9IG2 image
Deposition Date 2025-02-18
Release Date 2026-02-18
Last Version Date 2026-02-25
Entry Detail
PDB ID:
9IG2
Keywords:
Title:
Crystal structure of human aldehyde dehydrogenase 3 A1 (ALDH3A1) bound to allyl-isothiocyanate
Biological Source:
Source Organism(s):
Homo sapiens (Taxon ID: 9606)
Expression System(s):
Method Details:
Experimental Method:
Resolution:
2.05 Å
R-Value Free:
0.21
R-Value Work:
0.20
R-Value Observed:
0.20
Space Group:
P 21 21 21
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Aldehyde dehydrogenase, dimer
Gene (Uniprot):ALDH3A1
Chain IDs:A, B
Chain Length:467
Number of Molecules:2
Biological Source:Homo sapiens
Primary Citation
Dietary isothiocyanates inhibit the oxidative activity of salivary aldehyde dehydrogenase ALDH3A1 and modulate aroma release.
Food Chem 508 148324 148324 (2026)
PMID: 41672019 DOI: 10.1016/j.foodchem.2026.148324

Abstact

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.

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Primary Citation of related structures
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