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Information on EC 1.14.14.137 - (+)-abscisic acid 8'-hydroxylase
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1.14.14.137 (+)-abscisic acid 8'-hydroxylaseIUBMB Comments
A heme-thiolate protein (P-450). 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. Other enzymes involved in the abscisic-acid biosynthesis pathway are EC 1.1.1.288 (xanthoxin dehydrogenase), EC 1.2.3.14 (abscisic-aldehyde oxidase) and EC 1.13.11.51 (9-cis-epoxycarotenoid dioxygenase).
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Word Map
- 1.14.14.137
- epoxide
-
dormancy
-
9-cis-epoxycarotenoid
-
tyr113his
-
his139arg
-
phaseic
-
8'-hydroxylation
-
after-ripening
-
pre-harvest
-
+-abscisic
- diniconazole
- agriculture
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
aba 8'-hydroxylase, cyp707a, cyp707a2, cyp707a3, cyp707a1, ahcyp707a1, taaba8'oh1, aba-8'-hydroxylase, ahcyp707a2, abscisic acid 8'-hydroxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(+)-abscisic acid 8'-hydroxylase
ABA 8'-hydroxylase
abscisic acid 8'-hydroxylase
CYP707A
CYP707A1
CYP707A2
CYP707A3
CYP707A4
abscisic acid 8'-hydroxylase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2 = 8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
abscisate,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (8'-hydroxylating)
A heme-thiolate protein (P-450). 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. Other enzymes involved in the abscisic-acid biosynthesis pathway are EC 1.1.1.288 (xanthoxin dehydrogenase), EC 1.2.3.14 (abscisic-aldehyde oxidase) and EC 1.13.11.51 (9-cis-epoxycarotenoid dioxygenase).
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CAS REGISTRY NUMBER
COMMENTARY
153190-37-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
phaseic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+-)-3'-methyl-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
32% of the activity with (+)-S-abscisate
-
-
?
(+-)-abscisic acid-3'-thio-n-butyl thiol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
2% of the activity with (+)-S-abscisate
-
-
?
(1'S)-(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is active with the naturally occuring (1'S)-(+)-enantiomer, but not with the naturally not occuring enantiomer (1'R)-(-)-abscisic acid. The C4'-oxo moiety coupled to the C2'-C3'-double bond in the key functional group for the enzyme to distinguish (1'S)-(+)-abscisic acid from (1'R)-(-)-abscisic acid
-
-
?
(2Z,4E)-5-[(1R,6R)-1-hydroxy-2,2,6-trimethylcyclohexyl]penta-2,4-dienoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
a structural analogue of abscisic acid lacking the C6 methyl group and the alpha,beta-unsaturated carbonyl in the six-membered ring, synthesis, overview. Both enantiomers of this analogue bind to the enzyme
-
-
?
(2Z,4E)-5-[(1S,6S)-1-hydroxy-2,2,6-trimethylcyclohexyl]penta-2,4-dienoic acid + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
a structural analogue of abscisic acid lacking the C6 methyl group and the alpha,beta-unsaturated carbonyl in the six-membered ring, synthesis, overview. Both enantiomers of this analogue bind to the enzyme
-
-
?
(S)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
1'-deoxy-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
99% of the activity with (+)-S-abscisate
-
-
?
1'-deoxy-1'-fluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
94% of the activity with (+)-S-abscisate
-
-
?
2'alpha,3'alpha-dihydro-2'alpha,3'alpha-epoxy-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
19% of the activity with (+)-S-abscisate
-
-
?
3'-bromo-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
5% of the activity with (+)-S-abscisate
-
-
?
3'-chloro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
19% of the activity with (+)-S-abscisate
-
-
?
3'-fluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
68% of the activity with (+)-S-abscisate
-
-
?
6-nor-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
60% of the activity with (+)-S-abscisate
-
-
?
7'-methyl-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
15% of the activity with (+)-S-abscisate
-
-
?
7'-nor-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
15% of the activity with (+)-S-abscisate
-
-
?
8'-fluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
11% of the activity with (+)-S-abscisate
-
-
?
8'-methylene-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
4% of the activity with (+)-S-abscisate
-
-
?
9',9'-difluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
9',9'-difluoro-8'-hydroxy-(+)-S-abscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
3% of the activity with (+)-S-abscisate
-
-
?
9'-fluoro-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
33% of the activity with (+)-S-abscisate
-
-
?
9'-methyl-(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
-
3% of the activity with (+)-S-abscisate
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
key enzyme in abscisic acid catabolism
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
isoform CYP707A3 is specific for (+)-isomer
isoform CYP707A3, no hydroxylation at 7’ position
-
?
(+)-S-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
for inhibitor studies the decrease in production of phaseic acid is measured
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
-
isomerisation of 8’-hydroxy-abscisic acid to phaseic acid is not catalyzed by enzyme
-
-
-
additional information
?
