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

Kamila Hynková, Yuji Nagata, Masamichi Takagi, Jiří Damborský

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)

Abstract

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. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)177-181
Number of pages5
JournalFEBS Letters
Volume446
Issue number1
DOIs
Publication statusPublished - 1999 Mar 5

Keywords

  • Active site mutant
  • Catalytic triad
  • Deamidation
  • Haloalkane dehalogenase
  • Xanthobacter autotrophicus GJ10
  • α,β-Hydrolase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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