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dc.contributor.authorNovak, Halina
dc.contributor.authorSayer, Christopher
dc.contributor.authorIsupov, MN
dc.contributor.authorGotz, D
dc.contributor.authorSpragg, AM
dc.contributor.authorLittlechild, JA
dc.date.accessioned2014-07-29T12:18:23Z
dc.date.issued2014-05-02
dc.description.abstractA 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.sponsorshipWellcome Trusten_GB
dc.description.sponsorshipEPSRCen_GB
dc.description.sponsorshipHRMen_GB
dc.description.sponsorshipUniversity of Exeteren_GB
dc.description.sponsorshipBBSRCen_GB
dc.identifier.citationVol. 588, Issue 9, pp. 1616 - 1622en_GB
dc.identifier.doi10.1016/j.febslet.2014.02.056
dc.identifier.grantnumberBB/L002035/1en_GB
dc.identifier.otherS0014-5793(14)00185-9
dc.identifier.urihttp://hdl.handle.net/10871/15282
dc.language.isoenen_GB
dc.publisherElsevieren_GB
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pubmed/24613925en_GB
dc.relation.urlhttp://www.sciencedirect.com/science/article/pii/S0014579314001859en_GB
dc.rights.embargoreasonPublisher's policyen_GB
dc.subjectCatalytic activityen_GB
dc.subjectHaloalkane dehalogenaseen_GB
dc.subjectMarine Rhodobacteraceaeen_GB
dc.subjectThree-dimensional structureen_GB
dc.subjectAmino Acid Sequenceen_GB
dc.subjectBacterial Proteinsen_GB
dc.subjectCatalytic Domainen_GB
dc.subjectCrystallography, X-Rayen_GB
dc.subjectCyclohexanesen_GB
dc.subjectHydrocarbons, Halogenateden_GB
dc.subjectHydrolasesen_GB
dc.subjectHydrophobic and Hydrophilic Interactionsen_GB
dc.subjectKineticsen_GB
dc.subjectModels, Molecularen_GB
dc.subjectMolecular Sequence Dataen_GB
dc.subjectPropaneen_GB
dc.subjectProtein Bindingen_GB
dc.subjectProtein Structure, Secondaryen_GB
dc.subjectRhodobacteraceaeen_GB
dc.subjectSubstrate Specificityen_GB
dc.titleBiochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceaeen_GB
dc.typeArticleen_GB
exeter.place-of-publicationNetherlands
dc.descriptiontypes: Journal Article; Research Support, Non-U.S. Gov'ten_GB
dc.descriptionCopyright © 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.2014.02.056en_GB
dc.identifier.journalFEBS Lettersen_GB


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