9IG2
Crystal structure of human aldehyde dehydrogenase 3 A1 (ALDH3A1) bound to allyl-isothiocyanate
Summary for 9IG2
| Entry DOI | 10.2210/pdb9ig2/pdb |
| Descriptor | Aldehyde dehydrogenase, dimeric NADP-preferring, POTASSIUM ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | aldehyde dehydrogenase, nad-dependent oxidoreductase, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 104839.90 |
| Authors | Schwartz, M.,Neiers, F. (deposition date: 2025-02-18, release date: 2026-02-18, Last modification date: 2026-02-25) |
| Primary citation | Boichot, V.,Chaloyard, J.,Gourrat, K.,Moreno, J.,Saliou, J.M.,Heydel, J.M.,Canon, F.,Neiers, F.,Schwartz, M. Dietary isothiocyanates inhibit the oxidative activity of salivary aldehyde dehydrogenase ALDH3A1 and modulate aroma release. Food Chem, 508:148324-148324, 2026 Cited by PubMed Abstract: This study investigates the inhibitory effects of dietary isothiocyanates (ITCs) on the enzymatic activity of salivary aldehyde dehydrogenase ALDH3A1, a key enzyme involved in the metabolism of odorant aldehydes and abundantly expressed in the oronasal sphere. Using a combination of enzymology, X-ray crystallography and mass spectrometry, we demonstrate that ITCs significantly inhibit ALDH3A1 activity both in vitro and ex vivo in saliva. Our findings reveal that allyl-isothiocyanate forms a covalent adduct with the ALDH3A1 catalytic cysteine residue (Cys243) leading to an irreversible inhibition. This inhibition disrupts the metabolic conversion of aldehydes in saliva, thereby impacting aroma release. GC-MS analysis confirmed that ITC-mediated inhibition of salivary ALDH activity modulates the concentration of odorant metabolites in both liquid and gas phases. These results highlight the significant influence of dietary ITCs on salivary enzymatic activity and potential implications for aroma release and flavor modulation in the oral cavity. PubMed: 41672019DOI: 10.1016/j.foodchem.2026.148324 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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