Abstract
Class 3 ALDHs prefer NAD as coenzyme, but can use NADP effectively in vitro. They function as dimers of identical ~50kDa monomers, and share about 30% sequence identity with either of the tetrameric class 1 or 2 enzymes. Interest in the Class 3 ALDH (ALDH-3) has focused on its diversity of expression (Lindahl, 1992). No ALDH-3 activity is detectable in normal mammalian liver, but high levels are obtained after exposure to certain xenobiotics. Many neoplasms possess elevated ALDH-3 activities, while many normal tissues, such as cornea and stomach constitutively express ALDH-3. ALDH-3 enzymes prefer aromatic aldehydes and medium chain-length (C-6 to C-10) aliphatic aldehydes as substrate. Known substrates include benzaldehyde and hexenal as well as 4-hydroxynonenal derived from membrane lipid peroxidation (Lindahl and Peterson, 1991). The microsomal ALDH-3 has also received clinical attention from the recent demonstration that Sjögren-Larsson Syndrome is the result of mutations inactivating this “fatty aldehyde dehydrogenase” (DeLaurenzi, et al, 1996).
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Liu, ZJ. et al. (1996). Crystal Structure of a Class 3 Aldehyde Dehydrogenase at 2.6Å Resolution. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_1
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