Evidence for Structural Elasticity of Class A β-Lactamases in the Course of Catalytic Turnover of the Novel Cephalosporin Cefepime
Author:
Affiliation:
1. Contribution from the Departments of Chemistry, Medicine, and Biochemistry, Wayne State University, Detroit, Michigan 48202
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja9529753
Reference42 articles.
1. Inactivation of class A .beta.-lactamases by clavulanic acid: the role of arginine-244 in a proposed nonconcerted sequence of events
2. A Structure-Based Analysis of the Inhibition of Class A .beta.-Lactamases by Sulbactam
3. Penem BRL 42715: An Effective Inactivator for .beta.-Lactamases
4. Facilitation of the .DELTA.2 .fwdarw. .DELTA.1 pyrroline tautomerization of carbapenem antibiotics by the highly conserved arginine-244 of class A .beta.-lactamases during the course of turnover
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