title: Biochemical characterization of a novel haloalkane dehalogenase from a cold-adapted bacterium.
abstract: A haloalkane dehalogenase, DpcA, from Psychrobacter cryohalolentis K5, representing a novel psychrophilic member of the haloalkane dehalogenase family, was identified and biochemically characterized. DpcA exhibited a unique temperature profile with exceptionally high activities at low temperatures. The psychrophilic properties of DpcA make this enzyme promising for various environmental applications.
authors.affiliation: Loschmidt Laboratories, Department of Experimental Biology and Research Centre for Toxic Compounds in the Environment, Faculty of Science, Masaryk University, Brno, Czech Republic.
authors.forename: Ivana
authors.initials: I
authors.lastname: Drienovska
authors.forename: Eva
authors.initials: E
authors.lastname: Chovancova
authors.forename: Tana
authors.initials: T
authors.lastname: Koudelakova
authors.forename: Jiri
authors.initials: J
authors.lastname: Damborsky
authors.forename: Radka
authors.initials: R
authors.lastname: Chaloupkova
mesh_terms: D000222:Adaptation, Physiological; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D003080:Cold Temperature; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D044096:Psychrobacter / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000502:physiology; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D006867:Hydrolases; C046137:haloalkane dehalogenase