Abstract
Partially purified citrate synthase (EC 4.1.3.7) was isolated from submerged mycelium ofStreptomyces aureofaciens RIA 57, a strain producing chlortetracycline. Enzymatic activity was determined spectrophotometrically by means of 5,5′-dithio-bis-(2-nitrobenzoic acid). Citrate synthase was inhibited by ATP, inhibition being competitive with respect to acetyl coenzyme A. In 5mm concentration, ATP caused 55% inhibition of the enzyme. ADP, in the same concentration, caused 30% inhibition, while AMP caused none. Other natural nucleoside di- and triphosphates, in 1–5mm concentration, did not significantly affect citrate synthase inStreptomyces aureofaciens. Mg2+ inhibited the activity of the enzyme, but also reduced the negative effect of ATP. The role of ATP in regulation of the metabolic paths of acetyl CoA is discussed.
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Hošťálek, Z., Ryabushko, T.A., Cudlín, J. et al. Regulation of biosynthesis of secondary metabolites. Folia Microbiol 14, 121–127 (1969). https://doi.org/10.1007/BF02892880
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DOI: https://doi.org/10.1007/BF02892880