Structural insights into maize viviparous14, a key enzyme in the biosynthesis of the phytohormone abscisic acid

Simon A.J. Messing, L. Mario Amzel, Sandra B. Gabelli, Ignacia Echeverria, Jonathan T. Vogel, Jiahn Chou Guan, Bao Cai Tan, Harry J. Klee, Donald R. McCarty

Research output: Contribution to journalArticle

Abstract

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-A 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.

Original languageEnglish (US)
Pages (from-to)2970-2980
Number of pages11
JournalPlant Cell
Volume22
Issue number9
DOIs
StatePublished - Sep 2010

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology

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    Messing, S. A. J., Mario Amzel, L., Gabelli, S. B., Echeverria, I., Vogel, J. T., Guan, J. C., Tan, B. C., Klee, H. J., & McCarty, D. R. (2010). Structural insights into maize viviparous14, a key enzyme in the biosynthesis of the phytohormone abscisic acid. Plant Cell, 22(9), 2970-2980. https://doi.org/10.1105/tpc.110.074815