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Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2).

ABSTRACT: Carbapenem-resistant Enterobacteriaceae are resistant to most ?-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A ?-lactamase. Here, we present the first product complex crystal structures of KPC-2 with ?-lactam antibiotics containing hydrolyzed cefotaxime and faropenem. They provide experimental insights into substrate recognition by KPC-2 and its unique cephalosporinase/carbapenemase activity. These structures also represent the first product complexes for a wild-type serine ?-lactamase, elucidating the product release mechanism of these enzymes in general.

SUBMITTER: Pemberton OA 

PROVIDER: S-EPMC5506774 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

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Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2).

Pemberton Orville A OA   Zhang Xiujun X   Chen Yu Y  

Journal of medicinal chemistry 20170417 8

Carbapenem-resistant Enterobacteriaceae are resistant to most β-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A β-lactamase. Here, we present the first product complex crystal structures of KPC-2 with β-lactam antibiotics containing hydrolyzed cefotaxime and faropenem. They provide experimental insights into substrate recognition by KPC-2 and its unique cephalosporinase/carbapenemase activity. These structures also represent the first product c  ...[more]

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