Enzymes in jasmonate biosynthesis - Structure, function, regulation

被引:303
|
作者
Schaller, Andreas [1 ]
Stintzi, Annick [1 ]
机构
[1] Univ Hohenheim, Inst Plant Physiol & Biotechnol, D-70599 Stuttgart, Germany
关键词
Allene oxide cyclase; Allene oxide synthase; Crystal structure; CYP74; Jasmonate biosynthesis; Oxylipins; Oxophytodienoate reductase; Substrate specificity; ALLENE OXIDE SYNTHASE; BINDING CASSETTE TRANSPORTER; X-RAY-STRUCTURE; 12-OXOPHYTODIENOIC ACID REDUCTASE; COENZYME-A SYNTHETASE; ARABIDOPSIS-THALIANA; MOLECULAR-CLONING; BETA-OXIDATION; HYDROPEROXIDE LYASE; OXYLIPIN METABOLISM;
D O I
10.1016/j.phytochem.2009.07.032
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Jasmonates are a growing class of lipid-derived signaling molecules with diverse functions ranging from the initiation of biotic and abiotic stress responses to the regulation of plant growth and development. Jasmonate biosynthesis originates from polyunsaturated fatty acids in chloroplast membranes. In a first lipoxygenase-catalyzed reaction molecular oxygen is introduced to yield their 13-hydroperoxy derivatives. These fatty acid hydroperoxides are converted by allene oxide synthase and allene oxide cyclase to 12-oxophytodienoic acid (OPDA) and dinor-OPDA, i.e. the first cyclic intermediates of the pathway. In the subsequent step, the characteristic cyclopentanone ring structure of jasmonates is established by OPDA reductase. Until recently, jasmonic acid has been viewed as the end product of the pathway and as the bioactive hormone. it becomes increasingly clear, however, that biological activity extends to and may even differ between the various jasmonic acid metabolites and conjugates as well as its biosynthetic precursors. It has also become clear that oxygenated fatty acids give rise to a vast variety of bioactive compounds including but not limited to jasmonates. Recent insights into the structure, function, and regulation of the enzymes involved in jasmonate biosynthesis help to explain how this variety is generated while specificity is maintained. (c) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1532 / 1538
页数:7
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