Identification of the catalytic triad in the haloalkane dehalogenase from Sphingomonas paucimobilis UT26

FEBS Letters

Nagata, Yuji³  Takagi, Masamichi³  Hynková, Kamila¹  Damborský, Jiřı́² 

[1] Department of Environmental Chemistry and Ecotoxicology, Masaryk University, Kotlarska 2, 611 37 Brno, Czech Republic;Laboratory of Biomolecular Structure and Dynamics, Masaryk University, Kotlarska 2, 611 37 Brno, Czech Republic;Laboratory of Cellular Genetics, Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo 113, Japan

关键词: α;    β-Hydrolase;    Active site mutant;    Catalytic triad;    Deamidation;    Haloalkane dehalogenase;    Xanthobacter autotrophicus GJ10;   

DOI  :  10.1016/S0014-5793(99)00199-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB) is the enzyme involved in the γ-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 α/β-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 β-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 β-strand seven.

【 授权许可】

Unknown