Apyrase (ATP-diphosphohydrolase, EC 3.6.1.5) and inorganic pyrophosphatase (EC 3.6.1.1) were partially purified from S. aureofaciens RIA 57 and characterized. Apyrase degrades, in addition to ATP, other nucleoside triphosphates and nucleoside diphosphates, diphosphate, thiamine diphosphate, phosphoenolpyruvate and oligophosphates of chain length n less than 90. The apyrase activity was detected in the membrane and supernatant fractions. Its properties (substrate specificity. effect of inhibitors, pH optimum and effect of Mg2+ ions) were similar in both fractions except for the effect of oligomycin that inhibited only the membrane fraction. Pyrophosphatase exhibited a strict substrate specificity, substrates other than diphosphate being degraded relatively slowly. Of other enzymes exhibiting the phosphatase activity acid phosphatase (EC 3.1.3.2) and alkaline phosphatase (EC 3.1.3.1), trimetaphosphatase (EC 3.6.1.2) and exopolyphosphatase (EC 3.6.1.11) degrading oligophosphatase of chain length n = 15, 40 and 60, were detected.

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J Biol Chem. 1970 Mar 10;245(5):1115-21 PubMed

J Biochem. 1972 Mar;71(3):387-99 PubMed

Folia Microbiol (Praha). 1982;27(3):153-8 PubMed

Biochim Biophys Acta. 1960 Mar 11;38:460-9 PubMed

J Biochem. 1969 Jul;66(1):33-43 PubMed

Bacteriol Rev. 1977 Mar;41(1):47-99 PubMed

J Am Pharm Assoc Am Pharm Assoc. 1949 Aug;38(8):473-5 PubMed

J Biol Chem. 1951 Nov;193(1):265-75 PubMed

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

Role of phosphatases in the biosynthesis of chlortetracycline in Streptomyces aureofaciens