Effect of various alanine analogues on the ?-alanine-adding enzyme from Escherichia coli
- 1 May 1991
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 80 (1) , 111-115
- https://doi.org/10.1016/0378-1097(91)90218-y
Abstract
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.Keywords
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