## Abstract Herein, we present results from MD simulations of the Michaelis complex formed between the dizinc β‐lactamase from __B. fragilis__ and imipenem. We considered two catalytically important configurations, which differ in the presence or absence of a hydroxide bridge connecting the two zin
✦ LIBER ✦
Insights into the Structure and Dynamics of the Dinuclear Zinc β-Lactamase Site from Bacteroides fragilis †
✍ Scribed by Suárez, Dimas; Brothers, Edward N.; Merz, Kenneth M.
- Book ID
- 127333763
- Publisher
- American Chemical Society
- Year
- 2002
- Tongue
- English
- Weight
- 597 KB
- Volume
- 41
- Category
- Article
- ISSN
- 0006-2960
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## Abstract The metallo‐β‐lactamases require zinc or cadmium for hydrolyzing β‐lactam antibiotics and are inhibited by mercurial compounds. To date, there are no clinically useful inhibitors of this class of enzymes. The crystal structure of the Zn^2+^‐bound enzyme from __Bacteroides fragilis__ con
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