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FEBS Lett. 2014 May 2;588(9):1616-22. doi: 10.1016/j.febslet.2014.02.056. Epub 2014 Mar 5.

Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae.

Author information

  • 1The Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK.
  • 2Aquapharm Biodiscovery Ltd., European Centre for Marine Biotechnology, Dunstaffnage, Oban, Argyll PA37 1QA, UK.
  • 3The Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK. Electronic address: J.A.Littlechild@exeter.ac.uk.

Abstract

A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity. A deeper substrate binding pocket defines the enzyme preference towards substrates with longer carbon chains. Arg136 at the bottom of the substrate pocket is positioned to bind the distal halogen group of extended di-halogenated substrates.

Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

KEYWORDS:

Catalytic activity; Haloalkane dehalogenase; Marine Rhodobacteraceae; Three-dimensional structure

PMID:
24613925
[PubMed - indexed for MEDLINE]
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