Classification and substrate head-group specificity of membrane fatty acid desaturases

dc.contributor.authorLi, Dongdi
dc.contributor.authorMoorman, Ruth
dc.contributor.authorVanhercke, Thomas
dc.contributor.authorPetrie, James
dc.contributor.authorSingh, Surinder
dc.contributor.authorJackson, Colin
dc.date.accessioned2018-11-29T22:56:26Z
dc.date.available2018-11-29T22:56:26Z
dc.date.issued2016
dc.date.updated2018-11-29T08:12:21Z
dc.description.abstractMembrane fatty acid desaturases are a diverse superfamily of enzymes that catalyze the introduction of double bonds into fatty acids. They are essential in a range of metabolic processes, such as the production of omega-3 fatty acids. However, our structure–function understanding of this superfamily is still developing and their range of activities and substrate specificities are broad, and often overlapping, which has made their systematic characterization challenging. A central issue with characterizing these proteins has been the lack of a structural model, which has been overcome with the recent publication of the crystal structures of two mammalian fatty acid desaturases. In this work, we have used sequence similarity networks to investigate the similarity among over 5000 related membrane fatty acid desaturase sequences, leading to a detailed classification of the superfamily, families and subfamilies with regard to their function and substrate head-group specificity. This work will facilitate rapid prediction of the function and specificity of new and existing sequences, as well as forming a basis for future efforts to manipulate the substrate specificity of these proteins for biotechnology applications.
dc.format.mimetypeapplication/pdfen_AU
dc.identifier.issn2001-0370
dc.identifier.urihttp://hdl.handle.net/1885/153517
dc.publisherResearch Network of Computational and Structural Biotechnology
dc.sourceComputational and Structural Biotechnology Journal
dc.titleClassification and substrate head-group specificity of membrane fatty acid desaturases
dc.typeJournal article
dcterms.accessRightsOpen Accessen_AU
local.bibliographicCitation.lastpage349
local.bibliographicCitation.startpage341
local.contributor.affiliationLi, Dongdi, College of Science, ANU
local.contributor.affiliationMoorman, Ruth, College of Science, ANU
local.contributor.affiliationVanhercke, Thomas, CSIRO
local.contributor.affiliationPetrie, James, CSIRO
local.contributor.affiliationSingh, Surinder, CSIRO
local.contributor.affiliationJackson, Colin, College of Science, ANU
local.contributor.authoremailu4457141@anu.edu.au
local.contributor.authoruidLi, Dongdi, u4457141
local.contributor.authoruidMoorman, Ruth, u5808670
local.contributor.authoruidJackson, Colin, u4040768
local.description.notesImported from ARIES
local.identifier.absfor039999 - Chemical Sciences not elsewhere classified
local.identifier.ariespublicationa383154xPUB4319
local.identifier.citationvolume14
local.identifier.doi10.1016/j.csbj.2016.08.003
local.identifier.scopusID2-s2.0-84988575865
local.identifier.thomsonID000392630000041
local.identifier.uidSubmittedBya383154
local.type.statusPublished Version

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