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dc.contributor.authorRudden, Michelle
dc.contributor.authorHerman, Reyme
dc.contributor.authorRose, Matthew
dc.contributor.authorBawdon, Daniel
dc.contributor.authorCox, Diana S.
dc.contributor.authorDodson, Eleanor
dc.contributor.authorHolden, Matthew T. G.
dc.contributor.authorWilkinson, Anthony J.
dc.contributor.authorJames, A. Gordon
dc.contributor.authorThomas, Gavin H.
dc.identifier.citationRudden , M , Herman , R , Rose , M , Bawdon , D , Cox , D S , Dodson , E , Holden , M T G , Wilkinson , A J , James , A G & Thomas , G H 2020 , ' The molecular basis of thioalcohol production in human body odour ' , Scientific Reports , vol. 10 , 12500 .
dc.identifier.otherPURE: 269483989
dc.identifier.otherPURE UUID: 742663e7-f940-4b76-b383-ad34a34eb775
dc.identifier.otherRIS: urn:0706BC64E6B3916A725B5F68818F81F9
dc.identifier.otherRIS: Rudden2020
dc.identifier.otherScopus: 85088560710
dc.identifier.otherORCID: /0000-0002-4958-2166/work/78528144
dc.identifier.otherWOS: 000556872700033
dc.descriptionThis work was supported by the BBSRC Grant BB/N006615/1.en
dc.description.abstractBody odour is a characteristic trait of Homo sapiens, however its role in human behaviour and evolution is poorly understood. Remarkably, body odour is linked to the presence of a few species of commensal microbes. Herein we discover a bacterial enzyme, limited to odour-forming staphylococci that are able to cleave odourless precursors of thioalcohols, the most pungent components of body odour. We demonstrated using phylogenetics, biochemistry and structural biology that this cysteine-thiol lyase (C-T lyase) is a PLP-dependent enzyme that moved horizontally into a unique monophyletic group of odour-forming staphylococci about 60 million years ago, and has subsequently tailored its enzymatic function to human-derived thioalcohol precursors. Significantly, transfer of this enzyme alone to non-odour producing staphylococci confers odour production, demonstrating that this C-T lyase is both necessary and sufficient for thioalcohol formation. The structure of the C-T lyase compared to that of other related enzymes reveals how the adaptation to thioalcohol precursors has evolved through changes in the binding site to create a constrained hydrophobic pocket that is selective for branched aliphatic thioalcohol ligands. The ancestral acquisition of this enzyme, and the subsequent evolution of the specificity for thioalcohol precursors implies that body odour production in humans is an ancient process.
dc.relation.ispartofScientific Reportsen
dc.rightsCopyright © The Author(s) 2020. Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit
dc.subjectQR Microbiologyen
dc.titleThe molecular basis of thioalcohol production in human body odouren
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Medicineen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews.Infection and Global Health Divisionen
dc.contributor.institutionUniversity of St Andrews.Infection Groupen
dc.description.statusPeer revieweden

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