Studies in biosynthesis of polymetaphosphate by an enzyme from Corynebacterium xerosis

doi:10.1016/0006-3002(61)90945-3

Biochimica et Biophysica Acta

Volume 54, Issue 1, 25 November 1961, Pages 121-132

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Abstract

1.
1. An enzyme has been partially purified from Corynebacterium xerosis which catalyses the synthesis of polymetaphosphate from ATP.
2.
2. The enzyme was found to be completely inhibited by (NH₄)₂SO₄ and has an absolute requirement for Mg²⁺. ADP and AMP inhibited the synthesis at high concentrations.
3.
3. The experimental evidence obtained did not suggest the presence of a phosphate primer.
4.
4. No formation of “acid-soluble” intermediates was detected during the synthesis.
5.
5. Addition of low molecular phosphate polymers made no appreciable difference to the synthesis.
6.
6. The reversibility of the reaction, i.e. synthesis of ATP from ADP and polymetaphosphate, could not be demonstrated with the purified enzyme.

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Studies in biosynthesis of polymetaphosphate by an enzyme from Corynebacterium xerosis

Abstract

Biochim. Biophys. Acta

Biochim. Biophys. Acta

Nature

J. Chem. Soc.

Anal. Chem.

Ann. Rev. Biochem.

J. Biochem. (Tokyo)

Naturwissenschaften

Biochim. Biophys. Acta

J. Gen. Microbiol.