Abstract
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.
Copyright © 2015, American Society for Microbiology. All Rights Reserved.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Ampicillin / metabolism*
-
Ampicillin / pharmacology
-
Anti-Bacterial Agents / metabolism*
-
Anti-Bacterial Agents / pharmacology
-
Bacterial Typing Techniques
-
Base Sequence
-
Biotransformation
-
Cephalothin / metabolism*
-
Cephalothin / pharmacology
-
Gene Expression
-
Greece
-
Humans
-
Hydrolysis
-
Imipenem / metabolism*
-
Imipenem / pharmacology
-
Isoenzymes / genetics
-
Isoenzymes / metabolism
-
Kinetics
-
Klebsiella Infections / drug therapy
-
Klebsiella Infections / microbiology
-
Klebsiella pneumoniae / drug effects
-
Klebsiella pneumoniae / enzymology*
-
Klebsiella pneumoniae / genetics
-
Klebsiella pneumoniae / isolation & purification
-
Microbial Sensitivity Tests
-
Molecular Sequence Data
-
Sequence Analysis, DNA
-
beta-Lactam Resistance / genetics
-
beta-Lactamases / genetics
-
beta-Lactamases / metabolism
Substances
-
Anti-Bacterial Agents
-
Isoenzymes
-
Imipenem
-
Ampicillin
-
VIM-1 metallo-beta-lactamase
-
beta-Lactamases
-
Cephalothin