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Information on EC 1.3.1.42 - 12-oxophytodienoate reductase and Organism(s) Solanum lycopersicum and UniProt Accession Q9XG54
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1.3.1.42 12-oxophytodienoate reductaseIUBMB Comments
Involved in the conversion of linolenate into jasmonate in Zea mays.
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Word Map
- 1.3.1.42
-
jasmonic
-
allene
-
octadecanoids
- oxylipins
- cyclopentanone
-
ja-deficient
- environmental protection
The taxonomic range for the selected organisms is: Solanum lycopersicum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
12-oxophytodienoate reductase, 12-oxo-phytodienoic acid reductase, csopr3, osopr7, opda reductase, taopr1, 12-oxophytodienoate reductase 3, osopr8, oprii, 12-oxophytodienoate-10,11-reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
12-oxo-phytodienoic acid reductase
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-
-
-
OPR
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate:NADP+ 4-oxidoreductase
Involved in the conversion of linolenate into jasmonate in Zea mays.
CAS REGISTRY NUMBER
COMMENTARY
101150-03-2
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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
(15Z)-12-oxophyto-10,15-dienoate + NADPH
8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
-
-
-
?
(2E)-3,7-dimethylocta-2,6-dienal + NADH
(3S)-3,7-dimethyloct-6-enal + NAD+
above 99% conversion with OPR-1
-
-
?
(2E)-3,7-dimethylocta-2,6-dienal + NADPH
(3S)-3,7-dimethyloct-6-enal + NADP+
above 99% conversion with OPR-1
-
-
?
(2Z)-2-methylbut-2-enedioic acid + NADH
(2R)-2-methylbutanedioic acid + NAD+
above 99% conversion with OPR-1
-
-
?
(2Z)-2-methylbut-2-enedioic acid + NADPH
(2R)-2-methylbutanedioic acid + NADP+
above 99% conversion with OPR-1
-
-
?
(9R,13R)-(15Z)-12-oxophyto-10,15-dienoate + NADPH
(9R,13R)-8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
-
-
-
?
(9S,13S)-12-oxo-phytodienoic acid + NADPH + H+
3-oxo-2((2Z)-pentenyl)-cyclopentane-1-octanoic acid + NADP+
enzyme is a FMN-dependent oxidoreductase that catalyzes the reduction of the cyclopentenone (9S,13S)-12-oxophytodienoate to the corresponding cyclopentanone in the biosynthesis of the plant hormone jasmonic acid
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-
?
12-oxo-cis-phythodienoic acid + NADPH
cis-3-oxo-2-(2'-pentenyl)cyclopentane-1-octanoic acid + NADP+
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-
-
?
2,6,6-trimethylcyclohex-2-ene-1,4-dione + NADH
(6R)-2,2,6-trimethylcyclohexane-1,4-dione + NAD+
above 98% conversion with OPR-1
-
-
?
2,6,6-trimethylcyclohex-2-ene-1,4-dione + NADPH
(6R)-2,2,6-trimethylcyclohexane-1,4-dione + NADP+
above 98% conversion with OPR-1
-
-
?
2-methylcyclopent-2-en-1-one + NADH
(2S)-2-methylcyclopentanone + NAD+
58% conversion with OPR-1
-
-
?
2-methylcyclopent-2-en-1-one + NADPH
(2S)-2-methylcyclopentanone + NADP+
45% conversion with OPR-1
-
-
?
3-methyl-1-phenyl-1H-pyrrole-2,5-dione + NADH
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NAD+
99% conversion with OPR-1
-
-
?
3-methyl-1-phenyl-1H-pyrrole-2,5-dione + NADPH
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NADP+
99% conversion with OPR-1
-
-
?
[(E)-1-methyl-2-nitroethenyl]benzene + NADH + H+
[(1R)-1-methyl-2-nitroethyl]benzene + NAD+
above 99% conversion with OPR-1
-
-
?
[(E)-1-methyl-2-nitroethenyl]benzene + NADPH + H+
[(1R)-1-methyl-2-nitroethyl]benzene + NADP+
above 99% conversion with OPR-1
-
-
?
(15Z)-12-oxophyto-10,15-dienoate + NADPH
8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
-
-
-
?
(2E)-3,7-dimethylocta-2,6-dienal + NADH
(3S)-3,7-dimethyloct-6-enal + NAD+
90% conversion with OPR-3
-
-
?
(2E)-3,7-dimethylocta-2,6-dienal + NADPH
(3S)-3,7-dimethyloct-6-enal + NADP+
90% conversion with OPR-3
-
-
?
(9R,13R)-(15Z)-12-oxophyto-10,15-dienoate + NADPH
(9R,13R)-8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
(9S,13S)-(15Z)-12-oxophyto-10,15-dienoate + NADPH
(9S,13S)-8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
(9S,13S)-12-oxo-phytodienoic acid + NADPH
3-oxo-2((2Z)-pentenyl)-cyclopentane-1-octanoic acid + NADP+
-
-
-
?
