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. 1973 May;114(2):685–694. doi: 10.1128/jb.114.2.685-694.1973

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

Sharon D Cosloy a,2, Elizabeth McFall a
PMCID: PMC251827  PMID: 4574697

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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