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(+)-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
additional information
?
-
(+)-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
-
-
?
additional information
?
-
-
specific for (+)-isomer of abscisate
-
-
?
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(+)-1'-methoxy-abscisate
-
competitive
(+)-8',8'-difluoroabscisate
-
competitive
(+)-8'-acetylene-abscisate
(+)-8'-cyano-abscisic acid
-
competitive
(+)-8'-ethyl-abscisic acid
-
competitive
(+)-8'-methylacetylene-abscisic acid
-
competitive
(+)-8'-methylene-abscisate
-
competitive
(+)-8'-propargyl-abscisate
-
competitive
(+)-9'-allyl-abscisate
-
suicide inhibitor
(+)-9'-propargyl-abscisate
-
suicide inhibitor
(+-)-3'-methyl-abscisate
-
competitive, 64% inhibition at 0.05 mM
(+-)-abscisic acid-3'-thio-n-butyl thiol
-
competitive, 51% inhibition at 0.05 mM
(-)-8'-propargyl-abscisate
-
competitive
(-)-9'-propargyl-abscisate
-
suicide inhibitor
(-)-AHI1
-
competitive inhibition
(1'R)-(-)-4'-deoxo-abscisic acid
-
competitive inhibition
(1'R)-(-)-6-nor-abscisic acid
-
competitive inhibition
(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
(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
-
(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-chlorophenyl)-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
(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)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
(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
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-5H-imidazo[5,1-c][1,4]oxazin-8(6H)-one
(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-imidazo[2,1-c][1,4]oxazin-8-ol
(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[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]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
(Z)-1-(1-(4-chlorophenyl)-4,4-dimethylpent-1-en-2-yl)-1H-imidazole
-
-
1'-deoxy-(+)-S-abscisate
-
competitive, 73% inhibition at 0.05 mM
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-(4-chlorophenyl)-2-(1H-imidazol-1-yl)-4,4-dimethylpentan-1-ol
-
-
1-(4-chlorophenyl)-2-(1H-imidazol-1-yl)-4,4-dimethylpentan-1-one
-
-
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
3'-azido-(+)-S-abscisate
-
competitive, 38% inhibition at 0.05 mM
3'-bromo-(+)-S-abscisate
-
competitive, 65% inhibition at 0.05 mM
3'-chloro-(+)-S-abscisate
-
competitive, 70% inhibition at 0.05 mM
3'-fluoro-(+)-S-abscisate
-
competitive, 84% inhibition at 0.05 mM
3'-iodo-(+)-S-abscisate
-
competitive, 54% 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
3S-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
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
6-nor-(+)-S-abscisate
-
competitive, 88% inhibition at 0.05 mM
7'-methyl-(+)-S-abscisate
-
competitive, 83% inhibition at 0.05 mM
7'-nor-(+)-S-abscisate
-
competitive, 28% inhibition at 0.05 mM
7'-oxo abscisic acid
-
24% inhibition of the enzyme at 0.05 mM
8',8',8'-trifluoro-(+)-S-abscisate
-
competitive, 38% inhibition at 0.05 mM
8',8'-difluoro-(+)-S-abscisate
-
competitive, 83% inhibition at 0.05 mM
8'-fluoro-(+)-S-abscisate
-
competitive, 83% inhibition at 0.05 mM
8'-methyl-(+)-S-abscisate
-
competitive, 35% inhibition at 0.05 mM
8'-methylene-(+)-S-abscisate
-
competitive, 33% inhibition at 0.05 mM
9',9',9'-trifluoro-(+)-S-abscisate
-
competitive, 55% inhibition at 0.05 mM
9',9'-difluoro-(+)-S-abscisate
-
competitive, 76% inhibition at 0.05 mM
9'-fluoro-(+)-S-abscisate
-
competitive, 83% inhibition at 0.05 mM
9'-methyl-(+)-S-abscisate
-
competitive, 26% inhibition at 0.05 mM
abscisic aldehyde
-
competitive, 31% inhibition at 0.05 mM
CO
-
inhibition is reversible by blue and amber light
diniconazole
-
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
-
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-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
S-(+)-E-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol
S-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
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
Tetcyclacis
-
50% inhibition at 0.001 mM
(+)-8'-acetylene-abscisate
-
suicide inhibitor
(+)-8'-acetylene-abscisate
-
about 60% inactivation
(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)-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,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-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
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
-
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
(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 Arabidopsis enzyme with 10 microM inhibitor
(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)-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
(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; inhibitory activity is much weaker than that of S-UNI
(E)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
14% inhibition of recombinant Arabidopsis enzyme with 10 microM inhibitor
(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[2,1-c][1,4]oxazin-8(6H)-one
-
35% inhibition of recombinant Arabidopsis 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)-5H-imidazo[5,1-c][1,4]oxazin-8(6H)-one
-
52% inhibition of recombinant Arabidopsis 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, 91% inhibition of recombinant enzyme with 10 microM inhibitor; 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]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, 91% inhibition of recombinant Arabidopsis enzyme with 10 microM inhibitor
(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[2,1-c][1,4]oxazine
-
13% inhibition of recombinant Arabidopsis enzyme with 10 microM 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; competitive inhibitor
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
-
100% inhibition of recombinant Arabidopsis 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; 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]oxazin-8-ol
-
69% inhibition of recombinant Arabidopsis 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]oxazine
-
31% 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]oxazine
-
31% inhibition of recombinant Arabidopsis enzyme with 10 microM inhibitor
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
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
