Biochemical characterization of haloalkane dehalogenases DrbA and DmbC, Representatives of a Novel Subfamily
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
19502442
PubMed Central
PMC2725514
DOI
10.1128/aem.00199-09
PII: AEM.00199-09
Knihovny.cz E-zdroje
- MeSH
- Bacteria enzymologie MeSH
- cirkulární dichroismus MeSH
- DNA bakterií chemie genetika MeSH
- hydrolasy chemie genetika izolace a purifikace metabolismus MeSH
- molekulární sekvence - údaje MeSH
- multimerizace proteinu MeSH
- Mycobacterium bovis enzymologie MeSH
- sekvenční analýza DNA MeSH
- substrátová specifita MeSH
- terciární struktura proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- DNA bakterií MeSH
- haloalkane dehalogenase MeSH Prohlížeč
- hydrolasy MeSH
This study focuses on two representatives of experimentally uncharacterized haloalkane dehalogenases from the subfamily HLD-III. We report biochemical characterization of the expression products of haloalkane dehalogenase genes drbA from Rhodopirellula baltica SH1 and dmbC from Mycobacterium bovis 5033/66. The DrbA and DmbC enzymes show highly oligomeric structures and very low activities with typical substrates of haloalkane dehalogenases.
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Biochemical characterization of a novel haloalkane dehalogenase from a cold-adapted bacterium
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