A new natural IND-type metallo-β-lactamase variant, IND-5, was identified in a clinical isolate of Chryseobacterium indologenes. IND-5 shared 92.8% and 92.4% amino acid homology with IND-1 and IND-3, respectively. Purified enzyme (pI = 8.8, M r = 25,000) was able to hydrolyze penicillins, some narrow- and expanded-spectrum cephalosporins, and carbapenems but not monobactams.
Perilli, M., Caporale, B., Celenza, G., Pellegrini, C., Docquier, J.D., Mezzatesta, M., et al. (2007). Identification and characterization of a new metallo-β-lactamase, IND-5, from a clinical isolate of Chryseobacterium indologenes. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 51(8), 2988-2990 [10.1128/AAC.00083-07].
Identification and characterization of a new metallo-β-lactamase, IND-5, from a clinical isolate of Chryseobacterium indologenes
DOCQUIER J. D.;ROSSOLINI G. M.;
2007-01-01
Abstract
A new natural IND-type metallo-β-lactamase variant, IND-5, was identified in a clinical isolate of Chryseobacterium indologenes. IND-5 shared 92.8% and 92.4% amino acid homology with IND-1 and IND-3, respectively. Purified enzyme (pI = 8.8, M r = 25,000) was able to hydrolyze penicillins, some narrow- and expanded-spectrum cephalosporins, and carbapenems but not monobactams.
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https://hdl.handle.net/11365/8734
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