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Studies on Escherichia coli Enzymes Involved in the Synthesis of Uridine Diphosphate-N-Acetyl-Muramyl-Pentapeptide

Laboratory for Microbiology, State University, Catharijnesingel 59, Utrecht, The Netherlands

ABSTRACT

The specific activities of L-alanine:D-alanine racemase, D-alanine:D-alanine ligase, and the L-alanine, D-glutamic acid, meso-diaminopimelic acid, and D-alanyl-D-alanine adding enzymes were followed during growth of Escherichia coli. The specific activities were nearly independent of the growth phase. D-Alanine:D-alanine ligase was inhibited by D-alanyl-D-alanine, D-cycloserine, glycine, and glycyl-glycine. L-Alanine:D-alanine racemase was found to be sensitive to D-cycloserine, glycine, and glycyl-glycine. The L-alanine adding enzyme was inhibited by glycine and glycyl-glycine.

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• Herve, M., Boniface, A., Gobec, S., Blanot, D., Mengin-Lecreulx, D. (2007). Biochemical Characterization and Physiological Properties of Escherichia coli UDP-N-Acetylmuramate:L-Alanyl-{gamma}-D-Glutamyl-meso- Diaminopimelate Ligase. J. Bacteriol. 189: 3987-3995 [Abstract] [Full Text]