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Crystal structure of Arabidopsis thaliana 12‐oxophytodienoate reductase isoform 3 in complex with 8‐ iso prostaglandin A 1

Crystal structure of Arabidopsis thaliana 12‐oxophytodienoate reductase isoform 3 in complex with... <h1>INTRODUCTION</h1> Jasmonic acid (JA) is a plant secondary messenger that contributes to coordinated responses to many biotic and abiotic stresses, as well as other diverse processes such as pollen maturation and wound responses. 1 , 2 Biosynthesis of JA originates from linolenic acid in chloroplast membranes, and a number of enzymes are involved in the conversion of this polyunsaturated fatty acid into cyclopentane containing compound JA. 3 12‐oxophytodienoate reductase 3 (OPR3), one of the enzymes involved in the biosynthesis of JA, uniquely catalyzes the reduction of the cyclopentenone ring of (9 S ,13 S )‐12‐oxophytodienoate [(9 S ,13 S )‐OPDA]. 4 The JA‐deficient phenotype of OPR3 loss‐of‐function mutants in Arabidopsis thaliana indicates that other OPR isoforms cannot substitute for OPR3 in JA biosynthesis. 5 The physiologically relevant (9 S ,13 S )‐enantiomer of OPDA is not a substrate for the majority of OPRs. 4 Thus the unique function of OPR3 in the biosynthesis of JA is a result of its relaxed stereoselectivity with respect to OPDA stereoisomers. While Arabidopsis thaliana OPR3 (AtOPR3) and Lycopersicon esculentum OPR3 (LeOPR3) reduce all four stereoisomers of OPDA, the large majority of OPR isoforms seem to resemble LeOPR1 and AtOPR1/2 in their substrate http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Proteins: Structure Function and Bioinformatics Wiley

Crystal structure of Arabidopsis thaliana 12‐oxophytodienoate reductase isoform 3 in complex with 8‐ iso prostaglandin A 1

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References (17)

Publisher
Wiley
Copyright
Copyright © 2011 Wiley‐Liss, Inc.
ISSN
0887-3585
eISSN
1097-0134
DOI
10.1002/prot.23153
pmid
21915915
Publisher site
See Article on Publisher Site

Abstract

<h1>INTRODUCTION</h1> Jasmonic acid (JA) is a plant secondary messenger that contributes to coordinated responses to many biotic and abiotic stresses, as well as other diverse processes such as pollen maturation and wound responses. 1 , 2 Biosynthesis of JA originates from linolenic acid in chloroplast membranes, and a number of enzymes are involved in the conversion of this polyunsaturated fatty acid into cyclopentane containing compound JA. 3 12‐oxophytodienoate reductase 3 (OPR3), one of the enzymes involved in the biosynthesis of JA, uniquely catalyzes the reduction of the cyclopentenone ring of (9 S ,13 S )‐12‐oxophytodienoate [(9 S ,13 S )‐OPDA]. 4 The JA‐deficient phenotype of OPR3 loss‐of‐function mutants in Arabidopsis thaliana indicates that other OPR isoforms cannot substitute for OPR3 in JA biosynthesis. 5 The physiologically relevant (9 S ,13 S )‐enantiomer of OPDA is not a substrate for the majority of OPRs. 4 Thus the unique function of OPR3 in the biosynthesis of JA is a result of its relaxed stereoselectivity with respect to OPDA stereoisomers. While Arabidopsis thaliana OPR3 (AtOPR3) and Lycopersicon esculentum OPR3 (LeOPR3) reduce all four stereoisomers of OPDA, the large majority of OPR isoforms seem to resemble LeOPR1 and AtOPR1/2 in their substrate

Journal

Proteins: Structure Function and Bioinformatics – Wiley

Published: Nov 1, 2011

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