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 Arabidopsis 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
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
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 Arabidopsis enzyme with 10 microM inhibitor
cytochrome c
-
0.1 mM, complete inhibition
cytochrome c
-
oxidized form
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
methyl (2E)-3-[1-[(1E)-1-(4-chlorophenyl)-3-hydroxy-4,4-dimethylpent-1-en-2-yl]-1H-imidazol-5-yl]prop-2-enoate
-
-
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-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol
-
R-(+)-uniconazole, 79% inhibition of recombinant Arabidopsis 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
R-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
-
87% inhibition of recombinant Arabidopsis 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-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol
-
S-(+)-uniconazole, 100% inhibition of recombinant Arabidopsis 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 Arabidopsis 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-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
-
100% inhibition of recombinant Arabidopsis enzyme with 10 microM inhibitor
uniconazole
-
-
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
-
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; about 5.6fold reduced expression in Arabidopsis thaliana mutant etr1 with altered gene expression of the ethylene signal transduction pathway
-
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
-
additional information
-
not inactivating: (+)-8-methylene-abscisate, (+)-8-methylacetylene-abscisate
-
additional information
-
inhibition of reaction at O2 concentrations less than 10% v/v
-
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0.0111
(+)-1'-methoxy-abscisate
-
pH 7.6, 30°C
0.00017
(+)-8',8'-difluoroabscisate
-
pH 7.25, 30°C
0.019
(+)-8'-acetylene-abscisate
-
pH 7.6, 30°C
0.187
(+)-8'-cyano-abscisic acid
-
pH 7.6, 30°C
0.0129
(+)-8'-ethyl-abscisic acid
-
pH 7.6, 30°C
0.284
(+)-8'-methylacetylene-abscisic acid
-
pH 7.6, 30°C
0.122
(+)-8'-methylene-abscisate
-
pH 7.6, 30°C
0.0011
(+)-8'-propargyl-abscisate
-
pH 7.6, 30°C
0.0055
(+)-9'-allyl-abscisate
-
pH 7.6, 30°C
0.00027
(+)-9'-propargyl-abscisate
-
pH 7.6, 30°C
0.056
(-)-8'-propargyl-abscisate
-
pH 7.6, 30°C
0.0135
(-)-9'-propargyl-abscisate
-
pH 7.6, 30°C
0.027
(1'R)-(-)-4'-deoxo-abscisic acid
-
pH 7.2-7.3, 30°C
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
-
-
0.00016
6-nor-(+)-S-abscisate
-
pH 7.25, 30°C
0.00071
8',8',8'-trifluoro-(+)-S-abscisate
-
pH 7.25, 30°C
0.00017
8',8'-difluoro-(+)-S-abscisate
-
pH 7.25, 30°C
0.00027
8'-fluoro-(+)-S-abscisate
-
pH 7.25, 30°C
0.00094
8'-methyl-(+)-S-abscisate
-
pH 7.25, 30°C
0.00543
8'-methylene-(+)-S-abscisate
-
pH 7.25, 30°C
0.00106
9',9',9'-trifluoro-(+)-S-abscisate
-
pH 7.25, 30°C
0.00025
9',9'-difluoro-(+)-S-abscisate
-
pH 7.25, 30°C
0.00078
9'-fluoro-(+)-S-abscisate
-
pH 7.25, 30°C
0.00429
9'-methyl-(+)-S-abscisate
-
pH 7.25, 30°C
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
0.0027
S-(+)-uniconazole
-
pH 7.2-7.3, 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
0.034
UNI-H
-
pH 7.2-7.3, 30°C, recombinant enzyme
0.0086
UNI-OMe
-
pH 7.2-7.3, 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.046
(1E,3R)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
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
0.0013
(1E,3S)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
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
0.0077
(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
Arabidopsis thaliana
pH 7.6, 22°C, recombinant isozyme CYP707A9
0.0023
(E)-1-(4-chlorophenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
0.028 - 0.058
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazine
0.009
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
0.0032
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-[1,2,4]triazolo[5,1-c][1,4]oxazin-8-ol
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
0.078
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-[1,2,4]triazolo[5,1-c][1,4]oxazine
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
0.0078
R-(+)-E-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
0.012
R-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
0.00018
S-(+)-E-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
0.0082
S-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[5,1-c][1,4]oxazine
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
additional information
additional information
-
0.028
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazine
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
0.058
(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazine
Oryza sativa
-
rice seedling, growth of second leaf sheath after 7 days in inhibitor medium
additional information
additional information
Malus sylvestris
-
3R-isomer abscinazole-F1 (3R-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol) has no growth-retardant effect on apple seedlings but induces stomatal closure and drought tolerance during dehydration at concentrations of 10, 50, and 100 microM (spray treatment) in contrast to uniconazole (S-(+)-E-1-(4-chlorophenyl)-4,4-dimethyl-2-(1,2,4-triazo-1-yl)-1-penten-3-ol) which has growth-retardant effects
-
additional information
additional information
Oryza sativa
-
no inhibition of rice seedling growth (second leaf sheath length) with (E)-6-tert-butyl-5-(4-chlorobenzylidene)-5Himidazo[2,1-c][1,4]oxazin-8(6H)-one, (E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol, 3S-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol, 3R-(E)-6-tert-butyl-5-(4-chlorobenzylidene)-6,8-dihydro-5H-imidazo[2,1-c][1,4]oxazin-8-ol
-
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major site of CYP707A1 and CYP707A3 expression
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low level
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high level
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CYP707A1 transcripts are highly abundant in the silique
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major site of CYP707A1 and CYP707A3 expression
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all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A1, overview
