Inhibition studies of glucose-6-phosphate dehydrogenase from tetracycline-producing Streptomyces aureofaciens.
NAD-linked activity of glucose-6-phosphate dehydrogenase from both low-producing and high-producing strains of Streptomyces aureofaciens was inhibited by ATP, ADP, AMP and Pi. The inhibition constants indicate that ADP was the most potent inhibitor. The NADP-linked activity remained unaffected even at relatively high concentrations of these inhibitors. All inhibitions of the NAD-linked activity were competitive with respect to NAD and noncompetitive with respect to glucose-6-phosphate. The results represent a possible new regulatory mechanism of glucose-6-phosphate dehydrogenase from a streptomycete and emphasize its involvement in the regulation of the biosynthesis of tetracyclines.
D000227:Adenine Nucleotides / Q000494:pharmacology; D005656:Fungal Proteins / Q000037:antagonists & inhibitors*; D005954:Glucosephosphate Dehydrogenase / Q000037:antagonists & inhibitors*; D009243:NAD / Q000378:metabolism; D010710:Phosphates / Q000494:pharmacology; D013304:Streptomyces aureofaciens / Q000201:enzymology* / Q000378:metabolism; D013754:Tetracyclines / Q000096:biosynthesis
D000227:Adenine Nucleotides; D005656:Fungal Proteins; D010710:Phosphates; D013754:Tetracyclines; D009243:NAD; D005954:Glucosephosphate Dehydrogenase