Activity of phosphoenolpyruvate carboxylase of an anthracycline-producing streptomycete.
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.
Dekleva
M L
ML
Department of Microbiology, Ohio State University, Columbus 43210.
Strohl
W R
WR
D000494:Allosteric Regulation; D000903:Antibiotics, Antineoplastic / Q000096:biosynthesis; D010728:Phosphoenolpyruvate / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology*
D000903:Antibiotics, Antineoplastic; D010728:Phosphoenolpyruvate