title: Identification of the catalytic triad in the haloalkane dehalogenase from Sphingomonas paucimobilis UT26.
abstract: The haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB) is the enzyme involved in the gamma-hexachlorocyclohexane degradation. This enzyme hydrolyses a broad range of halogenated aliphatic compounds via an alkyl-enzyme intermediate. LinB is believed to belong to the family of alpha/beta-hydrolases which employ a catalytic triad, i.e. nucleophile-histidine-acid, during the catalytic reaction. The position of the catalytic triad within the sequence of LinB was probed by a site-directed mutagenesis. The catalytic triad residues of the haloalkane dehalogenase LinB are proposed to be D108, H272 and E132. The topological location of the catalytic acid (E132) is after the beta-strand six which corresponds to the location of catalytic acid in the pancreatic lipase, but not in the haloalkane dehalogenase of Xanthobacter autotrophicus GJ10 which contains the catalytic acid after the beta-strand seven.
authors: Department of Environmental Chemistry and Ecotoxicology, Masaryk University, Brno, Czech Republic.
authors: K
authors: K
authors: Hynková
authors: Y
authors: Y
authors: Nagata
authors: M
authors: M
authors: Takagi
authors: J
authors: J
authors: Damborský
mesh_terms: D001665:Binding Sites / Q000235:genetics; D002384:Catalysis; D006867:Hydrolases / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D006867:Hydrolases; C046137:haloalkane dehalogenase