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Information on EC 1.14.14.137 - (+)-abscisic acid 8'-hydroxylase and Organism(s) Arabidopsis thaliana and UniProt Accession Q949P1
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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 taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(+)-abscisic acid 8'-hydroxylase
ABA 8'-hydroxylase
abscisic acid 8'-hydroxylase
CYP707A
CYP707A2
CYP707A3
abscisic acid 8'-hydroxylase
-
-
PATHWAY SOURCE
PATHWAYS
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.
CAS REGISTRY NUMBER
COMMENTARY
153190-37-5
-
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
(+)-abscisic acid + [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
(+)-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
-
-
for inhibitor studies the decrease in production of phaseic acid is measured
-
?
(+)-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
-
-
?
(+)-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
-
?
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
-
-
?
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
(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
-
-
-
-
?
additional information
?
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
?
(+)-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
-
-
?
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._
-
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-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
27% inhibition of recombinant enzyme with 10 microM inhibitor
(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
(-)-Abz-E2B, selective inhibitor
(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
-
(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
-
(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
-
(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
(+)-Abz-E2B
(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
-
(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
-
(E)-1-(1-(4-chlorophenyl)-3-fluoro-4,4-dimethylpent-1-en-2-yl)-1H-1,2,4-triazole
-
i.e. UNI-F
(E)-1-(1-(4-chlorophenyl)-4,4-dimethylpent-1-en-2-yl)-1H-imidazole
-
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
-
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)-5H-imidazo[2,1-c][1,4]oxazin-8(6H)-one
-
35% inhibition of recombinant enzyme with 10 microM inhibitor
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-5H-imidazo[5,1-c][1,4]oxazin-8(6H)-one
-
52% inhibition of recombinant enzyme with 10 microM inhibitor
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-5Himidazo[2,1-c][1,4]oxazin-8(6H)-one
-
-
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-5Himidazo[5,1-c][1,4]oxazin-8(6H)-one
-
-
(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
-
i.e. IMI-F
(S,E)-1-(1-(4-chlorophenyl)-3-methoxy-4,4-dimethylpent-1-en-2-yl)-1H-imidazole
-
i.e. IMI-OMe
1'-deoxy-1'-fluoro-(+)-S-abscisate
-
competitive, 100% inhibition at 0.05 mM
1'-deoxy-7'-hydroxy abscisic acid
-
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
-
62% inhibition at 0.01 mM
1-[(1E)-1-(4-chlorophenyl)-3-hydroxy-4,4-dimethylpent-1-en-2-yl]-1H-imidazole-5-carbaldehyde
-
91% inhibition at 0.01 mM
1-[(1E)-1-(4-chlorophenyl)-3-methoxy-4,4-dimethylpent-1-en-2-yl]-5-(methoxymethyl)-1H-imidazole
-
95% inhibition at 0.01 mM
2'alpha,3'alpha-dihydro-2'alpha,3'alpha-epoxy-(+)-S-abscisate
-
competitive, 56% inhibition at 0.05 mM
3R-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
-
abscinazole-F1, 95% inhibition of recombinant enzyme with 10 microM inhibitor
3S-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
-
abscinazole-F1, 96% inhibition of recombinant enzyme with 10 microM inhibitor
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
-
0.01 mM, inhibits by 63%
5'alpha,8'-cyclo-(+)-S-abscisate
-
competitive, 28% inhibition at 0.05 mM
8',8',8'-trifluoro-(+)-S-abscisate
-
competitive, 38% inhibition at 0.05 mM
9',9',9'-trifluoro-(+)-S-abscisate
-
competitive, 55% inhibition at 0.05 mM
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
-
100% inhibition at 0.01 mM
R-(+)-E-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol
-
R-(+)-uniconazole, 79% inhibition of recombinant enzyme with 10 microM inhibitor
R-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
-
87% inhibition of recombinant enzyme with 10 microM inhibitor
S-(+)-E-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol
-
S-(+)-uniconazole, 100% inhibition of recombinant enzyme with 10 microM inhibitor
S-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
-
100% inhibition of recombinant enzyme with 10 microM inhibitor
S-uniconazole
-
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
-
-
(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
-
0.01 mM, inhibits by 100%
(1E,3S)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
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
-
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
(E)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
14% inhibition of recombinant enzyme with 10 microM inhibitor
(E)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
inhibitory activity is much weaker than that of S-UNI
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
-
abscinazole-F1, 91% inhibition of recombinant enzyme with 10 microM inhibitor
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
-
abscinazole-F1, more than 50% inhibition at 0.01 mM, competitive inhibitor, is the most specific inhibitor against ABA 8'-hydroxylase, although it is not the strongest
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazine
-
-
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazine
-
13% inhibition of recombinant enzyme with 10 microM inhibitor
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
-
competitive inhibitor
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
-
100% inhibition of recombinant enzyme with 10 microM inhibitor
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-[1,2,4]triazolo[5,1-c][1,4]oxazin-8-ol
-
69% inhibition of recombinant enzyme with 10 microM inhibitor
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-[1,2,4]triazolo[5,1-c][1,4]oxazin-8-ol
-
more than 50% inhibition at 0.01 mM
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-[1,2,4]triazolo[5,1-c][1,4]oxazine
-
-
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-[1,2,4]triazolo[5,1-c][1,4]oxazine
-
31% inhibition of recombinant enzyme with 10 microM inhibitor
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 (2E)-3-[1-[(1E)-1-(4-chlorophenyl)-3-hydroxy-4,4-dimethylpent-1-en-2-yl]-1H-imidazol-5-yl]prop-2-enoate
-
98% inhibition at 0.01 mM
additional information
-
pH-dependent partition coefficient of the inhibitors at different pH values, overview, no inhibition by 7'-hydroxy abscisic acid, four-step synthesis of 7'-hydroxy-abscisic acid from alpha-ionone, overview
-
additional information
about 4.8fold reduced expression in Arabidopsis thaliana mutant aba2 with a mutation at the start of exon 2
-
additional information
about 5.6fold reduced expression in Arabidopsis thaliana mutant etr1 with altered gene expression of the ethylene signal transduction pathway
-
additional information
-
inhibitor synthesis, overview. Conformational energy profiles of ligands by computational molecular dynamics simulation, inhibition kinetics, overview. No inhibition by (1'R,2'R)-(-)-2',3'-dihydro-abscisic acid
-
additional information
development of a selective inhibitor of CYP707A, (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, by structurally modifying S-uniconazole, which functions as an inhibitor of CYP707A and as a gibberellin biosynthetic enzyme, but with low yield. Design of CYP707A inhibitors, Abz-T compounds, that have simpler structures in which the 1,2,3-triazolyl ring of (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 has been replaced with a triple bond, by successful synthesis in shorter steps, resulting in greater yields than that of (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. In the enzymatic assays, Abz-T compound (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 acts as a strong and selective inhibitor and is a more practical and effective inhibitor of CYP707A than (-)-Abz-E2B. Analysis of the biological effects in Arabidopsis thaliana reveals that (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 enhances abscisic acid effects more than (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 in seed germination and in the expression of ABA-responsive genes. Treatment with (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 induces stomatal closure and improves drought tolerance in Arabidopsis thaliana
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
high humidity reduces the abscisic acid levels by the activation of CYP707A1 and CYP707A3
-
additional information
-
NO regulates seed dormancy and germination and such action needs CYP707As family's participation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0034
(+)-abscisic acid
-
50 mM potassium phosphate buffer, pH 7.25, 50 microM NADPH, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00045
(1'R,2'R)-(-)-2',3'-dihydro-4'-deoxo-abscisic acid
-
pH 7.2-7.3, 30°C
0.00041
(1'S*,2'S*,6'S*)-(+-)-6-nor-2',3'-dihydro-4'-deoxo-8',8'-difluoro-abscisate
-
pH 7.25, 30°C
0.0004
(1'S*,2'S*,6'S*)-(+-)-6-nor-2',3'-dihydro-4'-deoxo-abscisate
-
pH 7.25, 30°C
0.00016
(1E)-1-(4-chlorophenyl)-2-[5-(hydroxymethyl)-1H-imidazol-1-yl]-4,4-dimethylpent-1-en-3-ol
