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β-内酰胺酶的多样性、结构及调控

The diversity, structure and regulation of beta-lactamases.

作者信息

Philippon A, Dusart J, Joris B, Frère J M

机构信息

Université Paris VII, Hôpital Cochin, Service de Bactériologie, France.

出版信息

Cell Mol Life Sci. 1998 Apr;54(4):341-6. doi: 10.1007/s000180050161.

DOI:10.1007/s000180050161
PMID:9614970
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11147397/
Abstract

beta-Lactamase production is responsible for the appearance of a large number of pathogenic bacterial strains exhibiting a high degree of resistance to beta-lactam antibiotics. A large number of enzymes have been described with very diverse primary structures and catalytic profiles. Nevertheless, all known three-dimensional structures of active-site serine beta-lactamases exhibit a high degree of similarity with apparently equivalent chemical functionalities in the same strategic positions. These groups might not, however, play identical roles in the various classes of enzymes. Structural data have also been recently obtained for the zinc metallo-beta-lactamases, but the detailed catalytic mechanisms might also differ widely, depending on the enzyme studied. Similarly, the induction of the synthesis of beta-lactamases is now better understood, but many questions remain to be answered.

摘要

β-内酰胺酶的产生导致了大量对β-内酰胺抗生素具有高度抗性的致病细菌菌株的出现。已经描述了许多具有非常不同的一级结构和催化特性的酶。然而,活性位点丝氨酸β-内酰胺酶的所有已知三维结构在相同的关键位置都表现出高度相似性,且具有明显等效的化学功能。然而,这些基团在各类酶中可能并不发挥相同的作用。最近也获得了锌金属β-内酰胺酶的结构数据,但具体的催化机制可能也因所研究的酶而有很大差异。同样,现在对β-内酰胺酶合成的诱导有了更好的理解,但仍有许多问题有待解答。