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Gene Review

BCZK3812  -  metallo-beta-lactamase

Bacillus cereus E33L

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Disease relevance of BCZK3812


High impact information on BCZK3812


Chemical compound and disease context of BCZK3812


Biological context of BCZK3812


Associations of BCZK3812 with chemical compounds


Other interactions of BCZK3812


Analytical, diagnostic and therapeutic context of BCZK3812


  1. The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. Carfi, A., Pares, S., Duée, E., Galleni, M., Duez, C., Frère, J.M., Dideberg, O. EMBO J. (1995) [Pubmed]
  2. Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes. Wommer, S., Rival, S., Heinz, U., Galleni, M., Frere, J.M., Franceschini, N., Amicosante, G., Rasmussen, B., Bauer, R., Adolph, H.W. J. Biol. Chem. (2002) [Pubmed]
  3. Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-beta-lactamases. Felici, A., Amicosante, G. Antimicrob. Agents Chemother. (1995) [Pubmed]
  4. Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo-beta-lactamase from Bacteroides fragilis. Fast, W., Wang, Z., Benkovic, S.J. Biochemistry (2001) [Pubmed]
  5. Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases. Felici, A., Perilli, M., Franceschini, N., Rossolini, G.M., Galleni, M., Frere, J.M., Oratore, A., Amicosante, G. Antimicrob. Agents Chemother. (1997) [Pubmed]
  6. Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase. Rasia, R.M., Vila, A.J. J. Biol. Chem. (2004) [Pubmed]
  7. The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding. Damblon, C., Jensen, M., Ababou, A., Barsukov, I., Papamicael, C., Schofield, C.J., Olsen, L., Bauer, R., Roberts, G.C. J. Biol. Chem. (2003) [Pubmed]
  8. Metal ion binding and coordination geometry for wild type and mutants of metallo-beta -lactamase from Bacillus cereus 569/H/9 (BcII): a combined thermodynamic, kinetic, and spectroscopic approach. de Seny, D., Heinz, U., Wommer, S., Kiefer, M., Meyer-Klaucke, W., Galleni, M., Frere, J.M., Bauer, R., Adolph, H.W. J. Biol. Chem. (2001) [Pubmed]
  9. The variation of catalytic efficiency of Bacillus cereus metallo-beta-lactamase with different active site metal ions. Badarau, A., Page, M.I. Biochemistry (2006) [Pubmed]
  10. Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-beta-lactamases. Siemann, S., Clarke, A.J., Viswanatha, T., Dmitrienko, G.I. Biochemistry (2003) [Pubmed]
  11. Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Osano, E., Arakawa, Y., Wacharotayankun, R., Ohta, M., Horii, T., Ito, H., Yoshimura, F., Kato, N. Antimicrob. Agents Chemother. (1994) [Pubmed]
  12. Bulgecin A: a novel inhibitor of binuclear metallo-beta-lactamases. Simm, A.M., Loveridge, E.J., Crosby, J., Avison, M.B., Walsh, T.R., Bennett, P.M. Biochem. J. (2005) [Pubmed]
  13. Cloning and characterization of blaVIM, a new integron-borne metallo-beta-lactamase gene from a Pseudomonas aeruginosa clinical isolate. Lauretti, L., Riccio, M.L., Mazzariol, A., Cornaglia, G., Amicosante, G., Fontana, R., Rossolini, G.M. Antimicrob. Agents Chemother. (1999) [Pubmed]
  14. Characterization of VIM-2, a carbapenem-hydrolyzing metallo-beta-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France. Poirel, L., Naas, T., Nicolas, D., Collet, L., Bellais, S., Cavallo, J.D., Nordmann, P. Antimicrob. Agents Chemother. (2000) [Pubmed]
  15. An evolutionary classification of the metallo-beta-lactamase fold proteins. Aravind, L. In Silico Biol. (Gedrukt) (1999) [Pubmed]
  16. Carbapenem derivatives as potential inhibitors of various beta-lactamases, including class B metallo-beta-lactamases. Nagano, R., Adachi, Y., Imamura, H., Yamada, K., Hashizume, T., Morishima, H. Antimicrob. Agents Chemother. (1999) [Pubmed]
  17. Inhibition of metallo-beta-lactamases by a series of mercaptoacetic acid thiol ester derivatives. Payne, D.J., Bateson, J.H., Gasson, B.C., Proctor, D., Khushi, T., Farmer, T.H., Tolson, D.A., Bell, D., Skett, P.W., Marshall, A.C., Reid, R., Ghosez, L., Combret, Y., Marchand-Brynaert, J. Antimicrob. Agents Chemother. (1997) [Pubmed]
  18. Selection of metalloenzymes by catalytic activity using phage display and catalytic elution. Ponsard, I., Galleni, M., Soumillion, P., Fastrez, J. Chembiochem (2001) [Pubmed]
  19. Hyperexpression in Escherichia coli, purification, and characterization of the metallo-beta-lactamase of Bacillus cereus 5/B/6. Shaw, R.W., Clark, S.D., Hilliard, N.P., Harman, J.G. Protein Expr. Purif. (1991) [Pubmed]
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