-
-
0.000035
(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
pH 7.6, 22°C, recombinant isozyme CYP707A12
0.034
(E)-1-(1-(4-chlorophenyl)-3-fluoro-4,4-dimethylpent-1-en-2-yl)-1H-1,2,4-triazole
-
pH 7.2-7.3, 30°C, recombinant enzyme
0.000027
(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
-
pH 7.25, 30°C, recombinant enzyme
0.00052
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-5H-imidazo[5,1-c][1,4]oxazin-8(6H)-one
-
10 microM inhibitor in 50 mM potassium phosphate buffer, pH 7.25, 50 microM NADPH, 30°C, recombinant enzyme
0.00042 - 0.00097
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
0.0012
(S,E)-1-(1-(4-chlorophenyl)-3-methoxy-4,4-dimethylpent-1-en-2-yl)-1H-imidazole
-
pH 7.2-7.3, 30°C, recombinant enzyme
0.00024
1-[(1E)-1-(4-chlorophenyl)-3-hydroxy-4,4-dimethylpent-1-en-2-yl]-1H-imidazole-5-carbaldehyde
-
-
0.00019
1-[(1E)-1-(4-chlorophenyl)-3-methoxy-4,4-dimethylpent-1-en-2-yl]-5-(methoxymethyl)-1H-imidazole
-
-
0.00042
3R-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
-
10 microM inhibitor in 50 mM potassium phosphate buffer, pH 7.25, 50 microM NADPH, 30°C, recombinant enzyme
0.00097
3S-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
-
10 microM inhibitor in 50 mM potassium phosphate buffer, pH 7.25, 50 microM NADPH, 30°C, recombinant enzyme
0.000195
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
-
-
0.00012
methyl (2E)-3-[1-[(1E)-1-(4-chlorophenyl)-3-hydroxy-4,4-dimethylpent-1-en-2-yl]-1H-imidazol-5-yl]prop-2-enoate
-
-
0.00022
methyl (2Z)-3-[1-[(1E)-1-(4-chlorophenyl)-3-hydroxy-4,4-dimethylpent-1-en-2-yl]-1H-imidazol-5-yl]prop-2-enoate
-
-
0.00145
R-(+)-E-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol
-
10 microM inhibitor in 50 mM potassium phosphate buffer, pH 7.25, 50 microM NADPH, 30°C
0.00001
S-(+)-E-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol
-
10 microM inhibitor in 50 mM potassium phosphate buffer, pH 7.25, 50 microM NADPH, 30°C, recombinant enzyme
0.00016
S-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
-
10 microM inhibitor in 50 mM potassium phosphate buffer, pH 7.25, 50 microM NADPH, 30°C, recombinant enzyme
additional information
additional information
-
inhibition kinetics, computational methods, overview
-
0.00042
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
-
3R-enantiomer, pH 7.25, 30°C
0.00097
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
-
3S-enantiomer, pH 7.25, 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000012
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A8
0.0002
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A6
0.000054
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A4
0.000064
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A12
0.0015
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A10
0.00024
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A7
0.001
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A5
0.0011
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A3
0.0012
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A11
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 7.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
CYP707A3 plays a major role in regulating abscisic acid levels, whereas CYP707A1 plays a minor role in regulating abscisic acid levels in shoots
CYP707A2 transcription is much higher than the other CYP707A genes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
CYP707A1 mutant shows similar phenotype to wild-type in freshly harvested or after-ripen seeds. Seeds of CYP707A1 mutant has its dormancy entirely broken 18 d after ripening. NO enhances the tolerance to abscisic acid in CYP707A1 mutant during germination. Abscisic acid concentrations decrease rapidly during the first 12 h in CYP707A1 mutant. NO enhances the tolerance to abscisic acid in CYP707A1 mutant
metabolism
physiological function
metabolism
-
key enzyme in the catabolism of abscisic acid (plant hormone involved in stress tolerance, seed dormancy, and other physiological events)
metabolism
-
ABA 8'-hydroxylase is the major and key P450 enzyme in the abscisic acid catabolism
physiological function
-
CYP707A1 and CYP707A3 are involved in stomatal opening in response to high humidity. Cyp707a1 and cyp707a3 mutants display lower stomatal conductance under turgid conditions (relative humidity 60%) than the wild-type. Cyp707a3 mutant exhibits high abscisic acid levels even after transferring to high-humidity conditions, whereas, under similar conditions, the cyp707a1 mutant exhibits low abscisic acid levels comparable to the wild-type. Stomatal closure of the cyp707a1 mutant, but not cyp707a3 mutant, is abscisic acid hypersensitive when epidermal peel ias treated with exogenous abscisic acid. CYP707A3 reduces the amount of mobile abscisic acid in vascular tissues in response to high humidity, whereas CYP707A1 inactivates local abscisic acid pools inside the guard cells
