Catabolism of Adenosine 5'-Monophosphate by Extracts of the Marine Bacterium Beneckea natriegens

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Abstract
SUMMARY: AMP is catabolized by cell-free extracts of Beneckea natriegens to inosine via adenosine by AMP nucleotidase and adenosine deaminase. In the presence of ATP, the AMP nucleotidase is inhibited and an AMP deaminase is activated, resulting in formation of IMP. When low concentrations of ATP are used, the IMP is converted, simultaneously with ATP consumption, to inosine by IMP nucleotidase, which is presumably ATP-sensitive. Since 5'-nucleotidases from various organisms are known to catabolize several ribonucleoside monophosphates, the AMP and IMP nucleotidase activities of B. natriegens may be due to the same enzyme. CTP, GTP and UTP inhibit AMP nucleotidase from B. natriegens without stimulating AMP deaminase, thus severely decreasing the rate of AMP breakdown.