Abstract
Hammel, Jay M. (The Pennsylvania State University, University Park) and L. N. Zimmerman. Growth stimulation of Streptococcus faecalis var. liquefaciens by canavanine. J. Bacteriol. 86:490–493. 1963.—l-Canavanine, a competitive inhibitor of arginine, was found to stimulate the growth of Streptococcus faecalis var. liquefaciens in the presence of arginine. This growth stimulation by canavanine was unique, since it previously was found to inhibit the growth of organisms which require arginine. When equimolar concentrations of arginine and canavanine were tested from 10−7 to 10−2m, maximal stimulation occurred at 10−4m. Canavanine concentrations of 5 × 10−6m to 10−2m stimulated growth in the presence of 5 × 10−5m arginine. Ornithine similarly stimulated growth. Canavanine inhibited the rate of arginine degradation by the arginine dihydrolase enzyme system in intact cells. It is assumed that the mechanism of canavanine stimulation involves an inhibition of arginine desimidase of the arginine dihydrolase enzyme system, which in turn makes more arginine available for growth over a longer period of time.
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Selected References
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- HARTMAN R. E., ZIMMERMAN L. N. Effect of the arginine dihydrolase enzyme system on proteinase biosynthesis by Streptococcus faecalis var. liquefaciens. J Bacteriol. 1960 Dec;80:753–761. doi: 10.1128/jb.80.6.753-761.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hills G. M. Ammonia production by pathogenic bacteria. Biochem J. 1940 Jul;34(7):1057–1069. doi: 10.1042/bj0341057. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KIHARA H., PRESCOTT J. M., SNELL E. E. The bacterial cleavage of canavanine to homoserine and guanidine. J Biol Chem. 1955 Nov;217(1):497–503. [PubMed] [Google Scholar]
- KIHARA H., SNELL E. E. The enzymatic cleavage of canavanine to O-ureidohomoserine and ammonia. J Biol Chem. 1957 May;226(1):485–495. [PubMed] [Google Scholar]
- KNIVETT V. A. Phosphorylation coupled with anaerobic breakdown of citrulline. Biochem J. 1954 Apr;56(4):602–606. [PMC free article] [PubMed] [Google Scholar]
- OGINSKY E. L., GEHRIG R. F. The arginine dihydrolase system of Streptococcus faecalis. I. Identification of citrulline as an intermediate. J Biol Chem. 1952 Oct;198(2):791–797. [PubMed] [Google Scholar]
- OGINSKY E. L., GEHRIG R. F. The arginine dihydrolase system of Streptococcus faecalis. II. Properties of arginine desimidase. J Biol Chem. 1952 Oct;198(2):799–805. [PubMed] [Google Scholar]
- SLADE H. D. Hydrolysis of arginine by soluble enzymes of Streptococcus faecalis. Arch Biochem Biophys. 1953 Jan;42(1):204–211. doi: 10.1016/0003-9861(53)90253-7. [DOI] [PubMed] [Google Scholar]
- WALKER J. B. Further studies on the mechanism of transamidinase action: transamidination in Streptomyces griseus. J Biol Chem. 1958 Mar;231(1):1–9. [PubMed] [Google Scholar]