physiological function
-
CYP707A2 plays a major role in abscisic acid catabolism during the first stage of imbibition and regulates seeds dormancy. NO can break the dormancy of wild-type seeds, but it cannot break cyp707a2 mutant seed dormancy
physiological function
CYP707A2 plays a major role in abscisic acid catabolism during the first stage of imbibition. CYP707A2 is involved in NO-induced dormancy break. CYP707A2 mutant shows a strong dormancy in freshly harvested seeds. CYP707A2 mutant still maintains strong dormancy until 30 d. NO does not enhance the tolerance to abscisic acid in CYP707A2 mutant during germination
physiological function
CYP707A3 mutant shows similar phenotype to wild-type in freshly harvested or after-ripen seeds, with the seeds of CYP707A3 mutant having a slightly higher germination rate than the wild-type. Seeds of CYP707A3 mutant has its dormancy entirely broken 18 d after ripening. NO enhances the tolerance to abscisic acid in CYP707A3 mutant during germination
physiological function
-
ABA 8'-hydroxylase is the major and key P450 enzyme in the abscisic acid catabolism
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). ABAH1_ARATH
467
1
53037
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
-
x * 53000, isoform CYC707A1, x * 52000, isoform CYP707A3, SDS-PAGE
53000
-
x * 53000, isoform CYC707A1, x * 52000, isoform CYP707A3, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
CYP707A2 knockout mutant, hyperdormancy in seeds, accumulates 6fold higher levels of abscisic acid than wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme production is induced, cells centrifuged, pellets resuspended in buffer A (50 mM potassium phosphate buffer, pH 7.25, 20% glycerol, 1 mM EDTA, 0.1 mM dithiothreitol), sonicated, centrifuged, supernatants collected
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a truncated CYP707A3 (707A3d28), which lacks the putative membrane-spanning segment of the N-terminus (residues 328) coexpressed in Escherichia coli strain BL21 with Arabidopsis P450 reductase
-
CYP707A3, coexpression with Arabidopsis thaliana P450 reductase ATR2 in Escherichia coli
-
expression in baculovirus system, isoforms CYP707A1, CYP707A3, CYP707A4
-
promoter fragment of the translational start of each CYP707A amplified and cloned into pENTR/D-TOPO vector, cloned into the binary vector, pGWB3, with a recombination cassette for the expression of GUS-fused protein. Resulting plasmids electroporated into Agrobacterium strain GV3101, which is used to transform wild-type Arabidopsis accession Columbia plants
-
recombinant truncated Arabidopsis enzyme (707A3d28, lack of putative membrane spanning segment at N-terminus), expressed in Escherichia coli BL21
-
truncated CYP707A3 (707A3d28), which lacks the putative membrane-spanning segment of the N-terminus, residues 3-28, coexpressed in Escherichia coli BL21 with Arabidopsis P450 reductase
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription decreases to a lower level after 12 h of imbibition
transcription increases during the first 6 h of imbibition
transcription decreases to a lower level after 12 h of imbibition
transcription increases during the first 6 h of imbibition
when wild-type plants are transferred to high-humidity conditions (relative humidity 90%), CYP707A1 and CYP707A3 transcript levels increase primarily in guard cells and vascular tissues, respectively
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ueno, K.; Yoneyama, H.; Saito, S.; Mizutani, M.; Sakata, K.; Hirai, N.; Todoroki, Y.
A lead compound for the development of ABA 8'-hydroxylase inhibitors
Bioorg. Med. Chem. Lett.
15
5226-5229
2005
Arabidopsis thaliana
Kushiro, T.; Okamoto, M.; Nakabayashi, K.; Yamagishi, K.; Kitamura, S.; Asami, T.; Hirai, N.; Koshiba, T.; Kamiya, Y.; Nambara, E.
The Arabidopsis cytochrome P450 CYP707A encodes ABA 8'-hydroxylases: key enzymes in ABA catabolism
EMBO J.
23
1647-1656
2004
Arabidopsis thaliana
Windsor, M.L.; Zeevaart, J.A.
Induction of ABA 8'-hydroxylase by (+)-S-, (-)-R- and 8'-8'-8'-trifluoro-S-abscisic acid in suspension cultures of potato and Arabidopsis
Phytochemistry
45
931-934
1997
Arabidopsis thaliana, Solanum tuberosum
Saito, S.; Hirai, N.; Matsumoto, C.; Ohigashi, H.; Ohta, D.; Sakata, K.; Mizutani, M.
Arabidopsis CYP707As encode (+)-abscisic acid 8'-hydroxylase, a key enzyme in the oxidative catabolism of abscisic acid
Plant Physiol.
134
1439-1449
2004
Arabidopsis thaliana
Ueno, K.; Yoneyama, H.; Mizutani, M.; Hirai, N.; Todoroki, Y.
