Abstract
A new natural IND-type metallo-beta-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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents / metabolism
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Anti-Bacterial Agents / pharmacology
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Carbapenems / metabolism
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Carbapenems / pharmacology
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Cephalosporins / metabolism
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Cephalosporins / pharmacology
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Chryseobacterium / drug effects
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Chryseobacterium / enzymology*
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Chryseobacterium / isolation & purification*
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Flavobacteriaceae Infections / microbiology*
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Humans
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Kinetics
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Penicillins / metabolism
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Penicillins / pharmacology
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Sequence Analysis, DNA
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beta-Lactam Resistance
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beta-Lactamases* / chemistry
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beta-Lactamases* / genetics
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beta-Lactamases* / isolation & purification
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beta-Lactamases* / metabolism
Substances
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Anti-Bacterial Agents
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Carbapenems
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Cephalosporins
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Penicillins
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beta-Lactamases