Mono- and binuclear Zn-β-lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ions
✍ Scribed by Raquel Paul-Soto; Maria Hernandez-Valladares; Moreno Galleni; Rogert Bauer; Michael Zeppezauer; Jean-Marie Frère; Hans-Werner Adolph
- Book ID
- 117109921
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 95 KB
- Volume
- 438
- Category
- Article
- ISSN
- 0014-5793
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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
## 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