Article
Role of beta-lactam carboxyl group on binding of penicillins and cephalosporins to class C beta-lactamases.
Proteins - 15 May 2003
Fenollar-Ferrer Cristina, Frau Juan, Donoso Josefa, Muñoz Francisco
Abstract excerpt
Molecular models for the Henry Michaelis complexes of Enterobacter cloacae, a class C beta-lactamase, with penicillin G and cephalotin have been constructed by using molecular mechanic calculations, based on the AMBER force field, to examine the molecular differentiation mechanisms between cephalosporins and penicillins in beta-lactamases. Ser318Ala and Thr316Ala mutations in both complexes and Asn346Ala and...
Topics
- Amino Acid Substitution
- Anti-Bacterial Agents
- Binding Sites
- Binding, Competitive
- Cephalosporinase
- Cephalosporins
- Cephalothin
- Enterobacter cloacae
- Models, Molecular
- Molecular Conformation
- Mutation
- Penicillin G
- Penicillins
- Protein Structure, Tertiary
- beta-Lactamases