ALDH
Detoxification of aldehydes generally occurs either via oxidation to the corresponding carboxylic acid or reduction to the alcohol. The aldehyde dehydrogenase (ALDH; EC 1.2.1.36) superfamily catalyzes the NAD(P)+-dependent oxidation of aldehydes to their respective carboxylic acid, only ALDH6A1 generating the CoA thioester product. The human genome encodes for at least 19 distinct ALDH genes. The structure of human ALDHs are similar, functioning as either homodimers or homotetramers, with each monomer comprised of at least three structural domains; a catalytic domain, a cofactor binding domain, and an oligomerization domain. Despite similarities in structure and function, the isoenzymes of the ALDH family of proteins have evolved to recognize different spectrums of aldehyde substrates due to differences in the size and shape of their respective substrate binding sites. These differences have permitted the development of some selective activators and inhibitors for various isoenzymes as therapeutics[1].
[1] C.A. Morgan et al. N,N-diethylaminobenzaldehyde (DEAB) as a substrate and mechanism-based inhibitor for human ALDH isoenzymes. Chem Biol Interact. 2015 Jun 5;234:18-28.
| Axon ID | Name | Description | From price | |
|---|---|---|---|---|
| 2551 | Alda 1 | Small molecule activator of ALDH2 | €65.00 | |
| 3725 | CVT-10216 | Highly selective, reversible inhibitor of ALDH-2 | €110.00 | |
| 2476 | DEAB | Potent inhibitor of cytosolic (class 1) aldehyde dehydrogenase (ALDH) enzymes | €50.00 | |
| 3915 | KOTX1 | Selective, non-cytotoxic and reversible ALDH1A3 inhibitor | €130.00 | |
| 3880 | MCI-INI-3 | Potent and selective ALDH1A3 inhibitor | €130.00 | |