Metabolism of D-serine in Escherichia coli K-12: mechanism of growth inhibition

J Bacteriol. 1973 May;114(2):685-94. doi: 10.1128/jb.114.2.685-694.1973.


Without significant killing, d-serine at concentrations greater than 50 mug/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.

MeSH terms

  • Bacterial Proteins / biosynthesis
  • Carbon Isotopes
  • Cell-Free System
  • Escherichia coli / enzymology
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism*
  • Isomerases / metabolism
  • L-Serine Dehydratase / biosynthesis
  • Mutation
  • Pantothenic Acid / biosynthesis
  • Serine / metabolism*
  • Serine / pharmacology
  • Stereoisomerism
  • Tritium


  • Bacterial Proteins
  • Carbon Isotopes
  • Tritium
  • Pantothenic Acid
  • Serine
  • L-Serine Dehydratase
  • Isomerases