The diversity, structure and regulation of β-lactamases

Cellular and Molecular Life Sciences

Volumn 54, Issue 4, 1998, Pages 341-346

  Philippon, A ^a   Dusart, J ^b   Joris, B ^b   Frere J M ^b  

^a UNIVERSITÉ PARIS DESCARTES   (France)

^b UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

Cephalosporins; Classification; Penicillins; Regulation; lactamases

Indexed keywords

BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; ZINC;

ANTIBIOTIC RESISTANCE; BACTERIUM; BIOSYNTHESIS; CATALYSIS; CONFERENCE PAPER; NONHUMAN; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

BACTERIA (MICROORGANISMS);

EID: 0031923401     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050161     Document Type: Conference Paper

References (22)

1. Bush K., Jacoby G. A. and Medeiros A. (1995) A functional classification scheme of β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39: 1211-1233
2. Jacoby G. A. and Medeiros A. A. (1991) More extended-spectrum β-lactamases. Antimicrob. Agents Chemother 35: 1697-704
3. Medeiros A. A. (1997) Evolution and dissemination of β-lactamases accelerated by generations of β-lactam antibiotics. Clin. Infect. Dis. 24: Suppl. S19-S45
4. Payne D. J. (1993) Metallo-β-lactamases. A new therapeutic challenge. J. Med. Microbiol. 39: 991-996
5. Carfi A., Pares S., Duée E., Galleni M., Duez C., Frère J. M. et al. (1995) The 3-D structure of a Zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 20: 4914-4921
6. Concha N. O., Rasmussen B. A., Bush K. and Herzberg O. (1996) Crystal structure of the wide-spectrum binucleur zinc β-lactamase from Bacteroides fragitis. Structure 4: 823-836
7. Hernandez-Valladares M., Felici A., Weber G., Adolph H. W., Zeppezauer M., Rossolini G. M. et al. (1997) Biochemistry 96: 11534-11541
8. Frère J. M. (1995) β-Lactamases and bacterial resistance to antibiotics. Mol. Microbiol. 16: 385-395
9. Knox J. R., Moews P. C. and Frère J. M. (1996) Molecular evolution of β-lactam resistance. Chemistry and Biology 3: 937-947
10. Oefner C., Darcy A., Daly J. J., Gubernator K., Charnas R. L., Heinze I. et al. (1990) Refined crystal structure of β-lactamase from Citrobacter freundii indicates a mechanism for β-lactam hydrolysis. Nature 343: 284-288
11. Damblon C., Raquet X., Lian L. Y., Lamotte-Brasseur J., Fonzé F., Charlier P. et al. (1996) The catalytic mechanism of β-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzyme. Proc. Natl. Acad. Sci. USA 93: 1747-1752
12. Lamotte-Brasseur J., Knox J., Kelly J. A., Charlier P., Fonzè L., Dideberg O. et al. (1994) The structures and catalytic mechanisms of active-site serine β-lactamases. Biotechnol. Gen. Eng. Rev. 12: 189-230
13. Christensen H., Martin M. T. and Waley S. G. (1990) β-Lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism. Biochem. J. 266: 853-861
14. Monnaie D., Virden R. and Frère J. M. (1992) A rapid-kinetic study of the class C β-lactamase of Enterobacter cloacae 908R. FEBS Lett. 306: 108-112
15. Ledent P. and Frère J. M. (1993) Substrate-induced inactivation of the OXA-2 β-lactamase. Biochem. J., 295: 871-878
16. Hardt K., Joris B., Lepage S., Brasseur R., Lampen J. O., Frère J. M. et al. (1997). The penicillin sensory transducer, BlaR, involved in the inducibility of β-lactamase synthesis in Bacillus licheniformis is embedded in the plasma membrane via a four α-helix bundle. Mol. Microbiol. 23: 935-944
17. Rowland S. J. and Dyke K. G. (1990) Tn552, a novel transposable element from Staphylococcus aureus. Mol. Microbiol. 4: 961-975
18. Tesch W., Ryffel C., Strässle A., Kayser F. H. and Berger-Bächi B. (1990) Evidence of a novel Staphylococcal mec-encoded element (mecR) controlling expression of Penicillin-Binding Protein 2′. Antimicrob. Agents Chemother. 34: 1703-1706
19. Magdalena J., Gérard C., Joris B., Forsman M. and Dusart J. (1997). The two β-lactamase genes of Streptomyces cacaoi, blaL and blaU are under the control of the same regulatory systems. Mol. Gen. Genetics 255: 187-193
20. Goethals K., Van Montagu M. and Holsters M. (1992) Conserved motifs in a divergent nod box of Azorhizobium caulinodans ORS571 reveal a common structure in promoters regulated by Lys-R type proteins. Proc. Natl. Acad. Sci. USA 89: 1646-1650
21. Jacobs C., Frère J. M. and Normark S. (1997) Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in Gram-negative bacteria. Cell 88: 823-832
22. Alksne L. E. and Rasmussen B. A. (1997) Expression of the AsbA1, OXA-12 and AsbM1 β-lactamases in Aeromonas jandaei AER14 is coordinated by a two components regulon. J. Bacteriol. 179: 2006-2013