Abstract
beta-Lactamase I catalyses the hydrolysis of penicillins by an acyl-enzyme mechanism. A procedure was developed for determining the rate constants for the acylation and deacylation steps for the good substrates benzylpenicillin and phenoxymethylpenicillin; this depends on determining the fraction of enzyme that is present as acyl-enzyme in the steady state.
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Selected References
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- Baldwin G. S., Edwards G. F., Kiener P. A., Tully M. J., Waley S. G., Abraham E. P. Production of a variant of beta-lactamase II with selectively decreased cephalosporinase activity by a mutant of Bacillus cereus 569/H/9. Biochem J. 1980 Oct 1;191(1):111–116. doi: 10.1042/bj1910111. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bicknell R., Waley S. G. Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by beta-lactamase I from Bacillus cereus. Biochem J. 1985 Oct 1;231(1):83–88. doi: 10.1042/bj2310083. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Davies R. B., Abraham E. P. Separation, purification and properties of beta-lactamase I and beta-lactamase II from Bacillus cereus 569/H/9. Biochem J. 1974 Oct;143(1):115–127. doi: 10.1042/bj1430115. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Duggleby R. G. Progress-curve analysis in enzyme kinetics. Numerical solution of integrated rate equations. Biochem J. 1986 Apr 15;235(2):613–615. doi: 10.1042/bj2350613. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Froede H. C., Wilson I. B. Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine. J Biol Chem. 1984 Sep 10;259(17):11010–11013. [PubMed] [Google Scholar]
- Hardy L. W., Kirsch J. F. Diffusion-limited component of reactions catalyzed by Bacillus cereus beta-lactamase I. Biochemistry. 1984 Mar;23(6):1275–1282. doi: 10.1021/bi00301a040. [DOI] [PubMed] [Google Scholar]
- Herzberg O., Moult J. Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5 A resolution. Science. 1987 May 8;236(4802):694–701. doi: 10.1126/science.3107125. [DOI] [PubMed] [Google Scholar]
- Knott-Hunziker V., Orlek B. S., Sammes P. G., Waley S. G. 6 beta-Bromopenicillanic acid inactivates beta-lactamase I. Biochem J. 1979 Jan 1;177(1):365–367. doi: 10.1042/bj1770365. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Madgwick P. J., Waley S. G. beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis. Biochem J. 1987 Dec 15;248(3):657–662. doi: 10.1042/bj2480657. [DOI] [PMC free article] [PubMed] [Google Scholar]
- PARKER C. W., DEWECK A. L., KERN M., EISEN H. N. The preparation and some properties of penicillenic acid derivatives relevant to penicillin hypersensitivity. J Exp Med. 1962 Apr 1;115:803–819. doi: 10.1084/jem.115.4.803. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Samraoui B., Sutton B. J., Todd R. J., Artymiuk P. J., Waley S. G., Phillips D. C. Tertiary structural similarity between a class A beta-lactamase and a penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase. 1986 Mar 27-Apr 2Nature. 320(6060):378–380. doi: 10.1038/320378a0. [DOI] [PubMed] [Google Scholar]
- Samuni A. A direct spectrophotometric assay and determination of Michaelis constants for the beta-lactamase reaction. Anal Biochem. 1975 Jan;63(1):17–26. doi: 10.1016/0003-2697(75)90185-2. [DOI] [PubMed] [Google Scholar]
- Waley S. G. A spectrophotometric assay of beta-lactamase action on penicillins. Biochem J. 1974 Jun;139(3):789–790. doi: 10.1042/bj1390789. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wharton C. W., Szawelski R. J. Half-time analysis of the integrated Michaelis equation. Simulation and use of the half-time plot and its direct linear variant in the analysis of some alpha-chymotrypsin, papain- and fumarase-catalysed reactions. Biochem J. 1982 May 1;203(2):351–360. doi: 10.1042/bj2030351. [DOI] [PMC free article] [PubMed] [Google Scholar]