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- W2087126312 endingPage "9692" @default.
- W2087126312 startingPage "9654" @default.
- W2087126312 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." @default.
- W2087126312 created "2016-06-24" @default.
- W2087126312 creator A5003218918 @default.
- W2087126312 creator A5005033602 @default.
- W2087126312 creator A5011343316 @default.
- W2087126312 creator A5026735505 @default.
- W2087126312 creator A5030937637 @default.
- W2087126312 creator A5033331324 @default.
- W2087126312 creator A5083351325 @default.
- W2087126312 creator A5089359259 @default.
- W2087126312 date "2015-04-29" @default.
- W2087126312 modified "2023-10-17" @default.
- W2087126312 title "Structural Basis for Carbapenem-Hydrolyzing Mechanisms of Carbapenemases Conferring Antibiotic Resistance" @default.
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