(9S,13S)-12-oxo-phytodienoic acid + NADPH + H+
?
FMN-dependent oxidoreductase, biosynthesis of the plant hormone jasmonic acid, the enzyme in plants relates to old yellow enzyme (OYE) from Saccharomyces cerevisiae
-
-
?
(9S,13S)-12-oxophytodienoate + NADPH
3-oxo-2((2Z)-pentenyl)-cyclopentane-1-octanoic acid + NADP+
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-
-
?
12-oxo-cis-phythodienoic acid + NADPH
cis-3-oxo-2-(2'-pentenyl)cyclopentane-1-octanoic acid + NADP+
-
-
-
?
2,6,6-trimethylcyclohex-2-ene-1,4-dione + NADH
(6R)-2,2,6-trimethylcyclohexane-1,4-dione + NAD+
77% conversion with OPR-3
-
-
?
2,6,6-trimethylcyclohex-2-ene-1,4-dione + NADPH
(6R)-2,2,6-trimethylcyclohexane-1,4-dione + NADP+
78% conversion with OPR-3
-
-
?
2-methylcyclopent-2-en-1-one + NADH
(2S)-2-methylcyclopentanone + NAD+
19% conversion with OPR-3
-
-
?
2-methylcyclopent-2-en-1-one + NADPH
(2S)-2-methylcyclopentanone + NADP+
27% conversion with OPR-3
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-
?
3-methyl-1-phenyl-1H-pyrrole-2,5-dione + NADH
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NAD+
99% conversion with OPR-3
-
-
?
3-methyl-1-phenyl-1H-pyrrole-2,5-dione + NADPH
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NADP+
99% conversion with OPR-3
-
-
?
3-methylcyclopent-2-en-1-one + NADH
(3S)-3-methylcyclopentanone + NAD+
2% conversion with OPR-3
-
-
?
3-methylcyclopent-2-en-1-one + NADPH
(3S)-3-methylcyclopentanone + NADP+
1% conversion with OPR-3
-
-
?
3-oxo-2((2Z)-pentenyl)-cyclopentane-1-octanoic acid + NADP+
?
in vitro, OPR3 reduces the jasmonic acid precursor (9S,13S)-12-oxophytodienoate as well as the enantiomeric (9R,13R)-12-oxophytodienoate, while its isozyme OPR1 is highly selective, accepting only (9R,13R)-12-oxophytodienoate as a substrate, the enzyme in plants relates to old yellow enzyme (OYE) from Saccharomyces cerevisiae
-
-
?
[(E)-1-methyl-2-nitroethenyl]benzene + NADH + H+
[(1S)-1-methyl-2-nitroethyl]benzene + NAD+
69% conversion with OPR-3
-
-
?
[(E)-1-methyl-2-nitroethenyl]benzene + NADPH + H+
[(1S)-1-methyl-2-nitroethyl]benzene + NADP+
72% conversion with OPR-3
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-
?
(9R,13R)-(15Z)-12-oxophyto-10,15-dienoate + NADPH
(9R,13R)-8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
isozyme OPR1, no activity with the (9S,13S)-(15Z)-12-oxophyto-10,15-dienoate enantiomer
-
-
?
(9R,13R)-(15Z)-12-oxophyto-10,15-dienoate + NADPH
(9R,13R)-8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
isozymes OPR3
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-
?
(9S,13S)-(15Z)-12-oxophyto-10,15-dienoate + NADPH
(9S,13S)-8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
product is the direct precursor in the jasmonate biosynthesis
-
-
?
(9S,13S)-(15Z)-12-oxophyto-10,15-dienoate + NADPH
(9S,13S)-8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
isozyme OPR3
-
-
?
additional information
?
-
phylogenetic analysis, enzyme is involved in octadecanoid biosynthesis which has differential roles for in the local versus the systemic wound response
-
-
?
additional information
?
-
phylogenetic analysis, enzyme is involved in octadecanoid biosynthesis which has differential roles for in the local versus the systemic wound response
-
-
?
additional information
?
-
phylogenetic analysis, enzyme is involved in octadecanoid biosynthesis which has differential roles for in the local versus the systemic wound response
-
-
?
additional information
?
-
isozyme OPR-1 does not convert 3-methylcyclopent-2-en-1-one
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-
?
additional information
?
-
isozyme OPR-1 does not convert 3-methylcyclopent-2-en-1-one
-
-
?
additional information
?
-
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isozyme OPR-1 does not convert 3-methylcyclopent-2-en-1-one
-
-
?
additional information
?
-
OPR1-like enzymes are highly selective, accepting only (9R,13R)-12-oxophytodienoate as a substrate
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-
?
additional information
?
