Activity of phosphoenolpyruvate carboxylase of an anthracycline-producing streptomycete
- 1 November 1988
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 34 (11) , 1241-1246
- https://doi.org/10.1139/m88-218
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 Co ASH.This publication has 0 references indexed in Scilit: