Effect of various alanine analogues on the L-alanine-adding enzyme from Escherichia coli.
An extract from Escherichia coli containing the L-alanine-adding enzyme with a high specific activity was prepared. Several compounds structurally related to L-alanine were tested as inhibitors of this activity. Intact amino and carboxyl groups were necessary for an interaction with the enzyme. Certain halogenated (haloalanines) or unsaturated (L-vinylglycine, L-propargylglycine, 3-cyano-L-alanine) amino acids were good inhibitors. Radioactive glycine, serine and 1-aminoethylphosphonic acid were tested as substrates. Whereas glycine or L-serine gave rise to the formation of the corresponding nucleotide product, no synthesis of UDP-N-acetylmuramyl-L-1-aminoethylphosphonic acid could be detected.
Liger
D
D
Enveloppes Bactériennes et Peptides, URA 1131 du CNRS, Université de Paris-Sud, Orsay, France.
Blanot
D
D
van Heijenoort
J
J
D000409:Alanine / Q000031:analogs & derivatives* / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D010453:Peptide Synthases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013379:Substrate Specificity
D010453:Peptide Synthases; C023229:UDP-N-acetylmuramoyl-alanine synthetase; D000409:Alanine