Aldehyde dehydrogenase family 3 member B2 (ALDH3B2) (ALDH3B2)

Aldehyde dehydrogenase family 3 member B2 (ALDH3B2) is a member of the ALDH superfamily of enzymes responsible for the NAD(P)+-dependent oxidation of aldehydes to their corresponding carboxylic acids (UniProt: P48448). While ALDH1A1 and ALDH2 are the primary enzymes involved in ethanol and retinol metabolism, ALDH3B2 is part of a cluster of isozymes that specialize in the detoxification of medium- and long-chain aldehydes, including those derived from lipid peroxidation (PubMed: 8702751). In the liver, ALDH3B2 contributes to the metabolic defense against oxidative stress and reactive electrophiles. The enzyme has gained attention in oncology, as high expression levels in certain tumors are associated with resistance to cyclophosphamide and other aldehyde-generating chemotherapeutics (PubMed: 24385444). Most current pharmacological interactions involve broad-spectrum inhibitors like disulfiram, which are used to treat alcohol use disorder by inducing a toxic accumulation of acetaldehyde (PubChem: CID 3117). However, the lack of high-resolution structural data for ALDH3B2 specifically makes it a challenging target for selective drug design, often resulting in its classification as an off-target in broader ALDH inhibition studies.

Other names

ALDH8Aldehyde dehydrogenase 8Aldehyde dehydrogenase family 3 member B2

Inhibition of the catalytic activity of aldehyde dehydrogenase, preventing the conversion of aldehydes to carboxylic acids.