Characterization of human oxidoreductases involved in aldehyde odorant metabolism

Research output: Contribution to journalResearch articleContributedpeer-review


  • Valentin Boichot - , L'Institut Agro Dijon (Author)
  • Franck Menetrier - , L'Institut Agro Dijon (Author)
  • Jean Michel Saliou - , Université de Lille (Author)
  • Frederic Lirussi - , INSERM - Institut national de la santé et de la recherche médicale, University Of Bourgogne Franche-comté, University Of Franche-comté (Author)
  • Francis Canon - , L'Institut Agro Dijon (Author)
  • Mireille Folia - , Université de Bourgogne (Author)
  • Jean Marie Heydel - , L'Institut Agro Dijon (Author)
  • Thomas Hummel - , Department of Otorhinolaryngology, Head and Neck Surgery, University Hospital Carl Gustav Carus Dresden (Author)
  • Susanne Menzel - , Department of Otorhinolaryngology, Head and Neck Surgery, University Hospital Carl Gustav Carus Dresden (Author)
  • Maria Steinke - , University of Würzburg, Fraunhofer Institute for Silicate Research ISC (Author)
  • Stephan Hackenberg - , RWTH Aachen University (Author)
  • Mathieu Schwartz - , L'Institut Agro Dijon (Author)
  • Fabrice Neiers - , L'Institut Agro Dijon (Author)


Oxidoreductases are major enzymes of xenobiotic metabolism. Consequently, they are essential in the chemoprotection of the human body. Many xenobiotic metabolism enzymes have been shown to be involved in chemosensory tissue protection. Among them, some were additionally shown to be involved in chemosensory perception, acting in signal termination as well as in the generation of metabolites that change the activation pattern of chemosensory receptors. Oxidoreductases, especially aldehyde dehydrogenases and aldo–keto reductases, are the first barrier against aldehyde compounds, which include numerous odorants. Using a mass spectrometry approach, we characterized the most highly expressed members of these families in the human nasal mucus sampled in the olfactory vicinity. Their expression was also demonstrated using immunohistochemistry in human epitheliums sampled in the olfactory vicinity. Recombinant enzymes corresponding to three highly expressed human oxidoreductases (ALDH1A1, ALDH3A1, AKR1B10) were used to demonstrate the high enzymatic activity of these enzymes toward aldehyde odorants. The structure‒function relationship set based on the enzymatic parameters characterization of a series of aldehyde odorant compounds was supported by the X-ray structure resolution of human ALDH3A1 in complex with octanal.


Original languageEnglish
Article number4876
JournalScientific reports
Issue number1
Publication statusPublished - 25 Mar 2023

External IDs

PubMed 36966166
ORCID /0000-0001-7650-1731/work/146644564
ORCID /0000-0001-9713-0183/work/146645374


ASJC Scopus subject areas


  • Humans, Oxidoreductases/metabolism, Odorants/analysis, Xenobiotics/metabolism, Smell/physiology, Respiratory System/metabolism, Alcohol Oxidoreductases/metabolism, Receptors, Odorant/genetics