Structural highlights
Publication Abstract from PubMed
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.
Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae.,Novak HR, Sayer C, Isupov MN, Gotz D, Spragg AM, Littlechild JA FEBS Lett. 2014 May 2;588(9):1616-22. doi: 10.1016/j.febslet.2014.02.056. Epub, 2014 Mar 5. PMID:24613925[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Novak HR, Sayer C, Isupov MN, Gotz D, Spragg AM, Littlechild JA. 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. PMID:24613925 doi:http://dx.doi.org/10.1016/j.febslet.2014.02.056
