Structure-functional characterization of haloalkane dehalogenases

Tatyana Prudnikova1,2, Oksana Degtjarik1, Iuliia Iermak1,  Katsiaryna Tratsiak1,3, Michal Kuty1,2 and  Ivana Kuta Smatanova1,2

1 University of South Bohemia, Faculty of Science, Branišovska 1670, CZ-37005 Česke Budejovice, Czech Republic

2 Academy of Sciences of the Czech Republic, Institute of Nanobiology and Structural Biology GCRC, Zamek 136, 373 33 Nove Hrady, Czech Republic

3 Institute of Organic Chemistry and Biochemistry and Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Flemingovo n.2, Prague 6, Czech Republic


Haloalkane dehalogenases (EC are bacterial enzymes cleaving a carbon-halogen bond by a hydrolytic mechanism in a broad range of halogenated aliphatic compounds (1) . The enzymes can be potentially applied in bioremediation, biosensing, biosynthesis, cellular imaging and protein immobilization (2). Structurally haloalkane dehalogenases belong to the α/β-hydrolase superfamily with two domain organization: an α/β-hydrolase core domain and α-helical cap domain, which lies on the top of the core domain. Active site residues are located in a hydrophobic cavity at the interface between the two domains and are connected to the protein surface by several tunnels. Nowadays more than 20 proteins and their mutant variants from haloalkane dehalogenases family are systematically studied. The main target is focused on research of proteins such as DhaA from Rhodococcus rhodochrous NCIMB 13064, DbeA of Bradyrhizobium elkanii USDA94, LinB of Sphingobium japonicum UT26 or noval haloalkane dehalogenases DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marynobacter sp. ELB 17, etc.

This research is supported by the GACR (P207/12/0775).

1.         Koudelakova T., et al., Biotechnol. J. 8, 32-45 (2011)

2.         Marek J., et al., Biochemistry. 39, 14082–14086 (2000)