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Information on EC 1.14.14.137 - (+)-abscisic acid 8'-hydroxylase
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1.14.14.137 (+)-abscisic acid 8'-hydroxylaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein found in plants. Catalyses the first step in the oxidative degradation of abscisic acid and is considered to be the pivotal enzyme in controlling the rate of degradation of this plant hormone . CO inhibits the reaction, but its effects can be reversed by the presence of blue light . The 8'-hydroxyabscisate formed can be converted into (-)-phaseic acid, most probably spontaneously.
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Word Map
- 1.14.14.137
-
dormancy
-
9-cis-epoxycarotenoid
-
imbibition
-
phaseic
-
8'-hydroxylation
-
pre-harvest
-
after-ripening
-
+-abscisic
-
aba-responsive
- diniconazole
-
epoxycarotenoids
- agriculture
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
aba 8'-hydroxylase, cyp707a, cyp707a2, cyp707a3, cyp707a1, abscisic acid 8'-hydroxylase, ahcyp707a1, taaba8'oh1, aba-8'-hydroxylase, ahcyp707a2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(+)-abscisic acid 8'-hydroxylase
ABA 8'-hydroxylase
abscisic acid 8'-hydroxylase
CYP707A
CYP707A1
CYP707A2
CYP707A3
CYP707A4
EC 1.14.13.93
-
-
formerly
-
abscisic acid 8'-hydroxylase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2 = 8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
abscisate,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (8'-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein found in plants. Catalyses the first step in the oxidative degradation of abscisic acid and is considered to be the pivotal enzyme in controlling the rate of degradation of this plant hormone [1]. CO inhibits the reaction, but its effects can be reversed by the presence of blue light [1]. The 8'-hydroxyabscisate formed can be converted into (-)-phaseic acid, most probably spontaneously.
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CAS REGISTRY NUMBER
COMMENTARY
153190-37-5
-
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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
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
phaseic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+-)-3'-methyl-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
32% of the activity with (+)-S-abscisate
-
-
?
(+-)-abscisic acid-3'-thio-n-butyl thiol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
2% of the activity with (+)-S-abscisate
-
-
?
(1'S)-(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is active with the naturally occuring (1'S)-(+)-enantiomer, but not with the naturally not occuring enantiomer (1'R)-(-)-abscisic acid. The C4'-oxo moiety coupled to the C2'-C3'-double bond in the key functional group for the enzyme to distinguish (1'S)-(+)-abscisic acid from (1'R)-(-)-abscisic acid
-
-
?
(2Z,4E)-5-[(1R,6R)-1-hydroxy-2,2,6-trimethylcyclohexyl]penta-2,4-dienoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
a structural analogue of abscisic acid lacking the C6 methyl group and the alpha,beta-unsaturated carbonyl in the six-membered ring, synthesis, overview. Both enantiomers of this analogue bind to the enzyme
-
-
?
(2Z,4E)-5-[(1S,6S)-1-hydroxy-2,2,6-trimethylcyclohexyl]penta-2,4-dienoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
a structural analogue of abscisic acid lacking the C6 methyl group and the alpha,beta-unsaturated carbonyl in the six-membered ring, synthesis, overview. Both enantiomers of this analogue bind to the enzyme
-
-
?
(S)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
1'-deoxy-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
99% of the activity with (+)-S-abscisate
-
-
?
1'-deoxy-1'-fluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
94% of the activity with (+)-S-abscisate
-
-
?
2'alpha,3'alpha-dihydro-2'alpha,3'alpha-epoxy-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
19% of the activity with (+)-S-abscisate
-
-
?
3'-bromo-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
5% of the activity with (+)-S-abscisate
-
-
?
3'-chloro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
19% of the activity with (+)-S-abscisate
-
-
?
3'-fluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
68% of the activity with (+)-S-abscisate
-
-
?
6-nor-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
60% of the activity with (+)-S-abscisate
-
-
?
7'-methyl-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
15% of the activity with (+)-S-abscisate
-
-
?
7'-nor-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
15% of the activity with (+)-S-abscisate
-
-
?
8'-fluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
11% of the activity with (+)-S-abscisate
-
-
?
8'-methylene-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
4% of the activity with (+)-S-abscisate
-
-
?
9',9'-difluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
9',9'-difluoro-8'-hydroxy-(+)-S-abscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
3% of the activity with (+)-S-abscisate
-
-
?
9'-fluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
33% of the activity with (+)-S-abscisate
-
-
?
9'-methyl-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
3% of the activity with (+)-S-abscisate
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
key enzyme in abscisic acid catabolism
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
isoform CYP707A3 is specific for (+)-isomer
isoform CYP707A3, no hydroxylation at 7 position
-
?
(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
for inhibitor studies the decrease in production of phaseic acid is measured
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
-
isomerisation of 8-hydroxy-abscisic acid to phaseic acid is not catalyzed by enzyme
-
-
?
additional information
?
