Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure

Author:

Knox J R1

Affiliation:

1. Department of Molecular and Cell Biology, University of Connecticut, Storrs 06269-3125, USA. knox@uconnvm.uconn.edu

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Reference93 articles.

1. Site-directed mutants, at position 166, of RTEM-1 ~-lactamase that form a stable acyl-enzyme intermediate with penicillin;Adachi H.;J. Biol. Chem.,1991

2. A standard numbering scheme for class A ~-lactamases;Ambler R. P.;Biochem. J.,1991

3. Belaaouaj A. C. Lapoumeroulie G. Vedel P. Nevot R. Krishnamoorthy and G. Paul. 1991. Amino acid 241 of TEM-1 is highly critical in conferring resistance to ampicillin-clavulanic acid combination: molecular characterization of a natural mutant abstr. 944 p. 256. In Program and abstracts of the 31st Interscience Conference on Antimicrobial Agents and Chemotherapy. American Society for Microbiology Washington D.C.

4. Characterization of a new TEM-type ~-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli;Blazquez J.;Antimicrob. Agents Chemother.,1993

5. Nucleotide sequence of the PSE-4 carbenicillinase gene and correlations with the Staphylococcus aureus PC1 ~-lactamase crystal structure;Boissinot M.;J. Biol. Chem.,1990

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