Identification of the Catalytic Triad in the Haloalkane Dehalogenase from Sphingomonas paucimobilis UT25

Authors

Hynkova, K., Nagata, Y., Takagi, M., Damborsky, J.

Source

FEBS LETTERS 446: 177-181 (1999)

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. (C) 1999 Federation of European Biochemical Societies.

Full text

Citation

Hynkova, K., Nagata, Y., Takagi, M., Damborsky, J., 1999: Identification of the Catalytic Triad in the Haloalkane Dehalogenase from Sphingomonas paucimobilis UT25. FEBS Letters 446: 177-181.

New Version of CAVER PyMOL Plugin
New Website of SinFonia Project
Congratulations to Katka on her BA’s Degree
Hanka’s Success at a Student Conference
KinTek Workshop First Time in Europe
Open Postdoctoral Position: Protein Structural Biologist
Pavel Vanacek and Antonin Kunka Awarded by Dean