PHOSPHO<i>ENOL</i>PYRUVATE CARBOXYLASE: A Ubiquitous, Highly Regulated Enzyme in Plants

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  • Raymond Chollet
    Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588-0664
  • Jean Vidal
    UA CNRS D-1128, Institut de Biotechnologie des Plantes, Université de Paris-Sud, Orsay Cedex, 91405 France
  • Marion H. O'Leary
    Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588-0664

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<jats:p> ▪ Abstract  Since plant phosphoenolpyruvate carboxylase (PEPC) was last reviewed in the Annual Review of Plant Physiology over a decade ago (O'Leary 1982), significant advances have been made in our knowledge of this oligomeric, cytosolic enzyme. This review highlights this exciting progress in plant PEPC research by focusing on the three major areas of recent investigation: the enzymology of the protein; its posttranslational regulation by reversible protein phosphorylation and opposing metabolite effectors; and the structure, expression, and molecular evolution of the nuclear PEPC genes. It is hoped that the next ten years will be equally enlightening, especially with respect to the three-dimensional structure of the plant enzyme, the molecular analysis of its highly regulated protein-Ser/Thr kinase, and the elucidation of its associated signal-transduction pathways in various plant cell types. </jats:p>

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