Journal
FEBS LETTERS
Volume 588, Issue 9, Pages 1616-1622Publisher
WILEY
DOI: 10.1016/j.febslet.2014.02.056
Keywords
Haloalkane dehalogenase; Marine Rhodobacteraceae; Three-dimensional structure; Catalytic activity
Funding
- Biotechnology and Biological Science Research Council, UK
- Aquapharm Biodiscovery, Oban
- University of Exeter
- BBSRC [BB/L002035/1]
- Wellcome Trust
- EU
- BBSRC
- EPSRC
Ask authors/readers for more resources
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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available