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Appl Environ Microbiol. 1968 October; 16(10): 1543-1547
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

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

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.

¹ Present address: Department of Biological Sciences, Purdue University, Lafayette, Ind. 47907.