Asymmetrical ligand binding by abscisic acid 8-hydroxylase
Bioorg. Med. Chem.
15
6311-6322
2007
Arabidopsis thaliana
Todoroki, Y.; Kobayashi, K.; Yoneyama, H.; Hiramatsu, S.; Jin, M.H.; Watanabe, B.; Mizutani, M.; Hirai, N.
Structure-activity relationship of uniconazole, a potent inhibitor of ABA 8-hydroxylase, with a focus on hydrophilic functional groups and conformation
Bioorg. Med. Chem.
16
3141-3152
2008
Arabidopsis thaliana
Shimomura, H.; Etoh, H.; Mizutani, M.; Hirai, N.; Todoroki, Y.
Effect of the minor ABA metabolite 7-hydroxy-ABA on Arabidopsis ABA 8-hydroxylase CYP707A3
Bioorg. Med. Chem. Lett.
17
4977-4981
2007
Arabidopsis thaliana
Ueno, K.; Araki, Y.; Hirai, N.; Saito, S.; Mizutani, M.; Sakata, K.; Todoroki, Y.
Differences between the structural requirements for ABA 8'-hydroxylase inhibition and for ABA activity
Bioorg. Med. Chem.
13
3359-3370
2005
Arabidopsis thaliana
Todoroki, Y.; Kobayashi, K.; Shirakura, M.; Aoyama, H.; Takatori, K.; Nimitkeatkai, H.; Jin, M.H.; Hiramatsu, S.; Ueno, K.; Kondo, S.; Mizutani, M.; Hirai, N.
Abscinazole-F1, a conformationally restricted analogue of the plant growth retardant uniconazole and an inhibitor of ABA 8-hydroxylase CYP707A with no growth-retardant effect
Bioorg. Med. Chem.
17
6620-6630
2009
Arabidopsis thaliana, Malus sylvestris, Oryza sativa
Cheng, W.H.; Chiang, M.H.; Hwang, S.G.; Lin, P.C.
Antagonism between abscisic acid and ethylene in Arabidopsis acts in parallel with the reciprocal regulation of their metabolism and signaling pathways
Plant Mol. Biol.
71
61-80
2009
Arabidopsis thaliana (O81077)
Todoroki, Y.; Aoyama, H.; Hiramatsu, S.; Shirakura, M.; Nimitkeatkai, H.; Kondo, S.; Ueno, K.; Mizutani, M.; Hirai, N.
Enlarged analogues of uniconazole, new azole containing inhibitors of ABA 8-hydroxylase CYP707A
Bioorg. Med. Chem. Lett.
19
5782-5786
2009
Arabidopsis thaliana
Liu, Y.; Shi, L.; Ye, N.; Liu, R.; Jia, W.; Zhang, J.
Nitric oxide-induced rapid decrease of abscisic acid concentration is required in breaking seed dormancy in Arabidopsis
New Phytol.
183
1030-1042
2009
Arabidopsis thaliana (O81077), Arabidopsis thaliana (Q949P1), Arabidopsis thaliana (Q9FH76), Arabidopsis thaliana (Q9LJK2)
Okamoto, M.; Tanaka, Y.; Abrams, S.R.; Kamiya, Y.; Seki, M.; Nambara, E.
High humidity induces abscisic acid 8-hydroxylase in stomata and vasculature to regulate local and systemic abscisic acid responses in Arabidopsis
Plant Physiol.
149
825-834
2009
Arabidopsis thaliana
Liu, Y.; Zhang, J.
Rapid accumulation of NO regulates ABA catabolism and seed dormancy during imbibition in Arabidopsis
Plant Signal. Behav.
4
905-907
2009
Arabidopsis thaliana
Todoroki, Y.; Naiki, K.; Aoyama, H.; Shirakura, M.; Ueno, K.; Mizutani, M.; Hirai, N.
Selectivity improvement of an azole inhibitor of CYP707A by replacing the monosubstituted azole with a disubstituted azole
Bioorg. Med. Chem. Lett.
20
5506-5509
2010
Arabidopsis thaliana
Okazaki, M.; Nimitkeatkai, H.; Muramatsu, T.; Aoyama, H.; Ueno, K.; Mizutani, M.; Hirai, N.; Kondo, S.; Ohnishi, T.; Todoroki, Y.
Abscinazole-E1, a novel chemical tool for exploring the role of ABA 8-hydroxylase CYP707A
Bioorg. Med. Chem.
19
406-413
2011
Arabidopsis thaliana
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