ALDH16A1 is a unique member of the aldehyde dehydrogenase superfamily that functions primarily as a non-catalytic protein involved in protein-protein interactions rather than enzymatic activity 12. Unlike most ALDH family members, human ALDH16A1 lacks the essential catalytic cysteine residue and exhibits no measurable aldehyde oxidation activity, classifying it as a pseudoenzyme 2. The protein contains two ALDH domains, four transmembrane domains, and a unique C-terminal domain with unknown function 12. ALDH16A1 regulates ferroptosis in SMARCA4-deficient lung cancer by binding thioredoxin (TXN), promoting its lysosomal degradation and inhibiting its oxidoreductase function, thereby enhancing cancer cell susceptibility to ferroptosis and improving chemotherapy/immunotherapy efficacy 3. In gliomas, ALDH16A1 contributes to tumor progression by modulating cell proliferation and migration through epithelial-mesenchymal transition 4. Disease relevance includes gout, where ALDH16A1 likely functions through interactions with HPRT1, a key uric acid metabolism enzyme 15, and postpartum depression, where elevated ALDH16A1 expression represents a risk factor 6. ALDH16A1 has also emerged as a potential biomarker in amyotrophic lateral sclerosis tear fluid proteomics 7.