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- Title
Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance.
- Authors
Jeong Ho Jeon; Jung Hun Lee; Jae Jin Lee; Kwang Seung Park; Karim, Asad Mustafa; Chang-Ro Lee; Byeong Chul Jeong; Sang Hee Lee
- Abstract
Carbapenems (imipenem, meropenem, biapenem, ertapenem, and doripenem) are β-lactam antimicrobial agents. Because carbapenems have the broadest spectra among all β-lactams and are primarily used to treat infections by multi-resistant Gram-negative bacteria, the emergence and spread of carbapenemases became a major public health concern. Carbapenemases are the most versatile family of β-lactamases that are able to hydrolyze carbapenems and many other β-lactams. According to the dependency of divalent cations for enzyme activation, carbapenemases can be divided into metallo-carbapenemases (zinc-dependent class B) and non-metallo-carbapenemases (zinc-independent classes A, C, and D). Many studies have provided various carbapenemase structures. Here we present a comprehensive and systematic review of three-dimensional structures of carbapenemase-carbapenem complexes as well as those of carbapenemases. We update recent studies in understanding the enzymatic mechanism of each class of carbapenemase, and summarize structural insights about regions and residues that are important in acquiring the carbapenemase activity.
- Subjects
CARBAPENEMS; DRUG resistance in bacteria; HYDROLYSIS; BETA lactam antibiotics; MOLECULAR structure; ENZYME activation
- Publication
International Journal of Molecular Sciences, 2015, Vol 16, Issue 5, p9654
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms16059654