Aldehyde dehydrogenase, dimeric NADP-preferring is an enzyme that in humans is encoded by the ALDH3A1 gene.[5][6][7]
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Aldehyde dehydrogenases oxidize various aldehydes to the corresponding acids. They are involved in the detoxification of alcohol-derived acetaldehyde and in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. The enzyme encoded by this gene forms a cytoplasmic homodimer that preferentially oxidizes aromatic aldehyde substrates. The gene is located within the Smith–Magenis syndrome region on chromosome 17.[7]
ALDH3A1 expression is notably high in the cornea of mammalian species, comprising from 5 to 50% of soluble protein content, but is almost absent from the cornea of other vertebrates.[8]