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 (NH 4) 2SO 4 and has an absolute requirement for Mg 2+. 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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