-
-
substrate recognition strictly requires the 6'-methyl groups
-
-
-
additional information
?
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
-
additional information
?
-
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
-
additional information
?
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
-
additional information
?
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
-
additional information
?
-
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
phaseic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(1'S)-(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is active with the naturally occuring (1'S)-(+)-enantiomer, but not with the naturally not occuring enantiomer (1'R)-(-)-abscisic acid. The C4'-oxo moiety coupled to the C2'-C3'-double bond in the key functional group for the enzyme to distinguish (1'S)-(+)-abscisic acid from (1'R)-(-)-abscisic acid
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
U6NHS3, U6NJF1
-
-
-
?
(+)-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
F1T0M7
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
W9S4Y0, W9SAM9, W9SJA3, W9SMK4, W9SPF5, W9ST04
-
-
-
?
(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
B8QBY2
-
-
-
?
(+)-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
E3TB04, E3TB05, E3TB06, E3TB07
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
E3TB04, E3TB05, E3TB06, E3TB07
-
-
-
?
(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
B8QBY2, R4WUP9, R4X4I5
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
S-(+)-abscisic acid + [reduced NADPH-hemoprotein reductase] + O2
8'-hydroxyabscisic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
O81077
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
?
-
Q05JG2
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
?
-
Q0J185
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
?
-
Q6ZDE3
a rapid decrease of the plant hormone abscisic acid to its oxidized derivative phaseic acid under submergence is a prerequisite for the enhanced elongation of submerged shoots of rice, ethylene has a regulatory role, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._; 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._; 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._; 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._; 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._; A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
-
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._; A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
-
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+-)-abscisic acid-3'-thio-n-butyl thiol
-
competitive, 51% inhibition at 0.05 mM
(1'R,2'R)-(-)-2',3'-dihydro-4'-deoxo-abscisic acid
-
competitive inhibition
(1'S*,2'S*,6'S*)-(+-)-6-nor-2',3'-dihydro-4'-deoxo-8',8'-difluoro-abscisate
-
50% inhibition at 0.00063 mM
(1'S*,2'S*,6'S*)-(+-)-6-nor-2',3'-dihydro-4'-deoxo-abscisate
-
50% inhibition at 0.00091 mM
(1E)-1-(4-chlorophenyl)-2-[2-(hydroxymethyl)-1H-imidazol-1-yl]-4,4-dimethylpent-1-en-3-ol
-
31% inhibition at 0.01 mM
(1E)-1-(4-chlorophenyl)-2-[5-(hydroxymethyl)-1H-imidazol-1-yl]-4,4-dimethylpent-1-en-3-ol
-
95% inhibition at 0.01 mM
(1E)-1-[4-(4-butyl-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
(1E)-1-[4-(4-heptyl-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 96%
(1E)-1-[4-[4-(1-hydroxybutyl)-1H-1,2,3-triazol-1-yl]phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 92%
(1E)-1-[4-[4-(1-hydroxyethyl)-1H-1,2,3-triazol-1-yl]phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 77%
(1E)-1-[4-[4-(hydroxymethyl)-1H-1,2,3-triazol-1-yl]phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 83%
(1E)-4,4-dimethyl-1-[4-(4-nonyl-1H-1,2,3-triazol-1-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 100%
(1E)-4,4-dimethyl-1-[4-(4-pentadecyl-1H-1,2,3-triazol-1-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 54%
(1E)-4,4-dimethyl-1-[4-(4-propyl-1H-1,2,3-triazol-1-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
0.01 mM, inhibits by 92%
(1E)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)-1-[4-(4-tridecyl-1H-1,2,3-triazol-1-yl)phenyl]pent-1-en-3-ol
-
0.01 mM, inhibits by 95%
(1E)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)-1-[4-(4-undecyl-1H-1,2,3-triazol-1-yl)phenyl]pent-1-en-3-ol
-
0.01 mM, inhibits by 100%
(1E,3R)-1-(3-[3-[2-(2-butoxyethoxy)ethoxy]prop-1-yn-1-yl]phenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
-
(1E,3R)-1-(4-[3-[2-(2-butoxyethoxy)ethoxy]prop-1-yn-1-yl]phenyl)-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
-
(1E,3R)-1-[4-(4-[[2-(2-butoxyethoxy)ethoxy]methyl]-1H-1,2,3-triazol-1-yl)phenyl]-4,4-dimethyl-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
(1E,3R)-4,4-dimethyl-1-[3-[4-(2,5,8,11-tetraoxadodecan-1-yl)-1H-1,2,3-triazol-1-yl]phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
strong and selective inhibitor, effects of the inhibitor on stomatal closure and drought tolerance, overview
(1E,3R)-4,4-dimethyl-1-[4-(2,5,8,11-tetraoxatetradec-13-yn-14-yl)phenyl]-2-(1H-1,2,4-triazol-1-yl)pent-1-en-3-ol
-
-
(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
(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)-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
(Z)-1-(1-(4-chlorophenyl)-4,4-dimethylpent-1-en-2-yl)-1H-imidazole
-
-
-
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
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
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
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
-
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
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
additional information
-
the mRNA level of OsABA8ox-2 does not increase under submergence culture conditions; the mRNA level of OsABA8ox-3 does not increase under submergence culture conditions; treatment of aerobic seedlings with ethylene and its precursor 1-aminocyclopropane-1-carboxylate rapidly induces the expression of OsABA8ox1, which is suppressed by 1-methylcyclopropene, an inhibitor of ethylene action. the mRNA level of OsABA8ox1 increases dramatically within 1 h under submergence culture conditions
-
additional information
the mRNA level of OsABA8ox-2 does not increase under submergence culture conditions; the mRNA level of OsABA8ox-3 does not increase under submergence culture conditions; treatment of aerobic seedlings with ethylene and its precursor 1-aminocyclopropane-1-carboxylate rapidly induces the expression of OsABA8ox1, which is suppressed by 1-methylcyclopropene, an inhibitor of ethylene action. the mRNA level of OsABA8ox1 increases dramatically within 1 h under submergence culture conditions
-
additional information
the mRNA level of OsABA8ox-2 does not increase under submergence culture conditions; the mRNA level of OsABA8ox-3 does not increase under submergence culture conditions; treatment of aerobic seedlings with ethylene and its precursor 1-aminocyclopropane-1-carboxylate rapidly induces the expression of OsABA8ox1, which is suppressed by 1-methylcyclopropene, an inhibitor of ethylene action. the mRNA level of OsABA8ox1 increases dramatically within 1 h under submergence culture conditions
-
additional information
the mRNA level of OsABA8ox-2 does not increase under submergence culture conditions; the mRNA level of OsABA8ox-3 does not increase under submergence culture conditions; treatment of aerobic seedlings with ethylene and its precursor 1-aminocyclopropane-1-carboxylate rapidly induces the expression of OsABA8ox1, which is suppressed by 1-methylcyclopropene, an inhibitor of ethylene action. the mRNA level of OsABA8ox1 increases dramatically within 1 h under submergence culture conditions
-
additional information
CYP707A1 is not affected by gibberellin 3 treatment, in contrast to pollination, which has a stimulating effect
-
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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
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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
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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
0.046
(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
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 7.3
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Jialing No. 40, grown in the mulberry garden of Southwest University, Chongqing, China, and cv. Guiyou No. 62
UniProt
brenda
-
-
-
brenda
about 3fold induction by (+)- or (-)-abscisate and about 15fold induction by 8’,8’,8’-trifluoro-abscisate
-
-
brenda
expression in baculovirus system, isoforms CYP707A1, CYP707A3, CYP707A4
-
-
brenda
rice cultivar Nipponbare, length of second leaf sheath of 7 days old seedlings grown in test solution
-
-
brenda
CYP707A1; four cDNAs CYP707A1-CYP707A4 encoding ABA 8'-hydroxylase
E3TB04
UniProt
brenda
CYP707A2; four cDNAs CYP707A1-CYP707A4 encoding ABA 8'-hydroxylase
E3TB05
UniProt
brenda
CYP707A3; four cDNAs CYP707A1-CYP707A4 encoding ABA 8'-hydroxylase
UniProt
brenda
CYP707A4; four cDNAs CYP707A1-CYP707A4 encoding ABA 8'-hydroxylase
UniProt
brenda
CYP707A1; four cDNAs CYP707A1-CYP707A4 encoding ABA 8'-hydroxylase
E3TB04
UniProt
brenda
CYP707A2; four cDNAs CYP707A1-CYP707A4 encoding ABA 8'-hydroxylase
E3TB05
UniProt
brenda
CYP707A3; four cDNAs CYP707A1-CYP707A4 encoding ABA 8'-hydroxylase
UniProt
brenda
CYP707A4; four cDNAs CYP707A1-CYP707A4 encoding ABA 8'-hydroxylase
UniProt
brenda
isoform TaABA8'OH1-A; cultivars Chinese Spring, Norin 61, Tamaizumi, TM1833, Hayakomugi, and Shinchunaga
UniProt
brenda
isoform TaABA8'OH1-B; cultivars Chinese Spring, Norin 61, Tamaizumi, TM1833, Hayakomugi, and Shinchunaga
UniProt
brenda
isoform TaABA8'OH1-D; cultivars Chinese Spring, Norin 61, Tamaizumi, TM1833, Hayakomugi, and Shinchunaga
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
CYP707A1 transcripts are highly abundant in the silique
brenda
additional information
all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A1, overview; all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A2, overview; all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A3, overview; all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A4, overview
brenda
-
all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A1, overview; all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A2, overview; all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A3, overview; all four CYP707As are expressed at varying intensities throughout sweet cherry fruit development, expression pattern of CYP707A4, overview
-
brenda
CYP707A2 transcription is much higher than the other CYP707A genes; CYP707A4 transcription is the lowest of the CYP707A genes
brenda
-
expression of ABA8ox3 is greatest among the three ABA8ox genes, while ABA8ox1 is hardly detected during germination
brenda
spatiotemporal expression pattern of TaCYP707A1B gene in hexaploid wheat
brenda
-
CYP707A3 plays a major role in regulating abscisic acid levels, whereas CYP707A1 plays a minor role in regulating abscisic acid levels in shoots
brenda
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; 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
brenda
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; 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
brenda
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; 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
