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. 1981 Sep;147(3):931–934. doi: 10.1128/jb.147.3.931-934.1981

Guanylate cyclase activity in Escherichia coli mutants defective in adenylate cyclase.

V Macchia, G Caputo, E Mandato, A Rocino, S Adhya, I Pastan
PMCID: PMC216130  PMID: 6115852

Abstract

Guanylate cyclase, which catalyzes the synthesis of guanosine 3',5'-monophosphate, has been assayed in several strains of Escherichia coli. They include wild-type cells and mutants defective in adenylate cyclase, which is responsible for the synthesis of adenosine 3',5'-phosphate. Our results demonstrate that adenylate cyclase and guanylate cyclase are two different enzymes in E. coli and suggest that the gene that encodes adenylate cyclase also plays a regulatory role in the synthesis of guanylate cyclase.

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Selected References

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