Bordet C, Perkins H R
Biochem J. 1970 Oct;119(5):877-83. doi: 10.1042/bj1190877.
A particulate preparation from Micrococcus lysodeikticus was used to synthesize cell-wall mucopeptide. Radioactive iodinated vancomycin became attached to the preparation simultaneously with a complete inhibition of mucopeptide synthesis. After mucopeptide synthesis had occurred in the absence of antibiotic, the preparation took up more vancomycin, suggesting that new binding sites terminating in acyl-d-alanyl-d-alanine had been produced. The mucopeptide product was divided into a soluble and an insoluble portion, both sensitive to lysozyme. The soluble portion did not combine with vancomycin and hence had presumably lost its terminal d-alanine residues, either by transpeptidation or because of carboxy-peptidase action. The synthesis of both portions was unaffected by the presence of penicillin, but the insoluble part showed increased affinity for vancomycin, thus indicating that penicillin had caused conservation of d-alanyl-d-alanine termini.
用溶壁微球菌的颗粒制剂来合成细胞壁粘肽。放射性碘化万古霉素附着于该制剂上的同时，粘肽合成被完全抑制。在无抗生素的情况下发生粘肽合成后，该制剂摄取了更多的万古霉素，这表明产生了以酰基 -d-丙氨酰 -d-丙氨酸结尾的新结合位点。粘肽产物分为可溶部分和不溶部分，二者均对溶菌酶敏感。可溶部分不与万古霉素结合，因此推测其末端d-丙氨酸残基要么通过转肽作用，要么由于羧肽酶的作用而丢失。两部分的合成均不受青霉素存在的影响，但不溶部分对万古霉素的亲和力增加，这表明青霉素导致了d-丙氨酰 -d-丙氨酸末端的保留。
