Activities of Arginine Dihydrolase and Phosphatase in Streptococcus faecalis and Streptococcus faecium

Author:

Mackey Jesse K.1,Beck Raymond W.1

Affiliation:

1. Department of Microbiology, University of Tennessee, Knoxville, Tennessee 37916

Abstract

Strains of Streptococcus faecalis and S. faecium are known to produce ammonia from arginine, but only S. faecalis couples the adenosine triphosphate (ATP) produced through the arginine dihydrolase pathway to growth processes. The specific activities of the arginine dihydrolase enzymes were found to be much lower in S. faecium (0.01 to 0.10) than in S. faecalis (0.24 to 1.60). Phosphatase activities in both strains were similar (up to 0.11), but equaled or exceeded the activities of the arginine dihydrolase enzymes in S. faecium . The failure of S. faecium to show increased growth in arginine media is explained on the basis of low activities of the arginine dihydrolase enzymes coupled with sufficient phosphatase activity to negate any benefit from ATP formed.

Publisher

American Society for Microbiology

Subject

General Pharmacology, Toxicology and Pharmaceutics,General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine

Reference22 articles.

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5. Utilization of arginine as an energy source for the growth of Streptococcus faecalis;Deibel R. H.;J. Bacteriol.,1964

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