Titre :

Characterization of human oxidoreductases involved in aldehyde odorant metabolism.

Auteur(s) :

Boichot, V. [Auteur]
Menetrier, F. [Auteur]
Saliou, Jean-Michel [Auteur]
Plateforme d’Analyse des Glycoconjugués - PLBS [PAGés]
Plateformes Lilloises en Biologie et Santé (PLBS) - UAR 2014 - US 41
Lirussi, F. [Auteur]
Canon, F. [Auteur]
Folia, M. [Auteur]
Heydel, J. M. [Auteur]
Hummel, T. [Auteur]
Menzel, S. [Auteur]
Steinke, M. [Auteur]
Hackenberg, S. [Auteur]
Schwartz, M. [Auteur]
Neiers, F. [Auteur]

Titre de la revue :

Scientific Reports

Nom court de la revue :

Sci Rep

Numéro :

13

Pagination :

4876

Date de publication :

2023-03-25

ISSN :

2045-2322

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

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 ...
Lire la suite >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.Lire moins >

Langue :

Anglais

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

Projet ANR :

Métabolites olfactifs des molécules odorantes : caractérisation et fonction dans la perception olfactive
Pellicule mucosal, flaveur, interaction & perception
Métabolisme de la flaveur en bouche et modulation de la perception par les enzymes du microbiote oral

Collections :

• Plateformes Lilloises en Biologie et Santé (PLBS) - UAR 2014 - US 41

Équipe(s) de recherche :

Plateforme d’Analyse des Glycoconjugués (PAGés)

Date de dépôt :

2023-12-21T06:40:42Z
2024-02-23T10:20:03Z