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; expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview; 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; 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; 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; 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; expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview; 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; 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; 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; 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
W9SJA3
expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview; expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview; 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; 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; 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; 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; expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview; 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; 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; 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; 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; expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview; 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; 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; 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; 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; expression profiles of isozyme genes during fruit development and under stress conditions are analyzed by quantitative reverse transcriptase polymerase chain reaction, detailed overview; 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; 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; 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; 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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
deletion in TaABA8'OH1 leads to increased abscisic acid level in the spikes and therefore increased drought sensitivity, phenotype, overview. Germination of the cyp707a1 cyp707a2 seeds appear not to be affected by the cold treatment, which induces early germination phenotype in the control wild-type and TaCYP707A1B-C seeds of transgenic Arabidospis thaliana, similar rate of transpirational water loss between the wild-type and mutant TaNCED2A-OE, cyp707a1/cyp707a2 and TaCYP707A1B-C lines during the entire period of dehydration
metabolism
physiological function
evolution
the enzyme belongs to the cytochrome P450 CYP707A family. The expressions of isozymes AhCYP707A1 and AhCYP707A2 play an important role in abscisic acid catabolism in peanut, particularly in response to osmotic stress; the enzyme belongs to the cytochrome P450 CYP707A family. The expressions of isozymes AhCYP707A1 and AhCYP707A2 play an important role in abscisic acid catabolism in peanut, particularly in response to osmotic stress
metabolism
-
ABA 8'-hydroxylase is the major and key P450 enzyme in the abscisic acid catabolism
metabolism
-
key enzyme in the catabolism of abscisic acid (plant hormone involved in stress tolerance, seed dormancy, and other physiological events)
metabolism
-
key enzyme in the catabolism of abscisic acid (plant hormone involved in stress tolerance, seed dormancy, and other physiological events)
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 a key enzyme in the oxidative catabolism of abscisic acid. Endogenous abscisic acid content is modulated by a dynamic balance between biosynthesis and catabolism, which are regulated by NCED1 and CYP707As transcripts, respectively, during fruit maturation and under stress conditions, overview; ABA 8'-hydroxylase is a key enzyme in the oxidative catabolism of abscisic acid. Endogenous abscisic acid content is modulated by a dynamic balance between biosynthesis and catabolism, which are regulated by NCED1 and CYP707As transcripts, respectively, during fruit maturation and under stress conditions, overview; ABA 8'-hydroxylase is a key enzyme in the oxidative catabolism of abscisic acid. Endogenous abscisic acid content is modulated by a dynamic balance between biosynthesis and catabolism, which are regulated by NCED1 and CYP707As transcripts, respectively, during fruit maturation and under stress conditions, overview; ABA 8'-hydroxylase is a key enzyme in the oxidative catabolism of abscisic acid. Endogenous abscisic acid content is modulated by a dynamic balance between biosynthesis and catabolism, which are regulated by NCED1 and CYP707As transcripts, respectively, during fruit maturation and under stress conditions, overview. Application of abscisic acid induces the expression of CYP707A1-CYP707A3 as well as PacNCED1, encoding 9-cis-epoxycarotenoid dioxygenase, but downregulates the CYP707A4 transcript level. Expressions of CYP707A1 and CYP707A3 are strongly increased by water stress, while no significant differences in CYP707A2 and CYP707A4 expression are observed between dehydrated and control fruits
metabolism
hydroxylation at the 8'-position of abscisic acid appears to be the key step of abscisic acid catabolism, and this reaction is catalyzed by ABA 8'-hydroxylase
metabolism
-
comparison of abscisic acid (ABA) metabolism and signaling in roots of flooded and water stressed plants of Carrizo citrange reveals that the hormone depletion is linked to the upregulation of CsAOG, involved in abscisic acid glycosyl ester (ABAGE) synthesis, and to a moderate induction of catabolism (CsCYP707A, an ABA 8'-hydroxylase) and buildup of dehydrophaseic acid (DPA). Drought strongly induces both ABA biosynthesis and catabolism (CsNCED1, 9-cis-neoxanthin epoxycarotenoid dioxygenase1, and CsCYP707A) rendering a significant hormone accumulation. In roots of flooded plants, restoration of control abscisic acid levels after stress release is associated to the upregulation of CsBGLU18 (an abscisic acid beta--glycosidase) that cleaves ABAGE
metabolism
biosynthesis and catabolism of abscisic acid (ABA) in plants are primarily regulated by 9-cis-epoxycarotenoid dioxygenases (NCEDs) and ABA 8'-hydroxylase (ABA8'OH), respectively
