| Literature DB >> 23939220 |
Andrea Fortova1, Eva Sebestova, Veronika Stepankova, Tana Koudelakova, Lenka Palkova, Jiri Damborsky, Radka Chaloupkova.
Abstract
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.Entities:
Keywords: 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
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Year: 2013 PMID: 23939220 DOI: 10.1016/j.biochi.2013.07.025
Source DB: PubMed Journal: Biochimie ISSN: 0300-9084 Impact factor: 4.079