PMID:8550531
| Citation |
Gubler, M, Appoldt, Y and Keck, W (1996) Overexpression, purification, and characterization of UDP-N-acetylmuramyl:L-alanine ligase from Escherichia coli. J. Bacteriol. 178:906-10 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
Amino Acid Sequence; Base Sequence; Escherichia coli/enzymology; Kinetics; Ligases/antagonists & inhibitors; Ligases/isolation & purification; Ligases/metabolism; Molecular Sequence Data; Substrate Specificity; Uridine Diphosphate N-Acetylmuramic Acid/analogs & derivatives; Uridine Diphosphate N-Acetylmuramic Acid/metabolism |
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