Biochemical characterization of the THIN-B metallo-β-lactamase of Janthinobacterium lividum

Antimicrobial Agents and Chemotherapy

Volumn 48, Issue 12, 2004, Pages 4778-4783

  Docquier, Jean Denis ^a,d   Lopizzo, Teresa ^a   Liberatori, Sabrina ^a   Prenna, Manuela ^b   Thaller, Maria Cristina ^c   Frère, Jean Marie ^d   Rossolini, Gian Maria ^a  

^a UNIVERSITY OF SIENA   (Italy)

^b UNIVERSITY OF CAMERINO   (Italy)

^c UNIVERSITY OF ROME TOR VERGATA   (Italy)

^d UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CARBAPENEM; CEFALORIDINE; CEPHALOSPORIN; MONOMER;

ARTICLE; BACTERIUM; CATALYSIS; CHELATION; CHEMICAL ANALYSIS; COMPLEX FORMATION; ENZYME PURIFICATION; ESCHERICHIA COLI; ION EXCHANGE CHROMATOGRAPHY; JANTHINOBACTERIUM LIVIDUM; MEASUREMENT; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS;

AMINO ACID SEQUENCE; BETA-LACTAMASES; CEPHALOSPORINS; CHELATING AGENTS; CHROMATOGRAPHY, ION EXCHANGE; CULTURE MEDIA; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; ESCHERICHIA COLI; KINETICS; MOLECULAR SEQUENCE DATA; PROTEOBACTERIA; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SULFHYDRYL COMPOUNDS; TRYPSIN;

EID: 9644273974     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.48.12.4778-4783.2004     Document Type: Article

References (29)

