| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1952163 | Biochimie | 2013 | 6 Pages |
•DspA from Strongylocentrotus purpuratus was expressed and characterized.•DspA is the first experimentally confirmed eukaryotic haloalkane dehalogenase.•The enzyme shows a preference for terminally brominated hydrocarbons.•The enantioselectivity towards 2-bromobutane makes DspA attractive for biocatalysis.•Other putative dehalogenases of eukaryotic origin were found by database searches.
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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