metabolism
-
ABA 8'-hydroxylase is a key enzyme in the oxidative catabolism of abscisic acid. Endogenous abscisic acid content is modulated by a dynamic balance between biosynthesis and catabolism, which are regulated by NCED1 and CYP707As transcripts, respectively, during fruit maturation and under stress conditions, overview; ABA 8'-hydroxylase is a key enzyme in the oxidative catabolism of abscisic acid. Endogenous abscisic acid content is modulated by a dynamic balance between biosynthesis and catabolism, which are regulated by NCED1 and CYP707As transcripts, respectively, during fruit maturation and under stress conditions, overview; ABA 8'-hydroxylase is a key enzyme in the oxidative catabolism of abscisic acid. Endogenous abscisic acid content is modulated by a dynamic balance between biosynthesis and catabolism, which are regulated by NCED1 and CYP707As transcripts, respectively, during fruit maturation and under stress conditions, overview; ABA 8'-hydroxylase is a key enzyme in the oxidative catabolism of abscisic acid. Endogenous abscisic acid content is modulated by a dynamic balance between biosynthesis and catabolism, which are regulated by NCED1 and CYP707As transcripts, respectively, during fruit maturation and under stress conditions, overview. Application of abscisic acid induces the expression of CYP707A1-CYP707A3 as well as PacNCED1, encoding 9-cis-epoxycarotenoid dioxygenase, but downregulates the CYP707A4 transcript level. Expressions of CYP707A1 and CYP707A3 are strongly increased by water stress, while no significant differences in CYP707A2 and CYP707A4 expression are observed between dehydrated and control fruits
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physiological function
-
ABA 8'-hydroxylase is the major and key P450 enzyme in the abscisic acid catabolism
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; 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; 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
-
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
-
important role for ABA8'OH-1 during early germination and in controlling dormancy in the coleorhiza
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
CYP707A1 is most important for abscisic acid catabolism in pollinated ovaries. Transgenic plants, overexpressing CYP707A1, have reduced abscisic acid levels and exhibit abscisic acid-deficient phenotypes. Initiation of adventitious root growth on the stem of the CYP707A1 overexpression plants
physiological function
all four CYP707As are expressed at varying intensities throughout fruit development and appear to play overlapping roles in abscisic acid catabolism throughout sweet cherry fruit development; all four CYP707As are expressed at varying intensities throughout fruit development and appear to play overlapping roles in abscisic acid catabolism throughout sweet cherry fruit development; all four CYP707As are expressed at varying intensities throughout fruit development and appear to play overlapping roles in abscisic acid catabolism throughout sweet cherry fruit development; all four CYP707As are expressed at varying intensities throughout fruit development and appear to play overlapping roles in abscisic acid catabolism throughout sweet cherry fruit development
physiological function
hydroxylation at the 8'-position of abscisic acid appears to be the key step of abscisic acid catabolism, and this reaction is catalyzed by ABA 8'-hydroxylase
physiological function
-
abscisic acid catabolism is represented by the induction of abscisic acid 8'-hydroxylase CYP707A1, which catalyzes the production of phaseic acid
physiological function
the abscisic acid catabolic enzyme ABA8'OH is encoded by members of the cytochrome P450 monooxygenase 707A (CYP707A) gene family, which play important roles in regulating seed abscisic acid level during seed development and therefore dormancy. Role of the B genome copy of the cytochrome P450 monooxygenase 707A1 (CYP707A1) gene of hexaploid wheat (TaCYP707A1B), which encodes ABA8'OH, in regulating seed dormancy and leaf dehydration tolerance
physiological function
abscisic acid (ABA) catabolism is one of the determinants of endogenous ABA levels affecting numerous aspects of plant growth and abiotic-stress responses. The major ABA catabolic pathway is triggered by ABA 8’-hydroxylation catalysed by ABA 8'-hydroxylase; abscisic acid (ABA) catabolism is one of the determinants of endogenous ABA levels affecting numerous aspects of plant growth and abiotic-stress responses. The major ABA catabolic pathway is triggered by ABA 8’-hydroxylation catalysed by ABA 8'-hydroxylase
physiological function
-
all four CYP707As are expressed at varying intensities throughout fruit development and appear to play overlapping roles in abscisic acid catabolism throughout sweet cherry fruit development; all four CYP707As are expressed at varying intensities throughout fruit development and appear to play overlapping roles in abscisic acid catabolism throughout sweet cherry fruit development; all four CYP707As are expressed at varying intensities throughout fruit development and appear to play overlapping roles in abscisic acid catabolism throughout sweet cherry fruit development; all four CYP707As are expressed at varying intensities throughout fruit development and appear to play overlapping roles in abscisic acid catabolism throughout sweet cherry fruit development
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
K9XZ60_STAC7
Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437)
444
0
50555
TrEMBL
