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Guanylate cyclase activity in Escherichia coli mutants defective in adenylate cyclase
Author(s) -
Vincenzo Macchia,
Gregory A. Caputo,
E Mandato,
A Rocino,
Sankar Adhya,
Ira Pastan
Publication year - 1981
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.147.3.931-934.1981
Subject(s) - cyclase , adenylate kinase , biology , guanylate cyclase 2c , gucy1a3 , gucy1b3 , gucy2d , escherichia coli , biochemistry , guanosine , mutant , guanosine triphosphate , growth hormone releasing hormone receptor , adenosine , enzyme , gtp' , gene , genetics , cancer , breast cancer , hormone receptor
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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