Work

Escherichia coli mutants completely deficient in adenosylmethionine decarboxylase and in spermidine biosynthesis.

Year: 1978

Type: article

Abstract: Mutants of Escherichia coli deficient in adenosylmethionine decarboxylase, an enzyme in the biosynthetic pathway for spermidine, were isolated after mutagenesis of E. coli K 12 with N-methyl-N-nitro-N-nitrosoguanidine or with the bacteriophage Mu. The mutated gene, designated speD, is at 2.7 min on the E. coli chromosome map. In several of the mutants resulting from Mu insertion both adenosylmethionine decarboxylase activity and spermidine were undetectable. The absence of spermidine from speD strains proves the essential role of adenosylmethionine decarboxylase in the biosynthetic pathway for spermidine. Despite the complete absence of spermidine, these mutants grew at 75% of the wild type rate.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(17)34853-6

Authors: C.W. Tabor, H. Tabor, E.W. Hafner

Institutions: National Institutes of Health, National Institute of Arthritis and Musculoskeletal and Skin Diseases

Language: English

Topic: Polyamine Metabolism and Applications

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1563103338

FWCI: 2.629

Cites: 32

Cited by: 56

Related to: 10