The localization of anhydrotetracycline oxygenase and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) was studied by determining the enzyme activities in subcellular fractions obtained by differential centrifugation of the mycelia of Streptomyces aureofaciens after lysozyme treatment. Glucose-6-phosphate dehydrogenase was a typical cytoplasmic enzyme both in the low- and high-production strain. Anhydrotetracycline oxygenase was found in the membrane fraction of the low-production strain. In the high-production strain, it was detected in several fractions, the highest activity being found in cytoplasm. The presence of 10 microM benzyl thiocyanate in the culture medium significantly changed the distribution of the latter enzyme in both strains. The redistribution of the enzymes is discussed with respect to tetracycline over-production.

Dairy Research Institute Prague Czechoslovakia

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Folia Microbiol (Praha). 1982;27(2):102-6 PubMed

Acta Biochim Pol. 1969;16(4):371-8 PubMed

Biotechnol Appl Biochem. 1986 Oct;8(5):375-8 PubMed

Methods Enzymol. 1975;43:606-7 PubMed

Folia Microbiol (Praha). 1987;32(5):402-10 PubMed

FEBS Lett. 1977 Sep 15;81(2):315-8 PubMed

Folia Microbiol (Praha). 1964 Mar;18:78-88 PubMed

Methods Enzymol. 1975;43:603-6 PubMed

Biochem J. 1985 Feb 1;225(3):639-43 PubMed

J Cell Biol. 1975 Aug;66(2):233-42 PubMed

J Hyg Epidemiol Microbiol Immunol. 1958;2(1):111-5 PubMed

J Gen Microbiol. 1974 Feb;80(2):389-400 PubMed

Protein profiles of Streptomyces aureofaciens producing tetracyclines: reappraisal of the effect of benzyl thiocyanate

Subcellular localization of enzymes in Streptomyces aureofaciens and its alteration by benzyl thiocyanate. I. Phosphatases and ATP-glucokinase