Abstract
Various cephalosporins, cefoxitin, moxalactam, imipenem and aztreonam were studied as substrates of six class C beta-lactamases. Nitrocefin, cephaloridine, cefazolin, cephalothin and cephalexin were good substrates, with kcat. values ranging from 27 to 5000 s-1. Cefuroxime, cefotaxime and cefoxitin exhibited low kcat. values (0.010-1.7 s-1) and low Km values, which suggested a rate-limiting deacylation. Imipenem and aztreonam were even poorer substrates (kcat. 2 x 10(-4)-3 x 10(-2) s-1) and, in the presence of a reporter substrate, behaved as transient inactivators. With moxalactam, biphasic kinetics were observed, indicating a possible rearrangement of the acyl-enzyme.
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Selected References
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- Berks M., Redhead K., Abraham E. P. Isolation and properties of an inducible and a constitutive beta-lactamase from Pseudomonas aeruginosa. J Gen Microbiol. 1982 Jan;128(1):155–159. doi: 10.1099/00221287-128-1-155. [DOI] [PubMed] [Google Scholar]
- Bush K., Freudenberger J. S., Sykes R. B. Interaction of azthreonam and related monobactams with beta-lactamases from gram-negative bacteria. Antimicrob Agents Chemother. 1982 Sep;22(3):414–420. doi: 10.1128/aac.22.3.414. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cartwright S. J., Waley S. G. beta-Lactamase inhibitors. Med Res Rev. 1983 Oct-Dec;3(4):341–382. doi: 10.1002/med.2610030402. [DOI] [PubMed] [Google Scholar]
- De Meester F., Frère J. M., Waley S. G., Cartwright S. J., Virden R., Lindberg F. 6-beta-Iodopenicillanate as a probe for the classification of beta-lactamases. Biochem J. 1986 Nov 1;239(3):575–580. doi: 10.1042/bj2390575. [DOI] [PMC free article] [PubMed] [Google Scholar]
- De Meester F., Joris B., Reckinger G., Bellefroid-Bourguignon C., Frère J. M., Waley S. G. Automated analysis of enzyme inactivation phenomena. Application to beta-lactamases and DD-peptidases. Biochem Pharmacol. 1987 Jul 15;36(14):2393–2403. doi: 10.1016/0006-2952(87)90609-5. [DOI] [PubMed] [Google Scholar]
- Faraci W. S., Pratt R. F. Mechanism of inhibition of the PC1 beta-lactamase of Staphylococcus aureus by cephalosporins: importance of the 3'-leaving group. Biochemistry. 1985 Feb 12;24(4):903–910. doi: 10.1021/bi00325a014. [DOI] [PubMed] [Google Scholar]
- Frère J. M., Joris B., Varetto L., Crine M. Structure-activity relationships in the beta-lactam family: an impossible dream. Biochem Pharmacol. 1988 Jan 1;37(1):125–132. doi: 10.1016/0006-2952(88)90764-2. [DOI] [PubMed] [Google Scholar]
- Galleni M., Frère J. M. A survey of the kinetic parameters of class C beta-lactamases. Penicillins. Biochem J. 1988 Oct 1;255(1):119–122. doi: 10.1042/bj2550119. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Joris B., De Meester F., Galleni M., Masson S., Dusart J., Frère J. M., Van Beeumen J., Bush K., Sykes R. Properties of a class C beta-lactamase from Serratia marcescens. Biochem J. 1986 Nov 1;239(3):581–586. doi: 10.1042/bj2390581. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Joris B., De Meester F., Galleni M., Reckinger G., Coyette J., Frere J. M., Van Beeumen J. The beta-lactamase of Enterobacter cloacae P99. Chemical properties, N-terminal sequence and interaction with 6 beta-halogenopenicillanates. Biochem J. 1985 May 15;228(1):241–248. doi: 10.1042/bj2280241. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Knott-Hunziker V., Petursson S., Waley S. G., Jaurin B., Grundström T. The acyl-enzyme mechanism of beta-lactamase action. The evidence for class C Beta-lactamases. Biochem J. 1982 Nov 1;207(2):315–322. doi: 10.1042/bj2070315. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Letarte R., Devaud-Felix M., Pechere J. C., Allard-Leprohon D. Enzymatic and immunological characterization of a new cephalosporinase from Enterobacter aerogenes. Antimicrob Agents Chemother. 1977 Aug;12(2):201–205. doi: 10.1128/aac.12.2.201. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Livermore D. M. Kinetics and significance of the activity of the Sabath and Abrahams' beta-lactamase of Pseudomonas aeruginosa against cefotaxime and cefsulodin. J Antimicrob Chemother. 1983 Feb;11(2):169–179. doi: 10.1093/jac/11.2.169. [DOI] [PubMed] [Google Scholar]
- Minami S., Inoue M., Mitsuhashi S. Purification and properties of a cephalosporinase from Enterobacter cloacae. Antimicrob Agents Chemother. 1980 Dec;18(6):853–857. doi: 10.1128/aac.18.6.853. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nikaido H., Normark S. Sensitivity of Escherichia coli to various beta-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic beta-lactamases: a quantitative predictive treatment. Mol Microbiol. 1987 Jul;1(1):29–36. doi: 10.1111/j.1365-2958.1987.tb00523.x. [DOI] [PubMed] [Google Scholar]
- Richmond M. H., Sykes R. B. The beta-lactamases of gram-negative bacteria and their possible physiological role. Adv Microb Physiol. 1973;9:31–88. doi: 10.1016/s0065-2911(08)60376-8. [DOI] [PubMed] [Google Scholar]
- Seeberg A. H., Tolxdorff-Neutzling R. M., Wiedemann B. Chromosomal beta-lactamases of Enterobacter cloacae are responsible for resistance to third-generation cephalosporins. Antimicrob Agents Chemother. 1983 Jun;23(6):918–925. doi: 10.1128/aac.23.6.918. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tajima M., Takenouchi Y., Sugawara S., Inoue M., Mitsuhashi S. Purification and properties of chromosomally mediated beta-lactamase from Citrobacter freundii GN7391. J Gen Microbiol. 1980 Dec;121(2):449–456. doi: 10.1099/00221287-121-2-449. [DOI] [PubMed] [Google Scholar]