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Binding of D- and L-captopril inhibitors to metallo-beta-lactamase studied by polarizable molecular mechanics and quantum mechanics.

Abstract:

The bacterial Zn2+ metallo-beta-lactamase from B. fragilis is a zinc-enzyme with two potential metal ion binding sites. It cleaves the lactam ring of antibiotics, thus contributing to the acquired resistance of bacteria against antibiotics. The present study bears on the binuclear form of the enzyme. We compare several possible binding modes of captopril, a mercaptocarboxamide inhibitor of several zinc-metalloenzymes. Two diastereoisomers of captopril were considered, with either a D- or an L...

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Publication status:
Published

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Publisher copy:
10.1002/jcc.10111

Authors


Hemmingsen, L More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Journal:
Journal of computational chemistry
Volume:
23
Issue:
13
Pages:
1281-1296
Publication date:
2002-10-05
DOI:
EISSN:
1096-987X
ISSN:
0192-8651
URN:
uuid:aceb3690-bf5a-46dd-ad98-9217b9c9a437
Source identifiers:
38363
Local pid:
pubs:38363

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