Aldehyde dehydrogenase family 3 member B2 (ALDH3B2)

Aldehyde dehydrogenase family 3 member B2 (ALDH3B2) is an oxidoreductase enzyme that catalyzes the conversion of medium- and long-chain fatty aldehydes—generated during lipid peroxidation and alcohol metabolism—into non-toxic fatty acids[3][4]. It is a member of the large ALDH gene superfamily, with structural conservation in its catalytic domains. ALDH3B2 is mostly cytoplasmic and has bioinformatically predicted phosphorylation sites. Although originally thought to be a possible pseudogene due to a frequent premature stop codon, evidence demonstrates expression of the full-length protein, likely via a stop codon readthrough mechanism[1]. ALDH3B2 plays a role in cellular detoxification and cell cycle regulation, and recent studies implicate it in cancer progression—especially in cholangiocarcinoma—where its overexpression is linked to higher cell proliferation, metastasis, and poor clinical outcomes[2]. Altered methylation of the ALDH3B2 locus is observed in infertile men, suggesting additional roles in reproduction and epigenetics[4][1].

Other names

ALDH8Long-chain fatty aldehyde dehydrogenaseAcetaldehyde dehydrogenase 8Aldehyde dehydrogenase 8

Oxidation and detoxification of cytotoxic aldehydes to non-toxic fatty acids; drugs targeting this enzyme would likely act as inhibitors or modulators of its activity[4][3].