Biochemical Characterization of VIM-39, a VIM-1-Like Metallo-β-Lactamase Variant from a Multidrug-Resistant Klebsiella pneumoniae Isolate from Greece
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
26369975
PubMed Central
PMC4649142
DOI
10.1128/aac.01935-15
PII: AAC.01935-15
Knihovny.cz E-zdroje
- MeSH
- ampicilin metabolismus farmakologie MeSH
- antibakteriální látky metabolismus farmakologie MeSH
- beta-laktamasy genetika metabolismus MeSH
- beta-laktamová rezistence genetika MeSH
- biotransformace MeSH
- cefalothin metabolismus farmakologie MeSH
- exprese genu MeSH
- hydrolýza MeSH
- imipenem metabolismus farmakologie MeSH
- infekce bakteriemi rodu Klebsiella farmakoterapie mikrobiologie MeSH
- izoenzymy genetika metabolismus MeSH
- kinetika MeSH
- Klebsiella pneumoniae účinky léků enzymologie genetika izolace a purifikace MeSH
- lidé MeSH
- mikrobiální testy citlivosti MeSH
- molekulární sekvence - údaje MeSH
- sekvence nukleotidů MeSH
- sekvenční analýza DNA MeSH
- techniky typizace bakterií MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Geografické názvy
- Řecko MeSH
- Názvy látek
- ampicilin MeSH
- antibakteriální látky MeSH
- beta-laktamasy MeSH
- cefalothin MeSH
- imipenem MeSH
- izoenzymy MeSH
- VIM-1 metallo-beta-lactamase MeSH Prohlížeč
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.
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GENBANK
KF131539