The molecular basis of thioalcohol production in human body odour
| Autor: | Matthew T. G. Holden, Daniel Bawdon, Diana S. Cox, Anthony J. Wilkinson, Reyme Herman, Eleanor J. Dodson, Matthew Rose, Michelle Rudden, A. Gordon James, Gavin H. Thomas |
|---|---|
| Přispěvatelé: | University of St Andrews. School of Medicine, University of St Andrews. Biomedical Sciences Research Complex, University of St Andrews. Infection and Global Health Division, University of St Andrews. Infection Group |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
0301 basic medicine Models Molecular Time Factors Staphylococcus lcsh:Medicine Ligands 01 natural sciences lcsh:Science Peptide sequence Phylogeny chemistry.chemical_classification Human Body Multidisciplinary QR Microbiology Carbon-Sulfur Lyases Biochemistry behavior and behavior mechanisms medicine.symptom Hydrophobic and Hydrophilic Interactions psychological phenomena and processes 010603 evolutionary biology Microbiology Article 03 medical and health sciences Bacterial Proteins Phylogenetics Body odour parasitic diseases medicine Humans Amino Acid Sequence Cysteine Sulfhydryl Compounds Binding site X-ray crystallography Binding Sites fungi lcsh:R DAS Bayes Theorem Lyase QR 030104 developmental biology Enzyme Structural biology chemistry Alcohols Odorants lcsh:Q Function (biology) |
| Zdroj: | Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020) Scientific Reports |
| ISSN: | 2045-2322 |
| Popis: | This work was supported by the BBSRC Grant BB/N006615/1. 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. Publisher PDF |
| Databáze: | OpenAIRE |
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