Gutmann L, Billot-Klein D, al-Obeid S, Klare I, Francoual S, Collatz E, van Heijenoort J
Laboratoire de Microbiologie Médicale, Université Paris VI, France.
Antimicrob Agents Chemother. 1992 Jan;36(1):77-80. doi: 10.1128/AAC.36.1.77.
Vancomycin was found to coinduce DD-carboxypeptidase activity, together with resistance, in eight low- or high-level glycopeptide-resistant strains of enterococci. The constitutively resistant mutant (MT10) of a low-level-resistant strain of Enterococcus faecium (D366) spontaneously expressed a level of carboxypeptidase similar to that of the induced strain D366. Pentapeptide, UDP-MurNac-pentapeptide, as well as D-alanyl-D-alanine were in vitro substrates for the carboxypeptidase which was not inhibited by penicillin. The level of vancomycin resistance correlated roughly with the level of carboxypeptidase activity. We infer from these results that the carboxypeptidase is one component of the glycopeptide resistance mechanism.
在八株低水平或高水平糖肽耐药的肠球菌中,发现万古霉素与耐药性共同诱导DD - 羧肽酶活性。粪肠球菌(D366)低水平耐药菌株的组成型耐药突变体(MT10)自发表达的羧肽酶水平与诱导菌株D366相似。五肽、UDP - MurNac - 五肽以及D - 丙氨酰 - D - 丙氨酸是该羧肽酶的体外底物,且该羧肽酶不受青霉素抑制。万古霉素耐药水平与羧肽酶活性水平大致相关。从这些结果我们推断,羧肽酶是糖肽耐药机制的一个组成部分。