Inactivation of Bacillus cereus .beta.-lactamase I by 6.beta.-bromopenicillanic acid: mechanism
- 19 August 1980
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 19 (17) , 3996-4003
- https://doi.org/10.1021/bi00558a017
Abstract
Note: In lieu of an abstract, this is the article's first page.Keywords
This publication has 11 references indexed in Scilit:
- Purification of hog liver isomerase. Mechanism of isomerization of 3-alkenyl and 3-alkynyl thioesters.Journal of Biological Chemistry, 1979
- Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.Proceedings of the National Academy of Sciences, 1979
- The inhibition of staphylococcal β-lactamase by clavulanic acidBiochemical Journal, 1979
- 6 β-Bromopenicillanic acid inactivates β-lactamase IBiochemical Journal, 1979
- 6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.Proceedings of the National Academy of Sciences, 1978
- CP-45,899, a Beta-Lactamase Inhibitor That Extends the Antibacterial Spectrum of Beta-Lactams: Initial Bacteriological CharacterizationAntimicrobial Agents and Chemotherapy, 1978
- Epimerization of 6.alpha.-bromopenicillanic acid and preparation of 6.beta.-bromopenicillanic acidThe Journal of Organic Chemistry, 1978
- Reversible inhibition of penicillinase by quinacillin: Evaluation of mechanisms involving two conformational states of the enzymeBiochemical and Biophysical Research Communications, 1978
- Chemical studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acidBiochemistry, 1978
- Kinetic studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acidBiochemistry, 1978