DspA from Strongylocentrotus purpuratus: The first biochemically characterized haloalkane dehalogenase of non-microbial origin.
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.
Loschmidt Laboratories, Department of Experimental Biology and Research Centre for Toxic Compounds in the Environment, Faculty of Science, Masaryk University, Kamenice 5/A13, 625 00 Brno, Czech Republic.
Andrea
A
Fortova
Eva
E
Sebestova
Veronika
V
Stepankova
Tana
T
Koudelakova
Lenka
L
Palkova
Jiri
J
Damborsky
Radka
R
Chaloupkova
D000595:Amino Acid Sequence / Q000235:genetics*; D000818:Animals; D002244:Carbon / Q000737:chemistry; D002384:Catalysis; D002942:Circular Dichroism; D003001:Cloning, Molecular; D015971:Gene Expression Regulation, Enzymologic; D006219:Halogens / Q000737:chemistry; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics*; D047270:Strongylocentrotus purpuratus / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
D006219:Halogens; D002244:Carbon; D006867:Hydrolases; C046137:haloalkane dehalogenase
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