Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1988 Oct 1;255(1):123–129. doi: 10.1042/bj2550123

A survey of the kinetic parameters of class C beta-lactamases. Cephalosporins and other beta-lactam compounds.

M Galleni 1, G Amicosante 1, J M Frère 1
PMCID: PMC1135199  PMID: 3264155

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.

Full text

PDF
123

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES