Meropenem and Chromacef Intermediates Observed in IMP-25 Metallo-β-Lactamase-Catalyzed Hydrolysis | Zendy

Peter Oelschlaeger | Zendy; Mahesh Aitha | Zendy; Hao Yang | Zendy; Joon S. Kang | Zendy; Antonia L. Zhang | Zendy; Eleanor M. Liu | Zendy; John D. Buynak | Zendy; Michael W. Crowder | Zendy

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Meropenem and Chromacef Intermediates Observed in IMP-25 Metallo-β-Lactamase-Catalyzed Hydrolysis

Author(s) -

Peter Oelschlaeger,

Mahesh Aitha,

Hao Yang,

Joon S. Kang,

Antonia L. Zhang,

Eleanor M. Liu,

John D. Buynak,

Michael W. Crowder

Publication year - 2015

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.04409-14

Subject(s) - hydrolysis , meropenem , catalysis , lactam , chemistry , enzyme , stereochemistry , reaction intermediate , active site , antibiotics , combinatorial chemistry , biochemistry , medicinal chemistry , antibiotic resistance

Metallo-β-lactamases inactivate most β-lactam antibacterials, and much attention has been paid to their catalytic mechanism. One issue of controversy has been whether β-lactam hydrolysis generally proceeds through an anionic intermediate bound to the active-site Zn(II) ions or not. The formation of an intermediate has not been shown conclusively in imipenemase (IMP) enzymes to date. Here, we provide evidence that intermediates are formed during the hydrolysis of meropenem and chromacef catalyzed by the variant IMP-25 and, to a lesser degree, IMP-1.

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