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all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A2, overview
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all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A3, overview
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all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A4, overview
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all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A1, overview
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all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A2, overview
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all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A4, overview
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all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A3, overview
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high expression
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CYP707A2 transcription is much higher than the other CYP707A genes
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CYP707A4 transcription is the lowest of the CYP707A genes
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expression of ABA8ox3 is greatest among the three ABA8ox genes, while ABA8ox1 is hardly detected during germination
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spatiotemporal expression pattern of TaCYP707A1B gene in hexaploid wheat
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CYP707A3 plays a major role in regulating abscisic acid levels, whereas CYP707A1 plays a minor role in regulating abscisic acid levels in shoots
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additional information
isozymes AhCYP707A1 and AhCYP707A2 are expressed ubiquitously in peanut roots, stems, and leaves with different transcript accumulation levels, including the higher expression of AhCYP707A1 in roots
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additional information
isozymes AhCYP707A1 and AhCYP707A2 are expressed ubiquitously in peanut roots, stems, and leaves with different transcript accumulation levels, including the higher expression of AhCYP707A1 in roots
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additional information
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isozymes AhCYP707A1 and AhCYP707A2 are expressed ubiquitously in peanut roots, stems, and leaves with different transcript accumulation levels, including the higher expression of AhCYP707A1 in roots
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additional information
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after-ripened coleorhiza
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additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A3 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A3 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A3 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A3 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A3 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A3 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A5 id higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A5 id higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A5 id higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A5 id higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A5 id higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A5 id higher at the primary stage and then sharply declines to a lower level at the late stage
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additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A6 is higher at the primary stage and then sharply declines to a lower level at the late stage
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additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A6 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A6 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A6 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A6 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression level of MaCYP707A6 is higher at the primary stage and then sharply declines to a lower level at the late stage
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression levels of MaCYP707A1, is higher at the primary stage and then sharply declines to a lower level at the late stage. The expression of MaCYP707A1 in the fruit quickly declines at treatment with inhibitor uniconazole
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression levels of MaCYP707A1, is higher at the primary stage and then sharply declines to a lower level at the late stage. The expression of MaCYP707A1 in the fruit quickly declines at treatment with inhibitor uniconazole
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression levels of MaCYP707A1, is higher at the primary stage and then sharply declines to a lower level at the late stage. The expression of MaCYP707A1 in the fruit quickly declines at treatment with inhibitor uniconazole
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression levels of MaCYP707A1, is higher at the primary stage and then sharply declines to a lower level at the late stage. The expression of MaCYP707A1 in the fruit quickly declines at treatment with inhibitor uniconazole
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression levels of MaCYP707A1, is higher at the primary stage and then sharply declines to a lower level at the late stage. The expression of MaCYP707A1 in the fruit quickly declines at treatment with inhibitor uniconazole
brenda
additional information
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview. During fruit development, the expression levels of MaCYP707A1, is higher at the primary stage and then sharply declines to a lower level at the late stage. The expression of MaCYP707A1 in the fruit quickly declines at treatment with inhibitor uniconazole
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additional information
high level in plant placenta
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additional information
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high level in plant placenta
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Cutler, A.J.; Rose, P.A.; Squires, T.M.; Loewen, M.K.; Shaw, A.C.; Quail, J.W.; Krochko, J.E.; Abrams, S.R.
