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DspA from Strongylocentrotus purpuratus: The first biochemically characterized haloalkane dehalogenase of non-microbial origin
A. Fortova, E. Sebestova, V. Stepankova, T. Koudelakova, L. Palkova, J. Damborsky, R. Chaloupkova,
Jazyk angličtina Země Francie
Typ dokumentu časopisecké články, práce podpořená grantem
- 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
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
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- $a 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.
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