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

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

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.

Keywords: Catalytic activity; Haloalkane dehalogenase; Marine Rhodobacteraceae; Three-dimensional structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Catalytic Domain
  • Crystallography, X-Ray
  • Cyclohexanes / chemistry
  • Hydrocarbons, Halogenated / chemistry
  • Hydrolases / chemistry*
  • Hydrophobic and Hydrophilic Interactions
  • Kinetics
  • Models, Molecular
  • Molecular Sequence Data
  • Propane / analogs & derivatives
  • Propane / chemistry
  • Protein Binding
  • Protein Structure, Secondary
  • Rhodobacteraceae / enzymology*
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Cyclohexanes
  • Hydrocarbons, Halogenated
  • Hydrolases
  • haloalkane dehalogenase
  • Propane
  • 1-bromohexane
  • 1,6-dichlorohexane
  • 1,3-dibromopropane

Associated data

  • GENBANK/KF032932
  • PDB/4BRZ
  • PDB/4C6H