title: Bacterial production and purification of phosphorylatable phosphoenolpyruvate carboxylase from tobacco.
abstract: Tobacco phosphoenolpyruvate carboxylase (PEPC) [EC 4.1.1.31] cDNA was efficiently expressed in E. coli under the control of the lacZ promoter. The enzyme, purified to homogeneity, had the same catalytic activity, and was phosphorylated in vitro by maize PEPC kinase.
authors.affiliation: Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Koizumi
authors.forename: F
authors.initials: F
authors.lastname: Sato
authors.forename: Y
authors.initials: Y
authors.lastname: Yamada
mesh_terms: D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D007763:Lac Operon; D010730:Phosphoenolpyruvate Carboxylase / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D010766:Phosphorylation; D010947:Plants, Toxic; D010957:Plasmids; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D014026:Nicotiana / Q000201:enzymology*
chemical_list: D011994:Recombinant Proteins; D010730:Phosphoenolpyruvate Carboxylase