-
-
substrate recognition strictly requires the 6'-methyl groups
-
-
?
additional information
?
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
?
additional information
?
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
?
additional information
?
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
?
additional information
?
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
?
additional information
?
-
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
phaseic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(1'S)-(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is active with the naturally occuring (1'S)-(+)-enantiomer, but not with the naturally not occuring enantiomer (1'R)-(-)-abscisic acid. The C4'-oxo moiety coupled to the C2'-C3'-double bond in the key functional group for the enzyme to distinguish (1'S)-(+)-abscisic acid from (1'R)-(-)-abscisic acid
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
key enzyme in abscisic acid catabolism
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
?
additional information
?
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
?
additional information
?
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
?
additional information
?
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
?
additional information
?
-
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH-hemoprotein reductase
-
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+-)-abscisic acid-3'-thio-n-butyl thiol
-
competitive, 51% inhibition at 0.05 mM
(1'R,2'R)-(-)-2',3'-dihydro-4'-deoxo-abscisic acid
-
competitive inhibition
(1'S*,2'S*,6'S*)-(+-)-6-nor-2',3'-dihydro-4'-deoxo-8',8'-difluoro-abscisate
-
50% inhibition at 0.00063 mM
(1'S*,2'S*,6'S*)-(+-)-6-nor-2',3'-dihydro-4'-deoxo-abscisate
-
50% inhibition at 0.00091 mM
(1E)-1-(4-chlorophenyl)-2-[2-(hydroxymethyl)-1H-imidazol-1-yl]-4,4-dimethylpent-1-en-3-ol
-
31% inhibition at 0.01 mM
(1E)-1-(4-chlorophenyl)-2-[5-(hydroxymethyl)-1H-imidazol-1-yl]-4,4-dimethylpent-1-en-3-ol
-
95% inhibition at 0.01 mM
(1E)-1-[4-(4-butyl-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
(1E)-1-[4-(4-heptyl-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 96%
(1E)-1-[4-[4-(1-hydroxybutyl)-1H-1,2,3-triazol-1-yl]phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 92%
(1E)-1-[4-[4-(1-hydroxyethyl)-1H-1,2,3-triazol-1-yl]phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 77%
(1E)-1-[4-[4-(hydroxymethyl)-1H-1,2,3-triazol-1-yl]phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 83%
(1E)-4,4-dimethyl-1-[4-(4-nonyl-1H-1,2,3-triazol-1-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 100%
(1E)-4,4-dimethyl-1-[4-(4-pentadecyl-1H-1,2,3-triazol-1-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 54%
(1E)-4,4-dimethyl-1-[4-(4-propyl-1H-1,2,3-triazol-1-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 92%
(1E)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)-1-[4-(4-tridecyl-1H-1,2,3-triazol-1-yl)phenyl]pent-1-en-3-ol
-
0.01 mM, inhibits by 95%
(1E)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)-1-[4-(4-undecyl-1H-1,2,3-triazol-1-yl)phenyl]pent-1-en-3-ol
-
0.01 mM, inhibits by 100%
(1E,3R)-1-(3-[3-[2-(2-butoxyethoxy)ethoxy]prop-1-yn-1-yl]phenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
(1E,3R)-1-(4-[3-[2-(2-butoxyethoxy)ethoxy]prop-1-yn-1-yl]phenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
(1E,3R)-1-[4-(4-[[2-(2-butoxyethoxy)ethoxy]methyl]-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
(1E,3R)-4,4-dimethyl-1-[3-[4-(2,5,8,11-tetraoxadodecan-1-yl)-1H-1,2,3-triazol-1-yl]phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
strong and selective inhibitor, effects of the inhibitor on stomatal closure and drought tolerance, overview
(1E,3R)-4,4-dimethyl-1-[4-(2,5,8,11-tetraoxatetradec-13-yn-14-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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(1E,3S)-1-(3-[3-[2-(2-butoxyethoxy)ethoxy]prop-1-yn-1-yl]phenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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(1E,3S)-1-(4-[3-[2-(2-butoxyethoxy)ethoxy]prop-1-yn-1-yl]phenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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(1E,3S)-1-[4-(4-[[2-(2-butoxyethoxy)ethoxy]methyl]-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
(1E,3S)-4,4-dimethyl-1-[3-(2,5,8,11-tetraoxatetradec-13-yn-14-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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(1E,3S)-4,4-dimethyl-1-[4-(2,5,8,11-tetraoxatetradec-13-yn-14-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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(E)-1-(1-(4-chlorophenyl)-3-fluoro-4,4-dimethylpent-1-en-2-yl)-1H-1,2,4-triazole
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i.e. UNI-F
(E)-1-(1-(4-chlorophenyl)-4,4-dimethylpent-1-en-2-yl)-1H-imidazole
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i.e. IMI-H
(E)-2-(2-((1-(4-(3-hydroxy-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-1-yl)phenyl)-1H-1,2,3-triazol-4-yl)methoxy)ethoxy)ethyl 4-methylbenzenesulfonate
