Aldehyde Dehydrogenase Gene Superfamily

Abstract

Aldehydehydrogenases (ALDHs) represent a group of NAD(P)⁺-dependent enzymes, which e similar primary structures and oxidize a wide spectrum of endogenous and exnous aldehydes (Lindahl, 1992; Vasiliou et al., 1995). Several ALDHs display broad strate specificities, oxidizing a variety of both aliphatic and aromatic aldehydes, whereather forms possess narrower substrate preferences. Based on substrate specificities, ALDH emes are broadly categorized as:a. semialdehyde dehydrogenases, including hydroxymuconic semialdehyde dehydrogenase (E.C. 1.2.1.32), Escherichia coli (EC 1.2.1.16) and mammalian (EC 1.2.1.24) succinate-semialdehyde dehydrogenase, glutamate semi aldehyde dehydrogenase (E.C. 1.2.1.41), aspartate semialdehyde dehydrogenase (E.C. 1.2.1.11), 2-amino-adipate-6-semialdehyde dehydrogenase (E.C. 1.2.1.31) and metylmalonate- semialdehyde dehydrogenase (E.C. 1.2.1.27), b. nonspecific ALDHs (E.C.I.2.1.3), c. other ALDHs including betaine dehydrogenase (E.C. 1.2.1.8), non phosphorylating glyceraldehyde 3-phosphatedehydrogenase (E.C. 1.2.1.9), phenylacetaldehyde dehydrogenase (EC 1.2.1.39), lactaldehyde dehydrogenase (EC 1.2.1.22), and d. ALDike proteins which represent certain other protein sequences, containing either complete or almost complete ALDH sequences. These include the 10-formyltetrahydrofolate dehydrogenase (E.C. 1.5.1.6), Δ¹-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12), antiquitin, a human 56-kDa androgen-binding protein, and the crystallins..