Abstract
Purified recombinant VIM-7 possesses efficient penicillinase and carbapenemase activities comparable to those of VIM-2. Cephalosporinase activity was variable and generally lower than those of VIM-1 and VIM-2. A homology model suggests that the VIM-7 Tyr-218 Phe substitution may be responsible for the reduced catalytic efficiency against certain cephalosporins, including ceftazidime and cefepime.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acremonium / metabolism
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Bacterial Proteins / metabolism*
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Catalysis
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Catalytic Domain / genetics
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Cefepime
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Ceftazidime / metabolism
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Cephalosporins / metabolism
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Kinetics
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Models, Molecular
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Mutation
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Penicillinase / metabolism*
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Structure-Activity Relationship
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Substrate Specificity
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beta-Lactamases / chemistry
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beta-Lactamases / genetics
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beta-Lactamases / metabolism*
Substances
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Bacterial Proteins
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Cephalosporins
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Recombinant Proteins
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Cefepime
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Ceftazidime
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Penicillinase
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beta-Lactamases
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carbapenemase