Phosphoenolpyruvate carboxylase: a new era of structural biology.
There have been remarkable advances in our knowledge of this important enzyme in the last decade. This review focuses on three recent topics: the three-dimensional structure of the protein, molecular mechanisms of catalytic and regulatory functions, and the molecular cloning and characterization of PEPC kinases, which are Ser/Thr kinases involved specifically in regulatory phosphorylation of vascular plant PEPC. Analysis by X-ray crystallography and site-directed mutagenesis for E. coli and maize PEPC identified the catalytic site and allosteric effector binding sites, and revealed the functional importance of mobile loops. We present the reaction mechanism of PEPC in which we assign the roles of individual amino acid residues. We discuss the unique molecular property of PEPC kinase and its possible regulation at the post-translational level.
Izui
Katsura
K
Laboratory of Plant Physiology, Graduate School of Biostudies, Kyoto University, Kyoto 606-8502, Japan. izui@kais.kyoto-u.ac.jp
Matsumura
Hiroyoshi
H
Furumoto
Tsuyoshi
T
Kai
Yasushi
Y
D002384:Catalysis; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D008958:Models, Molecular; D010730:Phosphoenolpyruvate Carboxylase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D010944:Plants / Q000201:enzymology; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism
C069767:phosphoenolpyruvate carboxylase kinase; D017346:Protein Serine-Threonine Kinases; D010730:Phosphoenolpyruvate Carboxylase