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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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 53390, sequence calculation; x * 55060, sequence calculation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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CYP707A2 knockout mutant, hyperdormancy in seeds, accumulates 6fold higher levels of abscisic acid than wild-type
additional information
generation of Tricticum aestivum mutant lines cyp707a1, cyp707a2, and cyp707a1/cyp707a2, phenotypes, overview
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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
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
a truncated CYP707A3 (707A3d28), which lacks the putative membrane-spanning segment of the N-terminus (residues 3–28) coexpressed in Escherichia coli strain BL21 with Arabidopsis P450 reductase
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cDNA CYP707A1, DNA and amino acid sequence determination and analysis, phylogenetic tree; cDNA CYP707A2, DNA and amino acid sequence determination and analysis, phylogenetic tree; cDNA CYP707A3, DNA and amino acid sequence determination and analysis, phylogenetic tree; cDNA CYP707A4, DNA and amino acid sequence determination and analysis, phylogenetic tree
coding region (base 6-1,478) amplified and cloned in the Gateway entry vector pENTR/D-TOPO. CYP707A1 coding region recombined between the Cauliflower Mosaic Virus 35S promoter in the pGD625 vector and the NOPALINE SYNTHASE terminator. Transgenic plants generated by Agrobacterium tumefaciens-mediated transformation
CYP707A3, coexpression with Arabidopsis thaliana P450 reductase ATR2 in Escherichia coli
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expression in baculovirus system, isoforms CYP707A1, CYP707A3, CYP707A4
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gene CYP707A1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, real-time quantitative RT-PCR enzyme expression analysis. Functional expression of AhCYP707A1 cDNA in yeast with recombinant AhCYP707A1 ABA 8’-hydroxylase catalytic activity in the microsomal fractions; gene CYP707A2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, real-time quantitative RT-PCR enzyme expression analysis
gene MnCYP707A1, DNA and amino acid sequence determination and analysis, isozymes sequence comparions and phylogenetic analysis, quatitative RT-PCR enzyme expression analysis; gene MnCYP707A2, DNA and amino acid sequence determination and analysis, isozymes sequence comparions and phylogenetic analysis, quatitative RT-PCR enzyme expression analysis; gene MnCYP707A3, DNA and amino acid sequence determination and analysis, isozymes sequence comparions and phylogenetic analysis, quatitative RT-PCR enzyme expression analysis; gene MnCYP707A4, DNA and amino acid sequence determination and analysis, isozymes sequence comparions and phylogenetic analysis, quatitative RT-PCR enzyme expression analysis; gene MnCYP707A5, DNA and amino acid sequence determination and analysis, isozymes sequence comparions and phylogenetic analysis, quatitative RT-PCR enzyme expression analysis; gene MnCYP707A6, DNA and amino acid sequence determination and analysis, isozymes sequence comparions and phylogenetic analysis, quatitative RT-PCR enzyme expression analysis
gene TaCYP707A1B, cloning from seedlings, expression analysis, ectopic expression of genes TaNCED2A and TaCYP707A1B in Arabidopsis thaliana Col-0 ecotype, using Agrobacterium tumefaciens AGL1 transformation method, results in altered seed abscisic acid level and dormancy with no effect on leaf abscisic acid content and transpirational water loss, phenotypes, overview. Quantitative and semiquantitative real-time and RT-PCR expression analysis
genes CYP707A1 and CYP707A2, quantitative real-time RT-PCR expression analysis
leaves from wild-type plants transfected with the expression plasmid NpABAH
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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
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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
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three genes OsABA8ox1, -2 and -3, expression analysis, expression of gene OsABA8ox1 in Saccharomyces cerevisiae microsomes, expression of gene OsABA8ox1 as GFP-tagged protein in Allium cepa cells in the endoplasmic reticulum; three genes OsABA8ox1, -2 and -3, expression analysis, expression of gene OsABA8ox1 in Saccharomyces cerevisiae microsomes, expression of gene OsABA8ox1 as GFP-tagged protein in Allium cepa cells in the endoplasmic reticulum; three genes OsABA8ox1, -2 and -3, expression analysis, expression of gene OsABA8ox1 in Saccharomyces cerevisiae microsomes, expression of gene OsABA8ox1 as GFP-tagged protein in Allium cepa cells in the endoplasmic reticulum
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3 h after tuber wounding, expression of isoforms CYP707A1 and CYP707A3 is increased more than 6fold and more than 69fold, respectively
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ABA8'OH-1 is up-regulated in after-ripened tissues, highest expression in after-ripened coleorhiza
-
application of abscisic acid induces the expression of CYP707A1. Expression of CYP707A1 is strongly increased by water stress; application of abscisic acid induces the expression of CYP707A2. Expression of CYP707A2 is not significantly altered in dehydrated fruits compared to control fruits; application of abscisic acid induces the expression of CYP707A3. Expression of CYP707A3 is strongly increased by water stress
application of abscisic acid suppresses the expression of CYP707A2. Expression of CYP707A2 is not significantly altered in dehydrated fruits compared to control fruits
concomitant with the production of capsidiol is the induction of ABA 8'-hydroxylase in elicited plants. Expression of ABAH is induced in wild-type plants and in Npaba2 and Npaba1 mutants after cellulase treatment at time points corresponding to the expression of 5-epiaristolochene synthase and 5-epi-aristolochene hydroxylase and capsidiol synthesis
