Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1990 Nov 1;271(3):729–734. doi: 10.1042/bj2710729

Characterization of a beta-lactamase produced in Mycobacterium fortuitum D316.

G Amicosante 1, N Franceschini 1, B Segatore 1, A Oratore 1, L Fattorini 1, G Orefici 1, J Van Beeumen 1, J M Frere 1
PMCID: PMC1149623  PMID: 2123098

Abstract

A beta-lactamase from Mycobacterium fortuitum D316 was purified and some physico-chemical properties and substrate profile determined. On the basis of its N-terminal sequence and of its sensitivity to beta-iodopenicillanate inactivation, the enzyme appeared to be a class A beta-lactamase, but its substrate profile was quite unexpected, since nine cephalosporins were among the eleven best substrates. The enzyme also hydrolysed ureidopenicillins and some so-called 'beta-lactamase-stable' cephalosporins.

Full text

PDF
729

Images in this article

730Fig. 1.
on p.730

Selected References

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

  1. Ambler R. P. The structure of beta-lactamases. Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):321–331. doi: 10.1098/rstb.1980.0049. [DOI] [PubMed] [Google Scholar]
  2. Amicosante G., Oratore A., Franceschini N., Maccarrone M., Strom R., Galleni M., Frère J. M. Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties. Biochem J. 1988 Sep 15;254(3):885–890. doi: 10.1042/bj2540885. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bidlingmeyer B. A., Cohen S. A., Tarvin T. L. Rapid analysis of amino acids using pre-column derivatization. J Chromatogr. 1984 Dec 7;336(1):93–104. doi: 10.1016/s0378-4347(00)85133-6. [DOI] [PubMed] [Google Scholar]
  4. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  5. Bush K. Classification of beta-lactamases: groups 1, 2a, 2b, and 2b'. Antimicrob Agents Chemother. 1989 Mar;33(3):264–270. doi: 10.1128/aac.33.3.264. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cavallini D., Graziani M. T., Dupré S. Determination of disulphide groups in proteins. Nature. 1966 Oct 15;212(5059):294–295. doi: 10.1038/212294a0. [DOI] [PubMed] [Google Scholar]
  7. Choubey D., Gopinathan K. P. Characterization of beta-lactamase from Mycobacterium butyricum ATCC 19979. Biochem Int. 1986 Feb;12(2):207–214. [PubMed] [Google Scholar]
  8. Cynamon M. H., Palmer G. S. In vitro susceptibility of Mycobacterium fortuitum to N-formimidoyl thienamycin and several cephamycins. Antimicrob Agents Chemother. 1982 Dec;22(6):1079–1081. doi: 10.1128/aac.22.6.1079. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Cynamon M. H., Palmer G. S. In vitro susceptibility of Mycobacterium fortuitum to amoxicillin or cephalothin in combination with clavulanic acid. Antimicrob Agents Chemother. 1983 Jun;23(6):935–937. doi: 10.1128/aac.23.6.935. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Dale J. W., Godwin D., Mossakowska D., Stephenson P., Wall S. Sequence of the OXA2 beta-lactamase: comparison with other penicillin-reactive enzymes. FEBS Lett. 1985 Oct 21;191(1):39–44. doi: 10.1016/0014-5793(85)80989-3. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. 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]
  13. Fattorini L., Fiorentino D., Amicosante G., Franceschini N., Oratore A., Orefici G. Beta-lactamase production and biological characteristics in nitrosoguanidine induced Mycobacterium fortuitum mutants. Acta Leprol. 1989;7 (Suppl 1):44–47. [PubMed] [Google Scholar]
  14. Galleni M., Lindberg F., Normark S., Cole S., Honore N., Joris B., Frere J. M. Sequence and comparative analysis of three Enterobacter cloacae ampC beta-lactamase genes and their products. Biochem J. 1988 Mar 15;250(3):753–760. doi: 10.1042/bj2500753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Joris B., De Meester F., Galleni M., Frère J. M., Van Beeumen J. The K1 beta-lactamase of Klebsiella pneumoniae. Biochem J. 1987 Apr 15;243(2):561–567. doi: 10.1042/bj2430561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kaneda S., Yabu K. Purification and some properties of beta-lactamase from Mycobacterium smegmatis. Microbiol Immunol. 1983;27(2):191–193. doi: 10.1111/j.1348-0421.1983.tb03583.x. [DOI] [PubMed] [Google Scholar]
  17. Kasik J. E., Peacham L. Properties of beta-lactamases produced by three species of mycobacteria. Biochem J. 1968 May;107(5):675–682. doi: 10.1042/bj1070675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  19. Matagne A., Misselyn-Bauduin A. M., Joris B., Erpicum T., Granier B., Frère J. M. The diversity of the catalytic properties of class A beta-lactamases. Biochem J. 1990 Jan 1;265(1):131–146. doi: 10.1042/bj2650131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Matthew M., Harris A. M. Identification of beta-lactamases by analytical isoelectric focusing: correlation with bacterial taxonomy. J Gen Microbiol. 1976 May;94(1):55–67. doi: 10.1099/00221287-94-1-55. [DOI] [PubMed] [Google Scholar]
  21. Oliva B., Marinucci M. C., Amicosante G., Oratore A., Bennett P. M. Citrobacter diversus ULA27 produces two forms of a chromosomal beta-lactamase. J Antimicrob Chemother. 1987 Jul;20(1):23–35. doi: 10.1093/jac/20.1.23. [DOI] [PubMed] [Google Scholar]
  22. Ricci G., Nardini M., Chiaraluce R., Duprè S., Cavallini D. Interaction of pantetheinase with sulfhydryl reagents and disulfides. Biochim Biophys Acta. 1986 Mar 7;870(1):82–91. doi: 10.1016/0167-4838(86)90011-7. [DOI] [PubMed] [Google Scholar]
  23. Wallace R. J., Jr, Nash D. R., Udou T., Steingrube V. A., Steele L. C., Swenson J. M., Silcox V. A. Isoelectric focusing of beta-lactamases in Mycobacterium fortuitum. Association of a single enzyme pattern with cefoxitin resistance. Am Rev Respir Dis. 1985 Nov;132(5):1093–1097. doi: 10.1164/arrd.1985.132.5.1093. [DOI] [PubMed] [Google Scholar]
  24. Woodruff H. B., Foster J. W. Microbiological Aspects of Penicillin: VII. Bacterial Penicillinase. J Bacteriol. 1945 Jan;49(1):7–17. doi: 10.1128/jb.49.1.7-17.1945. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Yabu K., Kaneda S., Ochiai T. Relationship between beta-lactamase activity and resistance to beta-lactam antibiotics in Mycobacterium smegmatis. Microbiol Immunol. 1985;29(9):803–809. doi: 10.1111/j.1348-0421.1985.tb00883.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES