DspA from Strongylocentrotus purpuratus: The first biochemically characterized haloalkane dehalogenase of non-microbial origin
Jazyk angličtina Země Francie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
23939220
DOI
10.1016/j.biochi.2013.07.025
PII: S0300-9084(13)00248-4
Knihovny.cz E-zdroje
- Klíčová slova
- CD, Catalytic activity, Enantioselectivity, Eukaryotic haloalkane dehalogenase, Gene mining, IPTG, PCA, Principle Component Analysis, Substrate specificity, T(m), circular dichroism, isopropyl β-D-thiogalactopyranoside, melting temperature,
- MeSH
- cirkulární dichroismus MeSH
- halogeny chemie MeSH
- hydrolasy chemie genetika MeSH
- katalýza MeSH
- klonování DNA MeSH
- regulace genové exprese enzymů MeSH
- sekvence aminokyselin genetika MeSH
- Strongylocentrotus purpuratus enzymologie genetika MeSH
- substrátová specifita MeSH
- uhlík chemie MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- haloalkane dehalogenase MeSH Prohlížeč
- halogeny MeSH
- hydrolasy MeSH
- uhlík MeSH
Haloalkane dehalogenases are known as bacterial enzymes cleaving a carbon-halogen bond in halogenated compounds. Here we report the first biochemically characterized non-microbial haloalkane dehalogenase DspA from Strongylocentrotus purpuratus. The enzyme shows a preference for terminally brominated hydrocarbons and enantioselectivity towards β-brominated alkanes. Moreover, we identified other putative haloalkane dehalogenases of eukaryotic origin, representing targets for future experiments to discover dehalogenases with novel catalytic properties.
Citace poskytuje Crossref.org
Discovery of Novel Haloalkane Dehalogenase Inhibitors
