PMID:2440022
| Citation |
Panagiotidis, CA, Blackburn, S, Low, KB and Canellakis, ES (1987) Biosynthesis of polyamines in ornithine decarboxylase, arginine decarboxylase, and agmatine ureohydrolase deletion mutants of Escherichia coli strain K-12. Proc. Natl. Acad. Sci. U.S.A. 84:4423-7 |
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| Abstract |
Escherichia coli K-12 mutants that carry deletions in their genes for ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) (speC), arginine decarboxylase (L-arginine carboxy-lyase, EC 4.1.1.19) (speA), and agmatine ureohydrolase (agmatinase or agmatine amidinohydrolase, EC 3.5.3.11) (speB) can still synthesize very small amounts of putrescine and spermidine. The putrescine concentration in these mutants was found to be 1/2500th that in spe+ cells. The pathway of putrescine synthesis appears to be through the biodegradative arginine decarboxylase, which converts arginine to agmatine, in combination with a low agmatine ureohydrolase activity--1/2000th that in spe+ strains. These results suggest that even such low levels of polyamines permit a low level of protein synthesis. Evidence is presented that the polyamine requirement for the growth of the polyamine-dependent speAB, speC deletion mutants, which are also streptomycin resistant, is not due to a decreased ability to synthesize polyamines. |
| Links | |
| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carboxy-Lyases/genetics; Carboxy-Lyases/metabolism; Drug Resistance, Microbial; Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/genetics; Genes; Genes, Bacterial; Ornithine Decarboxylase/genetics; Ornithine Decarboxylase/metabolism; Phenotype; Polyamines/biosynthesis; Putrescine/biosynthesis; RNA, Bacterial/biosynthesis; Streptomycin/pharmacology; Ureohydrolases/genetics; Ureohydrolases/metabolism |
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