Mechanism of inhibition of the PC1 .beta.-lactamase of Staphylococcus aureus by cephalosporins: importance of the 3'-leaving group
- 1 February 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 24 (4), 903-910
- https://doi.org/10.1021/bi00325a014
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 11 references indexed in Scilit:
- Pre-steady state beta-lactamase kinetics. The trapping of a covalent intermediate and the interpretation of pH rate profiles.Journal of Biological Chemistry, 1983
- Inhibition of the RTEM .beta.-lactamase from Escherichia coli. Interaction of the enzyme with derivatives of olivanic acidBiochemistry, 1982
- Pre-steady state beta-lactamase kinetics. Observation of a covalent intermediate during turnover of a fluorescent cephalosporin by the beta-lactamase of STaphylococcus aureus PC1.Journal of Biological Chemistry, 1981
- Inhibition of the RTEM .beta.-lactamase from Escherichia coli. Interaction of the enzyme with derivatives of olivanic acidBiochemistry, 1981
- Electronic structures of cephalosporins and penicillins. 11. Parabolic relationships between antibacterial activity of cephalosporins and .beta.-lactam reactivity predicted from molecular orbital calculationsJournal of the American Chemical Society, 1980
- Electronic structures of cephalosporins and penicillins. 9. Departure of a leaving group in cephalosporinsJournal of Medicinal Chemistry, 1979
- Reversible inhibition of penicillinase by quinacillin: Evaluation of mechanisms involving two conformational states of the enzymeBiochemical and Biophysical Research Communications, 1978
- Conformation of a stable intermediate on the folding pathway of Staphylococcus aureus penicillinaseBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Cephalosporinase and penicillinase activities of a β-lactamase from Pseudomonas pyocyaneaBiochemical Journal, 1965
- Statistical estimations in enzyme kineticsBiochemical Journal, 1961