Inhibitors of abscisic acid 8'-hydroxylase
Biochemistry
39
13614-13624
2000
Zea mays
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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
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Rose, P.A.; Cutler, A.J.; Irvine, N.M.; Shaw, A.C.; Squires, T.M.; Loewen, M.K.; Abrams, S.R.
8'-Acetylene ABA: an irreversible inhibitor of ABA 8'-hydroxylase
Bioorg. Med. Chem. Lett.
7
2543-2546
1997
Zea mays
-
brenda
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
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Cutler, A.J.; Squires, T.M.; Loewen, M.K.; Balsevich, J.J.
Induction of (+)-abscisic acid 8' hydroxylase by (+)-abscisic acid in cultured maize cells
J. Exp. Bot.
48
1787-1795
1997
Zea mays
-
brenda
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
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Krochko, J.E.; Abrams, G.D.; Loewen, M.K.; Abrams, S.R.; Cutler, A.J.
(+)-Abscisic acid 8'-hydroxylase is a cytochrome P450 monooxygenase
Plant Physiol.
118
849-860
1998
Zea mays
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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
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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
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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
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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
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Saika, H.; Okamoto, M.; Miyoshi, K.; Kushiro, T.; Shinoda, S.; Jikumaru, Y.; Fujimoto, M.; Arikawa, T.; Takahashi, H.; Ando, M.; Arimura, S.; Miyao, A.; Hirochika, H.; Kamiya, Y.; Tsutsumi, N.; Nambara, E.; Nakazono, M.
Ethylene promotes submergence-induced expression of OsABA8ox1, a gene that encodes ABA 8-hydroxylase in rice
Plant Cell Physiol.
48
287-298
2007
Oryza sativa (Q05JG2), Oryza sativa (Q0J185), Oryza sativa (Q6ZDE3), Oryza sativa
brenda
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
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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
brenda
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)
brenda
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
brenda
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)
brenda
Zhu, G.; Ye, N.; Zhang, J.
Glucose-induced delay of seed germination in rice is mediated by the suppression of ABA catabolism rather than an enhancement of ABA biosynthesis
Plant Cell Physiol.
50
644-651
2009
Oryza sativa
brenda
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
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Barrero, J.M.; Talbot, M.J.; White, R.G.; Jacobsen, J.V.; Gubler, F.
Anatomical and transcriptomic studies of the coleorhiza reveal the importance of this tissue in regulating dormancy in barley
Plant Physiol.
150
1006-1021
2009
Hordeum vulgare
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Mialoundama, A.S.; Heintz, D.; Debayle, D.; Rahier, A.; Camara, B.; Bouvier, F.
Abscisic acid negatively regulates elicitor-induced synthesis of capsidiol in wild tobacco
Plant Physiol.
150
1556-1566
2009
Nicotiana plumbaginifolia
brenda
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
brenda
Nitsch, L.M.; Oplaat, C.; Feron, R.; Ma, Q.; Wolters-Arts, M.; Hedden, P.; Mariani, C.; Vriezen, W.H.
Abscisic acid levels in tomato ovaries are regulated by LeNCED1 and SlCYP707A1
Planta
229
1335-1346
2009
Solanum lycopersicum (A9QNE7), Solanum lycopersicum
brenda
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
brenda
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