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

DOI: 10.1016/j.febslet.2014.02.056
PMID: 24613925

Authors: Halina R. Novak (University of Exeter) , Christopher Sayer (University of Exeter) , Misha Isupov (University of Exeter) , Dorothee Gotz (Aquapharm Biodiscovery Ltd.) , Andrew Mearns Spragg (Aquapharm Biodiscovery Ltd.) , Jennifer Littlechild (University of Exeter)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Febs Letters , VOL 588 (9) , PAGES 1616 - 1622

State: Published (Approved)
Published: May 2014
Diamond Proposal Number(s): 8889 , 6851

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.

Journal Keywords: Bacterial; Catalytic; Crystallography; X-Ray; Cyclohexanes; Hydrocarbons; Halogenated; Hydrolases; Hydrophobic; Kinetics; Models; Molecular; Propane; Protein; Secondary; Rhodobacteraceae; Substrate Specificity

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography

Other Facilities: None

Added On: 22/10/2014 15:37

Discipline Tags:

Biochemistry Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)