PHOSPHOENOLPYRUVATE CARBOXYLASE: A Ubiquitous, Highly Regulated Enzyme in Plants.
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.
Chollet
Raymond
R
Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588-0664, UA CNRS D-1128, Institut de Biotechnologie des Plantes, Universite de Paris-Sud, Orsay Cedex, 91405 France, Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588-0664.
Vidal
Jean
J
O'Leary
Marion H.
MH