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drought represses CsCYP707A expression 11.1 times with respect to control values. CsCYP707A1 expression slightly increases in roots of citrus subjected to soil flooding whereas it strongly decreases in response to water deficit
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expression of ABA8ox genes, especially ABA8ox2 and ABA8ox3, is sensitively suppressed in the presence of exogenously supplied glucose, leading to delay of germination
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expression of ABA8ox3 encoding ABA 8'-hydroxylase is significantly increased during the first 6 h of imbibition
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expression of AhCYP707A2 is significantly up-regulated by 20% PEG 6000 or 250 mmol/l NaCl in peanut roots, stems, and leaves, whereas the up-regulation of AhCYP707A1 transcript level by PEG 6000 or NaCl is observed only in roots instead of leaves and stems; expression of AhCYP707A2 is significantly up-regulated by 20% PEG 6000 or 250 mmol/l NaCl in peanut roots, stems, and leaves, whereas the up-regulation of AhCYP707A1 transcript level by PEG 6000 or NaCl is observed only in roots instead of leaves and stems
moderate induction of CsCYP707A by depletion of abscisic acid, strong induction by drought of both abscisic acid biosynthesis and catabolism, i.e. CsNCED1, 9-cis-neoxanthin epoxycarotenoid dioxygenase1, and CsCYP707A. Soil flooding induces a 2.5fold increase in CsCYP707A expression with respect to control values. Stress release in soil-flooded seedlings reduces CsCYP707A expression to control values but rewatering induces its expression up to 4.2fold. CsCYP707A1 expression slightly increases in roots of citrus subjected to soil flooding whereas it strongly decreases in response to water deficit
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mRNA concentration of CYP707A1 strongly increases after pollination in whole ovaries. CYP707A1 mRNA levels are several 100fold upregulated after pollination, specifically in ovules/placenta and not in pericarp. CYP707A1 overexpression line has approximately 45fold higher mRNA levels than wild-type
susceptibility to osmotic stress and the resistance to salt ions in peanut seedlings of CYP707A isozymes. The osmotic stress instead of ionic stress affects the expression of those genes and the biosynthesis of abscisic acid in peanut. No effect by Li+; susceptibility to osmotic stress and the resistance to salt ions in peanut seedlings of CYP707A isozymes. The osmotic stress instead of ionic stress affects the expression of those genes and the biosynthesis of abscisic acid in peanut. No effect by Li+
the enzyme is highly expressed during seed development; the enzyme is highly expressed during seed development; the enzyme is highly expressed during seed development
transcription decreases to a lower level after 12 h of imbibition; transcription decreases to a lower level after 12 h of imbibition; transcription decreases to a lower level after 12 h of imbibition; transcription decreases to a lower level after 12 h of imbibition
transcription increases during the first 6 h of imbibition; transcription increases during the first 6 h of imbibition; transcription increases during the first 6 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
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application of abscisic acid induces the expression of CYP707A1. Expression of CYP707A1 is strongly increased by water stress; application of abscisic acid induces the expression of CYP707A2. Expression of CYP707A2 is not significantly altered in dehydrated fruits compared to control fruits; application of abscisic acid induces the expression of CYP707A3. Expression of CYP707A3 is strongly increased by water stress
application of abscisic acid induces the expression of CYP707A1. Expression of CYP707A1 is strongly increased by water stress; application of abscisic acid induces the expression of CYP707A2. Expression of CYP707A2 is not significantly altered in dehydrated fruits compared to control fruits; application of abscisic acid induces the expression of CYP707A3. Expression of CYP707A3 is strongly increased by water stress
-
-
application of abscisic acid suppresses the expression of CYP707A2. Expression of CYP707A2 is not significantly altered in dehydrated fruits compared to control fruits
application of abscisic acid suppresses the expression of CYP707A2. Expression of CYP707A2 is not significantly altered in dehydrated fruits compared to control fruits
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
introduction of drought tolerance in apple seedlings, the 3R-isomer of the abscisic acid 8'-hydroxylase inhibitor 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)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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
brenda
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
brenda
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
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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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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, Oryza sativa (Q05JG2), Oryza sativa (Q0J185), Oryza sativa (Q6ZDE3)
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
brenda
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
brenda
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
brenda
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
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
brenda
Ren, J.; Sun, L.; Wu, J.; Zhao, S.; Wang, C.; Wang, Y.; Ji, K.; Leng, P.
