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1.3.1.42: 12-oxophytodienoate reductase

This is an abbreviated version!
For detailed information about 12-oxophytodienoate reductase, go to the full flat file.

Word Map on EC 1.3.1.42

Reaction

8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate
+
NADP+
=
(15Z)-12-oxophyto-10,15-dienoate
+
NADPH
+
H+

Synonyms

12-oxo phytodienoic acid reductase, 12-oxo-phytodienoate acid reductase, 12-oxo-phytodienoic acid reductase, 12-oxophytodienoate reductase, 12-oxophytodienoate reductase 1, 12-oxophytodienoate reductase 3, 12-oxophytodienoate reductase isoform 3, 12-oxophytodienoate-10,11-reductase, 12-oxophytodienoate10,11-reductase, CsOPR3, cyclopentenone reductase, HvOPR1, More, morphine reductase, old yellow enzyme, OPDA reductase, OPDA reductase I, OPR, OPR-1, OPR-3, OPR1, OPR2, OPR3, OPR3 oxidoreductase, OPR4, OPR5, OPR6, OPR7, OPR8, OPRI, OPRII, OsOPR01-1, OsOPR02-1, OsOPR04-1, OsOPR06-1, OsOPR08-1, OsOPR10, OsOPR11, OsOPR6, OsOPR7, OsOPR8, oxophytodienoate reductase, oxophytodienoic acid reductase, OYE, phytodienoic acid reductase, S64, TaOPR1

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.42 12-oxophytodienoate reductase

Engineering

Engineering on EC 1.3.1.42 - 12-oxophytodienoate reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E291L
sixfold faster turnover than wild-type. Crystallization in same space group as wild-type, but with strikingly different cell constants. Appears as monomer in the crystal
F74Y
OPR3 mutant, change in substrate specificity, similar increase in stereoselectivity is observed for the mutant as compared to the wild-type enzyme
F74Y/H244Y
OPR3 double-mutant, reduction of (9S,13S)-12-oxo-phytodienoic acid is slower in the double-mutant as in the wild type enzyme and the single mutants, the protein crystallizes as a monomer with none of the dimer interactions retain
H244Y
OPR3 mutant, change in substrate specificity, similar increase in stereoselectivity is observed for the mutant as compared to the wild-type enzyme
Y364F
crystallization as a monomer with none of the dimer interactions retained
additional information