caa a22 4500 605504709 CHVBK 20210128100617.0 cr unu---uuuuu 210128e20151201xx s 000 0 eng 10.1007/s00253-015-6954-x doi (NATIONALLICENCE)springer-10.1007/s00253-015-6954-x Properties and biotechnological applications of natural and engineered haloalkane dehalogenases [Elektronische Daten] [Yuji Nagata, Yoshiyuki Ohtsubo, Masataka Tsuda] Haloalkane dehalogenases (HLDs) convert halogenated compounds to corresponding alcohols, halides, and protons. They belong to α/β-hydrolases, and their principal catalytic mechanism is SN2 nucleophilic substitution followed by the addition of water. Since HLDs generally have broad and different substrate specificities, they have various biotechnological applications. HLDs have previously been believed to be present only in bacterial strains that utilize xenobiotic halogenated compounds, and three archetypal HLDs, i.e., DhlA, DhaA, and LinB, have been intensively investigated by biochemical, structural, and computational analyses. Furthermore, by using the resulting data and target-selected random mutagenesis approaches, these HLDs have been successfully engineered to improve their substrate specificities and activities. In addition, important insights into protein evolution have been obtained by studying these HLDs. At the same time, the genome and metagenome information has revealed that HLD homologues are widely distributed in many bacterial strains, including ones that have not been reported to degrade halogenated compounds. Some of these cryptic HLD homologues have been experimentally confirmed to be "true” HLDs with unique substrate specificities and enantioselectivities. Although their biological functions and physiological roles remain mysterious, these potential HLDs are considered promising materials for the development of new biocatalysts. Springer-Verlag Berlin Heidelberg, 2015 Haloalkane dehalogenase nationallicence Environmental pollutant nationallicence Halogenated compound nationallicence Hydrolase nationallicence Protein engineering nationallicence Bacterial genome nationallicence Protein evolution nationallicence Nagata Yuji Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, 980-8577, Sendai, Japan aut Ohtsubo Yoshiyuki Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, 980-8577, Sendai, Japan aut Tsuda Masataka Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, 980-8577, Sendai, Japan aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/23(2015-12-01), 9865-9881 0175-7598 99:23<9865 2015 99 253 https://doi.org/10.1007/s00253-015-6954-x text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6954-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Nagata Yuji Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, 980-8577, Sendai, Japan aut NATIONALLICENCE 700 1- Ohtsubo Yoshiyuki Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, 980-8577, Sendai, Japan aut NATIONALLICENCE 700 1- Tsuda Masataka Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, 980-8577, Sendai, Japan aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/23(2015-12-01), 9865-9881 0175-7598 99:23<9865 2015 99 253