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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.
- Source :
-
Antimicrobial agents and chemotherapy [Antimicrob Agents Chemother] 2015 Dec; Vol. 59 (12), pp. 7811-4. Date of Electronic Publication: 2015 Sep 14. - Publication Year :
- 2015
-
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.<br /> (Copyright © 2015, American Society for Microbiology. All Rights Reserved.)
- Subjects :
- Ampicillin pharmacology
Anti-Bacterial Agents pharmacology
Bacterial Typing Techniques
Base Sequence
Biotransformation
Cephalothin pharmacology
Gene Expression
Greece
Humans
Hydrolysis
Imipenem pharmacology
Isoenzymes genetics
Isoenzymes metabolism
Kinetics
Klebsiella Infections drug therapy
Klebsiella Infections microbiology
Klebsiella pneumoniae drug effects
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
Ampicillin metabolism
Anti-Bacterial Agents metabolism
Cephalothin metabolism
Imipenem metabolism
Klebsiella pneumoniae enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1098-6596
- Volume :
- 59
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Antimicrobial agents and chemotherapy
- Publication Type :
- Academic Journal
- Accession number :
- 26369975
- Full Text :
- https://doi.org/10.1128/AAC.01935-15