-
OPR1-like enzymes are highly selective, accepting only (9R,13R)-12-oxophytodienoate as a substrate
-
-
?
additional information
?
-
the photoinduced electron transfer is compared in the structurally homologous enzymes 12-oxophytodienoate reductase 1 (OPR1) and Old Yellow Enzyme 1 (OYE1). The inside of a protein active site is a complex/heterogeneous dielectric network where genetically programmed heterogeneity near the site of biological electron transfer can significantly affect the presence and lifetime of various intermediate states
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-
-
additional information
?
-
no activity of isozyme OPR2 with (15Z)-12-oxophyto-10,15-dienoate stereoisomers
-
-
?
additional information
?
-
no activity of isozyme OPR2 with (15Z)-12-oxophyto-10,15-dienoate stereoisomers
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-
?
additional information
?
-
no activity of isozyme OPR2 with (15Z)-12-oxophyto-10,15-dienoate stereoisomers
-
-
?
additional information
?
-
stereospecificity of isozymes, overview, isozyme OPR1 shows a broad substrate specificity reducing a wide range of alpha,beta-unsaturated carbonyl compounds
-
-
?
additional information
?
-
stereospecificity of isozymes, overview, isozyme OPR1 shows a broad substrate specificity reducing a wide range of alpha,beta-unsaturated carbonyl compounds
-
-
?
additional information
?
-
stereospecificity of isozymes, overview, isozyme OPR1 shows a broad substrate specificity reducing a wide range of alpha,beta-unsaturated carbonyl compounds
-
-
?
additional information
?
-
stereospecificity of isozymes, overview, isozyme OPR3 shows a broad substrate specificity reducing a wide range of alpha,beta-unsaturated carbonyl compounds
-
-
?
additional information
?
-
stereospecificity of isozymes, overview, isozyme OPR3 shows a broad substrate specificity reducing a wide range of alpha,beta-unsaturated carbonyl compounds
-
-
?
additional information
?
-
stereospecificity of isozymes, overview, isozyme OPR3 shows a broad substrate specificity reducing a wide range of alpha,beta-unsaturated carbonyl compounds
-
-
?
additional information
?
-
isozyme OPR-3 does not convert (2Z)-2-methylbut-2-enedioic acid
-
-
?
additional information
?
-
isozyme OPR-3 does not convert (2Z)-2-methylbut-2-enedioic acid
-
-
?
additional information
?
-
-
isozyme OPR-3 does not convert (2Z)-2-methylbut-2-enedioic acid
-
-
?
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
(15Z)-12-oxophyto-10,15-dienoate + NADPH
8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
-
-
-
?
(9R,13R)-(15Z)-12-oxophyto-10,15-dienoate + NADPH
(9R,13R)-8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
-
-
-
?
(9S,13S)-12-oxo-phytodienoic acid + NADPH + H+
3-oxo-2((2Z)-pentenyl)-cyclopentane-1-octanoic acid + NADP+
enzyme is a FMN-dependent oxidoreductase that catalyzes the reduction of the cyclopentenone (9S,13S)-12-oxophytodienoate to the corresponding cyclopentanone in the biosynthesis of the plant hormone jasmonic acid
-
-
?
(9S,13S)-(15Z)-12-oxophyto-10,15-dienoate + NADPH
(9S,13S)-8-[(1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl]octanoate + NADP+
product is the direct precursor in the jasmonate biosynthesis
-
-
?
(9S,13S)-12-oxo-phytodienoic acid + NADPH + H+
?
FMN-dependent oxidoreductase, biosynthesis of the plant hormone jasmonic acid, the enzyme in plants relates to old yellow enzyme (OYE) from Saccharomyces cerevisiae
-
-
?
3-oxo-2((2Z)-pentenyl)-cyclopentane-1-octanoic acid + NADP+
?
in vitro, OPR3 reduces the jasmonic acid precursor (9S,13S)-12-oxophytodienoate as well as the enantiomeric (9R,13R)-12-oxophytodienoate, while its isozyme OPR1 is highly selective, accepting only (9R,13R)-12-oxophytodienoate as a substrate, the enzyme in plants relates to old yellow enzyme (OYE) from Saccharomyces cerevisiae
-
-
?
additional information
?
-
phylogenetic analysis, enzyme is involved in octadecanoid biosynthesis which has differential roles for in the local versus the systemic wound response
-
-
?
additional information
?
-
phylogenetic analysis, enzyme is involved in octadecanoid biosynthesis which has differential roles for in the local versus the systemic wound response
-
-
?
additional information
?
-
phylogenetic analysis, enzyme is involved in octadecanoid biosynthesis which has differential roles for in the local versus the systemic wound response
-
-
?
additional information
?
-
OPR1-like enzymes are highly selective, accepting only (9R,13R)-12-oxophytodienoate as a substrate
-
-
?
additional information
?
