dc.contributor.author | Novak, Halina | |
dc.contributor.author | Sayer, Christopher | |
dc.contributor.author | Isupov, MN | |
dc.contributor.author | Gotz, D | |
dc.contributor.author | Spragg, AM | |
dc.contributor.author | Littlechild, JA | |
dc.date.accessioned | 2014-07-29T12:18:23Z | |
dc.date.issued | 2014-05-02 | |
dc.description.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. | en_GB |
dc.description.sponsorship | Wellcome Trust | en_GB |
dc.description.sponsorship | EPSRC | en_GB |
dc.description.sponsorship | HRM | en_GB |
dc.description.sponsorship | University of Exeter | en_GB |
dc.description.sponsorship | BBSRC | en_GB |
dc.identifier.citation | Vol. 588, Issue 9, pp. 1616 - 1622 | en_GB |
dc.identifier.doi | 10.1016/j.febslet.2014.02.056 | |
dc.identifier.grantnumber | BB/L002035/1 | en_GB |
dc.identifier.other | S0014-5793(14)00185-9 | |
dc.identifier.uri | http://hdl.handle.net/10871/15282 | |
dc.language.iso | en | en_GB |
dc.publisher | Elsevier | en_GB |
dc.relation.url | http://www.ncbi.nlm.nih.gov/pubmed/24613925 | en_GB |
dc.relation.url | http://www.sciencedirect.com/science/article/pii/S0014579314001859 | en_GB |
dc.rights.embargoreason | Publisher's policy | en_GB |
dc.subject | Catalytic activity | en_GB |
dc.subject | Haloalkane dehalogenase | en_GB |
dc.subject | Marine Rhodobacteraceae | en_GB |
dc.subject | Three-dimensional structure | en_GB |
dc.subject | Amino Acid Sequence | en_GB |
dc.subject | Bacterial Proteins | en_GB |
dc.subject | Catalytic Domain | en_GB |
dc.subject | Crystallography, X-Ray | en_GB |
dc.subject | Cyclohexanes | en_GB |
dc.subject | Hydrocarbons, Halogenated | en_GB |
dc.subject | Hydrolases | en_GB |
dc.subject | Hydrophobic and Hydrophilic Interactions | en_GB |
dc.subject | Kinetics | en_GB |
dc.subject | Models, Molecular | en_GB |
dc.subject | Molecular Sequence Data | en_GB |
dc.subject | Propane | en_GB |
dc.subject | Protein Binding | en_GB |
dc.subject | Protein Structure, Secondary | en_GB |
dc.subject | Rhodobacteraceae | en_GB |
dc.subject | Substrate Specificity | en_GB |
dc.title | Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae | en_GB |
dc.type | Article | en_GB |
exeter.place-of-publication | Netherlands | |
dc.description | types: Journal Article; Research Support, Non-U.S. Gov't | en_GB |
dc.description | Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. NOTICE: This is the author’s version of a work accepted for publication by Elsevier. Changes resulting from the publishing process, including peer review, editing, corrections, structural formatting and other quality control mechanisms, may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in FEBS Letters Vol. 588, Issue 9, pp. 1616 – 1622 DOI: 10.1016/j.febslet.2014.02.056 | en_GB |
dc.identifier.journal | FEBS Letters | en_GB |