A new natural IND-type metallo--lactamase variant, IND-5, was identified in a clinical isolate ofChryseobacterium indologenes. IND-5 shared 92.8% and 92.4% amino acid homology with IND-1 and IND-3,respectively. Purified enzyme (pI 8.8, Mr 25,000) was able to hydrolyze penicillins, some narrow- andexpanded-spectrum cephalosporins, and carbapenems but not monobactams.
Identification and Characterization of a New Metallo-_-Lactamase, IND-5, from a Clinical Isolate of Chryseobacterium indologenes
MEZZATESTA, Maria Lina;STEFANI, Stefania;
2007-01-01
Abstract
A new natural IND-type metallo--lactamase variant, IND-5, was identified in a clinical isolate ofChryseobacterium indologenes. IND-5 shared 92.8% and 92.4% amino acid homology with IND-1 and IND-3,respectively. Purified enzyme (pI 8.8, Mr 25,000) was able to hydrolyze penicillins, some narrow- andexpanded-spectrum cephalosporins, and carbapenems but not monobactams.File in questo prodotto:
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