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J. Bacteriol., Feb 1996, 906-910, Vol 178, No. 3
Copyright © 1996, American Society for Microbiology

Overexpression, purification, and characterization of UDP-N- acetylmuramyl:L-alanine ligase from Escherichia coli

M Gubler, Y Appoldt and W Keck
Department of Infectious Diseases, F. Hoffman-La Roche AG, CH-4002 Basel, Switzerland.

UDP-N-acetylmuramyl:L-alanine ligase from Escherichia coli was overexpressed more than 600-fold and purified to near homogeneity. The purified enzyme was found to ligate L-alanine, L-serine, and glycine, as well as the nonnatural amino acid beta-chloro-L-alanine, to UDP-N- acetylmuramic acid. On the basis of (i) the specificity constants of the enzyme determined for L-alanine, L-serine, and glycine and (ii) the levels of these amino acids in the intracellular pool, it was calculated that the rates of incorporation of L-serine and glycine into peptidoglycan precursor metabolites could maximally amount to 0.1 and 0.5%, respectively, of the rate of L-alanine incorporation.

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