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J Bacteriol. 1973 May; 114(2): 685-694
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

Metabolism of D-Serine in Escherichia coli K-12: Mechanism of Growth Inhibition1

Sharon D. Cosloy2 and Elizabeth McFall

a Department of Microbiology, New York University School of Medicine, New York, New York 10016

ABSTRACT

Without significant killing, D-serine at concentrations greater than 50 µg/ml inhibits growth in minimal media of mutants of Escherichia coli K-12 unable to form D-serine deaminase. The mutants eventually recover at lower concentrations. There is no evidence of D-serine toxicity in rich media. Toxicity is partially reversed by L-serine. D-Serine does not interfere with L-serine activation, one-carbon metabolism, or (Cronan, personal communication) formation of phosphatidylserine. Pizer (personal communication) finds, however, that it is a powerful feedback inhibitor of the first enzyme of L-serine biosynthesis. In the presence of L-serine, the residual toxicity is largely and noncompetitively over come by pantothenate, indicating that D-serine inhibits growth by affecting two targets: pantothenate biosynthesis and L-serine biosynthesis. L-Serine causes transient growth inhibition in E. coli K-12. Contaminating L-serine in D-serine preparations contributes to the D-serine inhibitory response.


FOOTNOTES

2 Present address: Department of Genetics, Public Health Research Institute of the City of New York, New York, N.Y. 10016.

1 Submitted by S.D.C. in partial fulfillment of the requirements for the Ph.D. degree at New York University School of Medicine, New York, N.Y.


J Bacteriol. 1973 May; 114(2): 685-694
Copyright © 1973 American Society for Microbiology. All Rights Reserved.




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