Sawai T
Division of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University.
Nihon Rinsho. 1997 May;55(5):1225-30.
The beta-lactamases are bacterial enzymes that inactivate beta-lactam antibiotics by catalyzing the hydrolysis of the amide group of the beta-lactam ring. They are the source of much bacterial resistance to those antibiotics. Structural studies on the enzymes, i.e., penicillinases and cephalosporinases, are now well-advanced and the up-to-date knowledge of this research field were explained together with the proposed mechanism of beta-lactam hydrolysis by a cephalosporinase. After the introduction of the beta-lactamase-stable beta-lactams such as oxyimino cephalosporins, R plasmid-mediated penicillinases and a chromosomal cephalosporinase have been found to be adapted to the new drugs by mutation. The characteristics of the mutant beta-lactamases and their importance in the bacterial resistance to the new beta-lactams were explained.
β-内酰胺酶是一类细菌酶,可通过催化β-内酰胺环酰胺基团的水解作用使β-内酰胺抗生素失活。它们是细菌对这些抗生素产生耐药性的主要原因。目前,关于这些酶(即青霉素酶和头孢菌素酶)的结构研究已取得很大进展,本文结合头孢菌素酶催化β-内酰胺水解的推测机制,对该研究领域的最新知识进行了解释。在引入了对β-内酰胺酶稳定的β-内酰胺类药物(如肟基头孢菌素)后,已发现R质粒介导的青霉素酶和一种染色体头孢菌素酶通过突变适应了这些新药。本文还解释了突变型β-内酰胺酶的特性及其在细菌对新型β-内酰胺类药物耐药性中的重要性。