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i.e. abscinazole-E1, or UT1-E2Ts, or Abz-E1, a specific potent inhibitor of ABA 8'-hydroxylase, that is a weak inhibitor of ent-kaurene oxidase, CYP701A, EC 1.14.13.78, both in vitro and in vivo
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-5Himidazo[2,1-c][1,4]oxazin-8(6H)-one
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(E)-6-tert-butyl-5-(4-chlorobenzylidene)-5Himidazo[5,1-c][1,4]oxazin-8(6H)-one
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(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-[1,2,4]triazolo[5,1-c][1,4]oxazin-8-ol
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-[1,2,4]triazolo[5,1-c][1,4]oxazine
(S,E)-1-(1-(4-chlorophenyl)-3-fluoro-4,4-dimethylpent-1-en-2-yl)-1H-imidazole
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i.e. IMI-F
(S,E)-1-(1-(4-chlorophenyl)-3-methoxy-4,4-dimethylpent-1-en-2-yl)-1H-imidazole
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i.e. IMI-OMe
1'-deoxy-1'-fluoro-(+)-S-abscisate
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competitive, 100% inhibition at 0.05 mM
1'-deoxy-7'-hydroxy abscisic acid
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63% inhibition of the enzyme at 0.05 mM
1-[(1E)-1-(4-chlorophenyl)-3-ethoxy-4,4-dimethylpent-1-en-2-yl]-5-(ethoxymethyl)-1H-imidazole
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62% inhibition at 0.01 mM
1-[(1E)-1-(4-chlorophenyl)-3-hydroxy-4,4-dimethylpent-1-en-2-yl]-1H-imidazole-5-carbaldehyde
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91% inhibition at 0.01 mM
1-[(1E)-1-(4-chlorophenyl)-3-methoxy-4,4-dimethylpent-1-en-2-yl]-5-(methoxymethyl)-1H-imidazole
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95% inhibition at 0.01 mM
2'alpha,3'alpha-dihydro-2'alpha,3'alpha-epoxy-(+)-S-abscisate
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competitive, 56% inhibition at 0.05 mM
4-(1-[4-[(1E)-3-hydroxy-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-1-yl]phenyl]-1H-1,2,3-triazol-4-yl)butanoic acid
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0.01 mM, inhibits by 63%
5'alpha,8'-cyclo-(+)-S-abscisate
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competitive, 28% inhibition at 0.05 mM
8',8',8'-trifluoro-(+)-S-abscisate
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competitive, 38% inhibition at 0.05 mM
9',9',9'-trifluoro-(+)-S-abscisate
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competitive, 55% inhibition at 0.05 mM
diniconazole
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potent competitive inhibitor, decreases seed germination rate by 65.6% at 36 h of imbibition
methyl (2E)-3-[1-[(1E)-1-(4-chlorophenyl)-3-hydroxy-4,4-dimethylpent-1-en-2-yl]-1H-imidazol-5-yl]prop-2-enoate
methyl (2Z)-3-[1-[(1E)-1-(4-chlorophenyl)-3-hydroxy-4,4-dimethylpent-1-en-2-yl]-1H-imidazol-5-yl]prop-2-enoate
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100% inhibition at 0.01 mM
S-uniconazole
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i.e. S-(+)-E-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol or UNI-OH, an azole-containing P450 inhibitor and a plant growth retardant, is a strong inhibitor of the enzyme, structure-activity relationship, the main site of action of UNI-OH is suggested to be ent-kaurene oxidase, EC 1.14.13.78, UNI-OH also inhibits brassinosteroid biosynthesis, and alters the level of other plant hormones, such as auxins, cytokinins, ethylene, and abscisic acid, overview
(1E)-1-[4-(4-butyl-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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0.01 mM, inhibits by 100%
(1E)-1-[4-(4-butyl-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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(1E,3R)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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27% inhibition of recombinant enzyme with 10 microM inhibitor
(1E,3R)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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27% inhibition of recombinant Arabidopsis enzyme with 10 microM inhibitor
(1E,3R)-1-[4-(4-[[2-(2-butoxyethoxy)ethoxy]methyl]-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
(-)-Abz-E2B, selective inhibitor
(1E,3R)-1-[4-(4-[[2-(2-butoxyethoxy)ethoxy]methyl]-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
(-)-Abz-E2B
(1E,3S)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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10% inhibition of recombinant enzyme with 10 microM inhibitor
(1E,3S)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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i.e. uniconazole
(1E,3S)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
i.e. S-uniconazole
(1E,3S)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
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10% inhibition of recombinant Arabidopsis enzyme with 10 microM inhibitor