1. Ambler, R. P. 1980. The structure of β-lactamases. Philos. Trans. R. Soc. Lond. B 289:321-331.
2. Aravind, L. 1999. An evolutionary classification of the metallo-β-lactamase fold proteins. In Silico Biol. 1:69-91.
3. Bellais, S., D. Aubert, T. Naas, and P. Nordmann. 2000. Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing β-lactamases in Chryseobacterium meningosepticum. Antimicrob. Agents Chemother. 44:1878-1886.
4. Bicknell, R., E. L. Emanuel, J. Gagnon, and S. G. Waley. 1985. The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia IID 1275. Biochem. J. 229:791-797.
5. Boschi, L., P. S. Mercuri, M. L. Riccio, G. Amicosante, M. Galleni, J. M. Frère, and G. M. Rossolini. 2000. The Legionella (Fluoribacter) gormanii metallo-β-lactamase: a new member of the highly divergent lineage of molecular-subclass B3 β-lactamases. Antimicrob. Agents Chemother. 44:1538-1543.
6. Callebaut, I., D. Moshous, J. P. Mornon, and J. P. de Villartay. 2002. Metallo-β-lactamase fold within nucleic acids processing enzymes: the β-CASP family. Nucleic Acids Res. 30:3592-3601.
7. Creighton, T. E. 1989. Disulfide bonds between cysteine residues, p. 156-168. In T. E. Creighton (ed.), Protein structure, a practical approach. IRL Press, Oxford, United Kingdom.
8. Daiyasu, H., K. Osaka, Y. Ishino, and H. Toh. 2001. Expansion of the zinc metallo-hydrolase family of the β-lactamase fold. FEBS Lett. 503:1-6.
9. Docquier, J. D., F. Pantanella, F. Giuliani, M. C. Thaller, G. Amicosante, M. Galleni, J. M. Frère, K. Bush, and G. M. Rossolini. 2002. CAU-1, a subclass B3 metallo-β-lactamase of low substrate affinity encoded by an ortholog present in the Caulobacter crescentus chromosome. Antimicrob. Agents Chemother. 46:1823-1830.
10. Docquier, J. D., J. Lamotte-Brasseur, M. Galleni, G. Amicosante, J. M. Frère, and G. M. Rossolini. 2003. On functional and structural heterogeneity of VIM-type metallo-β-lactamases. J. Antimicrob. Chemother. 51:257-266.
11. Felici, A., and G. Amicosante. 1995. Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-β-lactamases. Antimicrob. Agents Chemother. 39:192-199.
12. Felici, A., G. Amicosante, A. Oratore, R. Strom, P. Ledent, B. Joris, L. Fanuel, and J. M. Frère. 1993. An overview of the kinetic parameters of class B β-lactamases. Biochem. J. 291:151-155.
13. Franceschini, N., B. Caravelli, J. D. Docquier, M. Galleni, J. M. Frère, G. Amicosante, and G. M. Rossolini. 2000. Purification and biochemical characterization of the VIM-1 metallo-β-lactamase. Antimicrob. Agents Chemother. 44:3003-3007.
14. Galleni, M., J. Lamotte-Brasseur, G. M. Rossolini, J. Spencer, O. Dideberg, and J. M. Frère. 2001. Standard numbering scheme for class B β-lactamases. Antimicrob. Agents Chemother. 45:660-663.
15. Garcia-Saez, I., P. S. Mercuri, C. Papamicael, R. Kahn, J. M. Frère, M. Galleni, G. M. Rossolini, and O. Dideberg. 2003. Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-β-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril. J. Mol. Biol. 325:651-660.
16. Hernandez-Valladeres, M., A. Felici, G. Weber, H. W. Adolph, M. Zeppezauer, G. M. Rossolini, G. Amicosante, J. M. Frère, and M. Galleni. 1997. Zn(II) dependence of the Aeromonas hydrophila AE036 metallo-β- lactamase activity and stability. Biochemistry 36:11534-11541.
17. James, P., M. Quadroni, E. Carafoli, and G. Gonnet. 1994. Protein identification in DNA databases by peptide mass fingerprinting. Protein Sci. 3:1347-1350.
18. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
19. IMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes. Antimicrob. Agents Chemother. 43:890-901.
20. Laraki, N., N. Franceschini, G. M. Rossolini, P. Santucci, C. Meunier, E. de Pauw, G. Amicosante, J. M. Frère, and M. Galleni. 1999. Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-β-lactamase IMP-1 produced by Escherichia coli. Antimicrob. Agents Chemother. 43:902-906.
21. VIM, a new integron-borne metallo-β-lactamase gene from a Pseudomonas aeruginosa clinical isolate. Antimicrob. Agents Chemother. 43:1584-1590.
22. T produced in Escherichia coli. Antimicrob. Agents Chemother. 45:1254-1262.
23. Nordmann, P., and L. Poirel. 2002. Emerging carbapenemases in Gram-negative aerobes. Clin. Microbiol. Infect. 8:321-331.
24. Osano, E., Y. Arakawa, R. Wacharotayankun, M. Ohta, T. Horii, H. Ito, F. Yoshimura, and N. Kato. 1994. Molecular characterization of an enterobacterial metallo β-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Antimicrob. Agents Chemother. 38:71-78.
25. Rossolini, G. M., M. A. Condemi, F. Pantanella, J. D. Docquier, G. Amicosante, and M. C. Thaller. 2001. Metallo-β-lactamase producers in environmental microbiota: new molecular class B enzyme in Janthinobacterium lividum. Antimicrob. Agents Chemother. 45:837-844.
26. Saino, Y., F. Kobayashi, M. Inoue, and S. Mitsuhashi. 1982. Purification and properties of inducible penicillin β-lactamase isolated from Pseudomonas maltophilia. Antimicrob. Agents Chemother. 22:564-570.
27. Sambrook, J., and D. W. Russell. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
28. Ullah, J. H., T. R. Walsh, I. A. Taylor, D. C. Emery, C. S. Verma, S. J. Gamblin, and J. Spencer. 1998. The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution. J. Mol. Biol. 284:125-136.
29. Walsh, T. R., L. Hall, S. J. Assinder, W. W. Nichols, S. J. Cartwright, A. P. MacGowan, and P. M. Bennett. 1994. Sequence analysis of the L1 metallo-β-lactamase from Xanthomonas maltophilia. Biochim. Biophys. Acta 1218:199-201.