DspA from Strongylocentrotus purpuratus: The first biochemically characterized haloalkane dehalogenase of non-microbial origin

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.

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.