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.-Reference-Cited by-同舟云学术

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.

Published:1981-11 Issue:22 Volume:256 Page:11401-11404
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Anderson E.G.,Pratt R.F.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference26 articles.

1. Kinetic studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acid

2. Chemical studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acid

3. 6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.

4. 6 β-Bromopenicillanic acid inactivates β-lactamase I

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1. Evidence for Structural Elasticity of Class A β-Lactamases in the Course of Catalytic Turnover of the Novel Cephalosporin Cefepime;Journal of the American Chemical Society;1996-01-01

2. ß-Lactamase: mechanism of action;The Chemistry of β-Lactams;1992

3. The role of lysine-234 in .beta.-lactamase catalysis probed by site-directed mutagenesis;Biochemistry;1990-06-19

4. Cryoenzymology of staphylococcal .beta.-lactamase: trapping a serine-70-linked acyl-enzyme;Biochemistry;1990-01-09

5. Isolation of a Staphylococcus aureus β-lactamase-dicloxacillin complex and kinetic studies on the reactivation of the enzyme;Archives of Biochemistry and Biophysics;1989-01