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 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