + H2O
abscisic acid + D-glucose
in vitro activity of isozyme BG2
-
-
?
additional information
?
-
the enzyme does not hydrolyze beta-D-glucopyranosyl zeatin
-
-
?
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
-
-
-
?
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
-
-
-
-
?
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
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. 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
-
-
?
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
librated free abscisate may induce growth inhibition in Arabidopsis hypocotyls. Exogenously applied beta-D-glucopyranosyl abscisate may be absorbed by roots and hydrolyzed by beta-D-glucosidase, with the subsequent release of abscisate, which would potentially inhibit the growth of Arabidopsis hypocotyls
-
-
?
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
the stress hormone abscisic acid that enables plants to survive recurring stresses such as drought, cold, and high salt in soils. Abscisate concentrations can be rapidly increased in response to these osmotic stresses. The cleavage of glucose-conjugated abscisate by an abscisate-specific beta-glucosidase, AtBG1, is a way to produce bioactive abscisate in response to dehydration stress and also day/night conditions
-
-
?
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
the enzyme is specific for beta-D-glucopyranosyl abscisate
-
-
?
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
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
-
-
-
?
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
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. 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
-
-
?
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
librated free abscisate may induce growth inhibition in Arabidopsis hypocotyls. Exogenously applied beta-D-glucopyranosyl abscisate may be absorbed by roots and hydrolyzed by beta-D-glucosidase, with the subsequent release of abscisate, which would potentially inhibit the growth of Arabidopsis hypocotyls
-
-
?
beta-D-glucopyranosyl abscisate + H2O
beta-D-glucopyranose + abscisate
the stress hormone abscisic acid that enables plants to survive recurring stresses such as drought, cold, and high salt in soils. Abscisate concentrations can be rapidly increased in response to these osmotic stresses. The cleavage of glucose-conjugated abscisate by an abscisate-specific beta-glucosidase, AtBG1, is a way to produce bioactive abscisate in response to dehydration stress and also day/night conditions
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
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
BG2 localizes to the central vacuole. The N-terminal region of enzyme BG2 is responsible for the vacuolar targeting. The majority of BG2 localizes to the vacuole
abscisate generated by AtBG1 in the endoplasmic reticulum is secreted from cells into the apoplastic space of the leaf where it may play a role in initiation of ABA signaling
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
in Arabidopsis thaliana, abscisic acid levels are increased both through de novo biosynthesis and via beta-glucosidase homolog 1-mediated hydrolysis of Glc-conjugated abscisic acid. In addition to the de novo biosynthesis, abscisic acid is produced in multiple organelles by organelle-specific beta-glucosidases in response to abiotic stresses
malfunction
multiple Arabidopsis thaliana bg2 alleles with a T-DNA insertion in BG2 are more sensitive to dehydration and NaCl stress compared to the wild-type enzyme, whereas BG2 overexpression results in enhanced resistance to dehydration and NaCl stress
physiological function
malfunction
atbg1 plants exhibit abscisate deficiency and show decreased seed abscisate levels and a slightly decreased level of dehydration induced abscisate accumulation
malfunction
loss of AtBG1 causes defective stomatal movement, early germination, abiotic stress-sensitive phenotypes, and lower abscisate levels, whereas plants with ectopic AtBG1 accumulate higher abscisate levels and display enhanced tolerance to abiotic stress
physiological function
in addition to the de novo biosynthesis, abscisic acid is produced in multiple organelles by organelle-specific beta-glucosidases in response to abiotic stresses. BG2 increases abscisic acid levels in protoplasts upon application of exogenous Glc-conjugated abscisic acid
physiological function
-
the Arabidopsis beta-glucosidase AtBG1 hydrolyzes glucose-conjugated, biologically inactive abscisic acid to produce active abscisic acid, which increases the level of abscisic acid in plants. The phytohormone abscisic acid is critical for growth, development, and survival of plants in response to environmental stresses
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). BGL18_ARATH
528
1
60459
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
decamer
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
decamer
dehydration treatment causes ATBG1 to polymerize (molecular weights consistent with ATBG1 10-mers are observed) and this polymerization increases the specific activity of ATBG1 in hydrolysis of beta-D-glucopyranosyl abscisate
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
E426Q
site-directed mutagenesis the enzyme is not induced by Glc-conjugated abscisic acid and shows reduced activity compared to the wild-type enzyme
additional information
additional information
-
overexpression of BG2 rescues the bg1 mutant phenotype, as observed for the overexpression of NCED3 in bg1 mutants. NaCl stress-sensitive root growth of bg2-1 and bg2-2 mutants
additional information
overexpression of BG2 rescues the bg1 mutant phenotype, as observed for the overexpression of NCED3 in bg1 mutants. NaCl stress-sensitive root growth of bg2-1 and bg2-2 mutants
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GFP-tagged enzyme from vacuoles by ultracentrifugation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transient expression of HA-tagged wild-type enzyme BG1 in protoplasts
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
-
transient expression of HA-tagged wild-type enzyme and mutant E426Q in protoplasts, expression of GFP-tagged enzyme in vacuoles
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schroeder, J.I.; Nambara, E.
A quick release mechanism for abscisic acid
Cell
126
1023-1025
2006
Arabidopsis thaliana (Q9SE50)
Lee, K.H.; Piao, H.L., Kim, H.Y.; Choi, S.M.; Jiang, F.; Hartung, W.; Hwang, I.; Kwak, J.M.; Lee, I.J.; Hwang, I.
Activation of glucosidase via stress-induced polymerization rapidly increases active pools of abscisic acid
Cell
126
1109-1120
2006
Arabidopsis thaliana (Q9SE50)
Verslues, P.E.; Zhu, J.K.
New developments in abscisic acid perception and metabolism
Curr. Opin. Plant Biol.
10
447-452
2007
Arabidopsis thaliana (Q9SE50)
Kato-Noguchi, H.; Tanaka, Y.
Effect of ABA-beta-D-glucopyranosyl ester and activity of ABA-beta-D-glucosidase in Arabidopsis thaliana
J. Plant Physiol.
165
788-790
2008
Arabidopsis thaliana (Q9SE50), Arabidopsis thaliana
Han, Y.J.; Cho, K.C.; Hwang, O.J.; Choi, Y.S.; Shin, A.Y.; Hwang, I.; Kim, J.I.
Overexpression of an Arabidopsis beta-glucosidase gene enhances drought resistance with dwarf phenotype in creeping bentgrass
Plant Cell Rep.
31
1677-1686
2012
Arabidopsis thaliana
Xu, Z.Y.; Lee, K.H.; Dong, T.; Jeong, J.C.; Jin, J.B.; Kanno, Y.; Kim, D.H.; Kim, S.Y.; Seo, M.; Bressan, R.A.; Yun, D.J.; Hwang, I.
A vacuolar beta-glucosidase homolog that possesses glucose-conjugated abscisic acid hydrolyzing activity plays an important role in osmotic stress responses in Arabidopsis
Plant Cell
24
2184-2199
2012
Arabidopsis thaliana, Arabidopsis thaliana (Q9SE50), Arabidopsis thaliana Col-0, Arabidopsis thaliana Col-0 (Q9SE50)
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