Biochemical characterization of a novel haloalkane dehalogenase from a cold-adapted bacterium
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
22582053
PubMed Central
PMC3416366
DOI
10.1128/aem.00485-12
PII: AEM.00485-12
Knihovny.cz E-zdroje
- MeSH
- bakteriální proteiny chemie genetika metabolismus MeSH
- fyziologická adaptace * MeSH
- hydrolasy chemie genetika metabolismus MeSH
- kinetika MeSH
- koncentrace vodíkových iontů MeSH
- nízká teplota * MeSH
- Psychrobacter enzymologie genetika růst a vývoj fyziologie MeSH
- substrátová specifita MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bakteriální proteiny MeSH
- haloalkane dehalogenase MeSH Prohlížeč
- hydrolasy MeSH
A haloalkane dehalogenase, DpcA, from Psychrobacter cryohalolentis K5, representing a novel psychrophilic member of the haloalkane dehalogenase family, was identified and biochemically characterized. DpcA exhibited a unique temperature profile with exceptionally high activities at low temperatures. The psychrophilic properties of DpcA make this enzyme promising for various environmental applications.
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