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...

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Bibliographic Details
Published inBiotechnology and applied biochemistry Vol. 8; no. 5; p. 375
Main Authors Neuzil, J, Novotná, J, Bĕhal, V, Hostálek, Z
Format Journal Article
LanguageEnglish
Published United States 01.10.1986
Subjects
Adenine Nucleotides - pharmacology
Fungal Proteins - antagonists & inhibitors
Glucosephosphate Dehydrogenase - antagonists & inhibitors
NAD - metabolism
Phosphates - pharmacology
Streptomyces aureofaciens - enzymology
Streptomyces aureofaciens - metabolism
Tetracyclines - biosynthesis
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Summary: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.
ISSN:0885-4513