Cloning and expression analysis of cDNAs for ABA 8'-hydroxylase during sweet cherry fruit maturation and under stress conditions
J. Plant Physiol.
167
1486-1493
2010
Prunus avium (E3TB04), Prunus avium (E3TB05), Prunus avium (E3TB06), Prunus avium (E3TB07), Prunus avium, Prunus avium Hongdeng (E3TB04), Prunus avium Hongdeng (E3TB05), Prunus avium Hongdeng (E3TB06), Prunus avium Hongdeng (E3TB07)
brenda
Chono, M.; Matsunaka, H.; Seki, M.; Fujita, M.; Kiribuchi-Otobe, C.; Oda, S.; Kojima, H.; Kobayashi, D.; Kawakami, N.
Isolation of a wheat (Triticum aestivum L.) mutant in ABA 8-hydroxylase gene: effect of reduced ABA catabolism on germination inhibition under field condition
Breed. Sci.
63
104-115
2013
Triticum aestivum (B8QBY2), Triticum aestivum (R4WUP9), Triticum aestivum (R4X4I5), Triticum aestivum
brenda
Suttle, J.C.; Lulai, E.C.; Huckle, L.L.; Neubauer, J.D.
Wounding of potato tubers induces increases in ABA biosynthesis and catabolism and alters expression of ABA metabolic genes
J. Plant Physiol.
170
560-566
2013
Solanum tuberosum
brenda
Sales, L.; Ohara, H.; Ohkawa, K.; Saito, T.; Todoroki, Y.; Srilaong, V.; Kondo, S.
Salt tolerance in apple seedlings is affected by an inhibitor of ABA 8'-hydroxylase CYP707A
J. Plant Growth Regul.
36
643-650
2017
Malus domestica (F1T0M7)
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brenda
Cai, Y.; Zhu, P.; Liu, C.; Zhao, A.; Yu, J.; Wang, C.; Li, Z.; Huang, P.; Yu, M.
Characterization and expression analysis of cDNAs encoding abscisic acid 8'-hydroxylase during mulberry fruit maturation and under stress conditions
Plant Cell Tissue Organ. Cult.
127
237-249
2016
Morus notabilis (W9S4Y0), Morus notabilis (W9SAM9), Morus notabilis (W9SJA3), Morus notabilis (W9SMK4), Morus notabilis (W9SPF5), Morus notabilis (W9ST04)
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brenda
Arbona, V.; Zandalinas, S.I.; Manzi, M.; Gonzalez-Guzman, M.; Rodriguez, P.L.; Gomez-Cadenas, A.
Depletion of abscisic acid levels in roots of flooded Carrizo citrange (Poncirus trifoliata L. Raf. x Citrus sinensis L. Osb.) plants is a stress-specific response associated to the differential expression of PYR/PYL/RCAR receptors
Plant Mol. Biol.
93
623-640
2017
Citrus sinensis x Citrus trifoliata
brenda
Son, S.; Chitnis, V.R.; Liu, A.; Gao, F.; Nguyen, T.N.; Ayele, B.T.
Abscisic acid metabolic genes of wheat (Triticum aestivum L.) identification and insights into their functionality in seed dormancy and dehydration tolerance
Planta
244
429-447
2016
Triticum aestivum (B8QBY2), Triticum aestivum
brenda
Liu, S.; Lv, Y.; Wan, X.R.; Li, L.M.; Hu, B.; Li, L.
Cloning and expression analysis of cDNAs encoding ABA 8'-hydroxylase in peanut plants in response to osmotic stress
PLoS ONE
9
e97025
2014
Arachis hypogaea, Arachis hypogaea (U6NHS3), Arachis hypogaea (U6NJF1)
brenda
Takeuchi, J.; Okamoto, M.; Mega, R.; Kanno, Y.; Ohnishi, T.; Seo, M.; Todoroki, Y.
Abscinazole-E3M, a practical inhibitor of abscisic acid 8'-hydroxylase for improving drought tolerance
Sci. Rep.
6
37060
2016
Arabidopsis thaliana (Q9FH76)
brenda
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