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The molecular basis of thioalcohol production in human body odour
DOI:
10.1038/s41598-020-68860-z
Authors:
Michelle
Rudden
(University of York)
,
Reyme
Herman
(University of York)
,
Matthew
Rose
(University of York)
,
Daniel
Bawdon
(University of York)
,
Diana S.
Cox
(Unilever R&D)
,
Eleanor
Dodson
(University of York)
,
Matthew T. G.
Holden
(University of St Andrews)
,
Anthony J.
Wilkinson
(University of York)
,
A. Gordon
James
(Unilever R&D)
,
Gavin H.
Thomas
(University of York)
Co-authored by industrial partner:
Yes
Type:
Journal Paper
Journal:
Scientific Reports
, VOL 10
State:
Published (Approved)
Published:
July 2020
Diamond Proposal Number(s):
18598
,
13587

Abstract: Body 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.
Diamond Keywords: Body Odour; Enzymes; Bacteria
Subject Areas:
Biology and Bio-materials,
Chemistry
Instruments:
I03-Macromolecular Crystallography
,
I04-Macromolecular Crystallography
Added On:
10/08/2020 13:26
Documents:
s41598-020-68860-z.pdf
Discipline Tags:
Biochemistry
Chemistry
Structural biology
Organic Chemistry
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)