Adenyl cyclase of bacteria

Abstract

Extracts from 21 strains of bacteria were screened for adenyl cyclase activity. Adenyl cyclase from Arthrobacter globiformis, Brevibacterium liquefaciens and Micrococcus lysodeikticus was found in the 30,000 g supernatant fraction and was activated by pyruvate, whereas the enzyme from Alkaligenes faecalis, Corynebacterium equi, Erwinia carotovora, Escherichia coli, and Nocardia erythropolis was found in the 30,000 g precipitate and was not activated by pyruvate. In Arthrobacter citreus and Micrococcus flavus adenyl cyclase was found in the 30,000 g precipitate and was activated by pyruvate. Cyclic nucleotide phosphodiesterase activity was observed in extracts from some of the bacteria investigated. Serratia marcescens, Arthrobacter citreus, Brevibacterium ammoniagenes, and Erwinia carotovora contained strong phosphodiesterase activity. Adenyl cyclase of Nocardia erythropolis was studied in some detail. The enzyme required Mg 2+ or Mn 2+ for activity, Mn 2+ being far more effective than Mg 2+. The enzyme was strongly inhibited by GTP, UTP, CTP, ITP, 3′-AMP, oxalacetate, and by pyridoxal phosphate. NaF, epinephrine, and norepinephrine, compounds which stimulate animal adenyl cyclase activity, had no effect on the Nocardia enzyme.