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Biochemical Characterization of VIM-39, a VIM-1-Like Metallo-?-Lactamase Variant from a Multidrug-Resistant Klebsiella pneumoniae Isolate from Greece.

ABSTRACT: VIM-39, a VIM-1-like metallo-?-lactamase variant (VIM-1 Thr33Ala His224Leu) was identified in a clinical isolate of Klebsiella pneumoniae belonging to sequence type 147. VIM-39 hydrolyzed ampicillin, cephalothin, and imipenem more efficiently than did VIM-1 and VIM-26 (a VIM-1 variant with the His224Leu substitution) because of higher turnover rates.

SUBMITTER: Papagiannitsis CC

PROVIDER: S-EPMC4649142 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature

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Biochemical Characterization of VIM-39, a VIM-1-Like Metallo-β-Lactamase Variant from a Multidrug-Resistant Klebsiella pneumoniae Isolate from Greece.

Papagiannitsis Costas C CC Pollini Simona S De Luca Filomena F Rossolini Gian Maria GM Docquier Jean-Denis JD Hrabák Jaroslav J

Antimicrobial agents and chemotherapy 20150914 12

VIM-39, a VIM-1-like metallo-β-lactamase variant (VIM-1 Thr33Ala His224Leu) was identified in a clinical isolate of Klebsiella pneumoniae belonging to sequence type 147. VIM-39 hydrolyzed ampicillin, cephalothin, and imipenem more efficiently than did VIM-1 and VIM-26 (a VIM-1 variant with the His224Leu substitution) because of higher turnover rates. ...[more]

PMID: 26369975

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