-
OPR1-like enzymes are highly selective, accepting only (9R,13R)-12-oxophytodienoate as a substrate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
in the dimer interface of enzyme, a sulfate ion is bound which forms hydrogen bonds with two arginines of protomer A and one arginine of loop L6 of the partner protomer B. Sulfate ion may mimic the phosphate group of phosphorylated T364
-
additional information
-
in the dimer interface of enzyme, a sulfate ion is bound which forms hydrogen bonds with two arginines of protomer A and one arginine of loop L6 of the partner protomer B. Sulfate ion may mimic the phosphate group of phosphorylated T364
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
for oxidative half-reaction, kox of trans-hex-2-2enal is 0.3 per sec
-
additional information
additional information
-
for oxidative half-reaction, kox of trans-hex-2-2enal is 0.3 per sec
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OPR1_SOLLC
376
0
42415
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
dimer
concentration-dependent shift from monomer with 40000 Da at 0.022 mM to dimer with 80000 Da at 0.358 mM, dynamic light scattering
monomer
concentration-dependent shift from monomer with 40000 Da at 0.022 mM to dimer with 80000 Da at 0.358 mM, dynamic light scattering
additional information
rapid monomer-dimer equilibrium with a high dissociation constant in vitro
additional information
-
rapid monomer-dimer equilibrium with a high dissociation constant in vitro
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
OPR1:p-hydroxybenzaldehyde complex at 2.3 A resolution, determination of the crystal structures of OPR1 in complex with the ligand p-hydroxybenzaldehyde, structural comparison with the OPR1:(9R,13R)-12-oxophytodienoate complex and further biochemical and mutational analyses reveals that 2 active-site residues, Tyr78 and Tyr246 in OPR1 are critical for substrate filtering
at 2.0 A resolution, determination of the crystal structures of OPR3 in complex with the ligand p-hydroxybenzaldehyde, structural comparison with the OPR1:(9R,13R)-12-oxophytodienoate complex and further biochemical and mutational analyses reveals that 2 active-site residues, Phe74 and His244 in OPR3 are critical for substrate filtering
native enzyme and mutants E291L and Y364F. Wild-type enzyme crystallizes as an extraordinary self-inhibiting dimer, dimerization is actively driven by the mutual binding of the two L6 loops into the two active sites
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isozyme OPR1 from Escherichia coli by nickel affinity chromatography
recombinant His-tagged isozyme OPR2 from Escherichia coli by nickel affinity chromatography
recombinant His-tagged isozyme OPR3 from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged isozyme OPR1 in Escherichia coli, transient expression of isozyme OPR1 as enhanced-GFP- or RFP-fusion protein in onion epidermal cells for subcellular localization study
expression of His-tagged isozyme OPR2 in Escherichia coli
expression of His-tagged isozyme OPR3 in Escherichia coli, transient expression of isozyme OPR3 as enhanced-GFP- or RFP-fusion protein in onion epidermal cells for subcellular localization study
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Breithaupt, C.; Strassner, J.; Breitinger, U.; Huber, R.; Macheroux, P.; Schaller, A.; Clausen, T.
X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE
Structure
9
419-429
2001
Solanum lycopersicum
Strassner, J.; Schaller, F.; Frick, U.B.; Howe, G.A.; Weiler, E.W.; Amrhein, N.; Macheroux, P.; Schaller, A.
Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response
Plant J.
32
585-601
2002
Arabidopsis thaliana, Solanum lycopersicum (Q9FEW9), Solanum lycopersicum (Q9FEX0), Solanum lycopersicum (Q9XG54)
Breithaupt, C.; Kurzbauer, R.; Lilie, H.; Schaller, A.; Strassner, J.; Huber, R.; Macheroux, P.; Clausen, T.
Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerization
Proc. Natl. Acad. Sci. USA
103
14337-14342
2006
Solanum lycopersicum (Q9FEW9), Solanum lycopersicum
Hall, M.; Stueckler, C.; Kroutil, W.; Macheroux, P.; Faber, K.
Asymmetric bioreduction of activated alkenes using cloned 12-oxophytodienoate reductase isoenzymes OPR-1 and OPR-3 from Lycopersicon esculentum (tomato): a striking change of stereoselectivity
Angew. Chem.
46
3934-3937
2007
Solanum lycopersicum (Q9FEW9), Solanum lycopersicum (Q9XG54), Solanum lycopersicum
Breithaupt, C.; Kurzbauer, R.; Schaller, F.; Stintzi, A.; Schaller, A.; Huber, R.; Macheroux, P.; Clausen, T.
Structural basis of substrate specificity of plant 12-oxophytodienoate reductases
J. Mol. Biol.
392
1266-1277
2009
Solanum lycopersicum (Q9FEW9), Solanum lycopersicum (Q9XG54)
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