Aldehyde dehydrogenase 8 family member A1 (ALDH8A1)

Aldehyde dehydrogenase 8 family member A1 (ALDH8A1) is a human enzyme coded by the ALDH8A1 gene. It is classified in the aldehyde dehydrogenase superfamily, responsible for oxidizing aldehydes to their corresponding acids using NAD as a cofactor. ALDH8A1 was initially proposed to mediate the biosynthesis of 9-cis-retinoic acid, but current data indicates its main role is as the aldehyde dehydrogenase of the kynurenine pathway, converting 2-aminomuconic semialdehyde to 2-aminomuconate during tryptophan catabolism. It shows strong specificity and activity for 9-cis-retinal compared to other retinoids, and contributes to pathways important for vitamin A metabolism and neuroactive compound biosynthesis. Dysfunction of related aldehyde dehydrogenases is implicated in various metabolic and neurological disorders, but ALDH8A1-specific pathologies are less well defined[1][3][4][7][8].

Other names

ALDH8A1ALDH12DJ352A20.2aldehyde dehydrogenase 8 family, member A12-aminomuconic semialdehyde dehydrogenaseretinal dehydrogenase 4 (RALDH4)[1][3][5][6][9]

Not explicitly characterized for drugs; inhibitors would function by blocking oxidoreductase activity of the enzyme[3][7].