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Literature summary for 1.14.14.137 extracted from

  • Ueno, K.; Yoneyama, H.; Mizutani, M.; Hirai, N.; Todoroki, Y.
    Asymmetrical ligand binding by abscisic acid 8-hydroxylase (2007), Bioorg. Med. Chem., 15, 6311-6322.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
(-)-AHI1 competitive inhibition Arabidopsis thaliana
(1'R)-(-)-4'-deoxo-abscisic acid competitive inhibition Arabidopsis thaliana
(1'R)-(-)-6-nor-abscisic acid competitive inhibition Arabidopsis thaliana
(1'R,2'R)-(-)-2',3'-dihydro-4'-deoxo-abscisic acid competitive inhibition Arabidopsis thaliana
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 Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Arabidopsis thaliana
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(1'S)-(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2 Arabidopsis thaliana 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 8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1'S)-(+)-abscisate + [reduced NADPH-hemoprotein reductase] + O2 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 Arabidopsis thaliana 8'-hydroxyabscisate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
(2Z,4E)-5-[(1R,6R)-1-hydroxy-2,2,6-trimethylcyclohexyl]penta-2,4-dienoic acid + [reduced NADPH-hemoprotein reductase] + O2 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 Arabidopsis thaliana ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
(2Z,4E)-5-[(1S,6S)-1-hydroxy-2,2,6-trimethylcyclohexyl]penta-2,4-dienoic acid + [reduced NADPH-hemoprotein reductase] + O2 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 Arabidopsis thaliana ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?

Synonyms

Synonyms Comment Organism
ABA 8'-hydroxylase
-
Arabidopsis thaliana
abscisic acid 8'-hydroxylase
-
Arabidopsis thaliana
CYP707A
-
Arabidopsis thaliana
CYP707A3
-
Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2 7.3 assay at Arabidopsis thaliana

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00045
-
(1'R,2'R)-(-)-2',3'-dihydro-4'-deoxo-abscisic acid pH 7.2-7.3, 30°C Arabidopsis thaliana
0.027
-
(1'R)-(-)-4'-deoxo-abscisic acid pH 7.2-7.3, 30°C Arabidopsis thaliana

General Information

General Information Comment Organism
metabolism ABA 8'-hydroxylase is the major and key P450 enzyme in the abscisic acid catabolism Arabidopsis thaliana
physiological function ABA 8'-hydroxylase is the major and key P450 enzyme in the abscisic acid catabolism Arabidopsis thaliana