Liger D, Blanot D, van Heijenoort J
Enveloppes Bactériennes et Peptides, URA 1131 du CNRS, Université de Paris-Sud, Orsay, France.
FEMS Microbiol Lett. 1991 May 1;64(1):111-5. doi: 10.1016/0378-1097(91)90218-y.
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.
制备了来自大肠杆菌的一种提取物，其含有具有高比活性的L-丙氨酸添加酶。测试了几种与L-丙氨酸结构相关的化合物作为该活性的抑制剂。完整的氨基和羧基对于与该酶相互作用是必需的。某些卤代（卤代丙氨酸）或不饱和（L-乙烯基甘氨酸、L-炔丙基甘氨酸、3-氰基-L-丙氨酸）氨基酸是良好的抑制剂。测试了放射性甘氨酸、丝氨酸和1-氨基乙基膦酸作为底物。虽然甘氨酸或L-丝氨酸导致相应核苷酸产物的形成，但未检测到UDP-N-乙酰胞壁酰-L-1-氨基乙基膦酸的合成。
