title: Activity of phosphoenolpyruvate carboxylase of an anthracycline-producing streptomycete.
abstract: During fermantation studies on the production of anthracycline antibiotics by Streptomyces C5, it was observed that among the intermediate metabolism enzymes tested, only phosphoenolpyruvate carboxylase (PEPCase; EC 4.1.1.31) increased significantly in specific activity during stationary phase. The specific activity of the Streptomyces C5 PEPCase increased ca. 3-fold during antibiotic production phase from the logarithmic phase levels. To characterize the regulation of the enzyme further, the Streptomyces C5 PEPCase was purified 150-fold from crude extracts. Acetyl-CoA and Mg2+ were shown to be required for PEPCase activity. The activity of the partially purified PEPCase was stimulated slightly by fructose 1,6-bisphosphate and AMP, and was inhibited severely by oxaloacetate, aspartate, malate, succinate, ATP, citrate, and CoASH.
authors.affiliation: Department of Microbiology, Ohio State University, Columbus 43210.
authors.forename: M L
authors.initials: ML
authors.lastname: Dekleva
authors.forename: W R
authors.initials: WR
authors.lastname: Strohl
mesh_terms: D000494:Allosteric Regulation; D000903:Antibiotics, Antineoplastic / Q000096:biosynthesis; D010728:Phosphoenolpyruvate / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology*
chemical_list: D000903:Antibiotics, Antineoplastic; D010728:Phosphoenolpyruvate