Structural Insights into Maize Viviparous14, a Key Enzyme in the Biosynthesis of the Phytohormone Abscisic Acid

被引：136

作者：

Messing, Simon A. J. ^{[1
]}

Gabelli, Sandra B. ^{[1
]}

Echeverria, Ignacia ^{[1
]}

Vogel, Jonathan T. ^{[2
]}

Guan, Jiahn Chou ^{[2
]}

Tan, Bao Cai ^{[2
]}

Klee, Harry J. ^{[2
]}

McCarty, Donald R. ^{[2
]}

Amzel, L. Mario ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Biophys & Biophys Chem, Baltimore, MD 21205 USA

[2] Univ Florida, Dept Hort Sci, Gainesville, FL 32611 USA

来源：

PLANT CELL | 2010年 / 22卷 / 09期

基金：

美国国家科学基金会;

关键词：

CAROTENOID CLEAVAGE DIOXYGENASE; VITAMIN-A FORMATION; 9-CIS-EPOXYCAROTENOID DIOXYGENASE; MOLECULAR-IDENTIFICATION; GERMINATION STIMULANT; SUBSTRATE-SPECIFICITY; ARABIDOPSIS; INHIBITION; VP14; CRYSTALLIZATION;

D O I：

10.1105/tpc.110.074815

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：

The key regulatory step in the biosynthesis of abscisic acid (ABA), a hormone central to the regulation of several important processes in plants, is the oxidative cleavage of the 11,12 double bond of a 9-cis-epoxycarotenoid. The enzyme viviparous14 (VP14) performs this cleavage in maize (Zea mays), making it a target for the rational design of novel chemical agents and genetic modifications that improve plant behavior through the modulation of ABA levels. The structure of VP14, determined to 3.2-angstrom resolution, provides both insight into the determinants of regio- and stereospecificity of this enzyme and suggests a possible mechanism for oxidative cleavage. Furthermore, mutagenesis of the distantly related CCD1 of maize shows how the VP14 structure represents a template for all plant carotenoid cleavage dioxygenases (CCDs). In addition, the structure suggests how VP14 associates with the membrane as a way of gaining access to its membrane soluble substrate.

引用

页码：2970 / 2980

页数：11

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