Subunit interactions in mammalian liver aldehyde dehydrogenases.

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Aldehyde dehydrogenases are multisubunit enzymes. The first ones purified were 500 amino acid homotetramers, cytosolic and mitochondrial in origin, and later called class 1 and 2, respectively. These two forms of the enzyme share 70% sequence identity with each other. A third class of enzyme characterized had 452 amino acids and was dimeric. The class 3 enzymes were microsomal, tumor specific or inducible in origin and shared less than 40% homology with the class 1 and 2 enzymes (Hempel et al., 1993). More is known about the enzymology of the class 1 and 2 enzymes, though the 3-dimensional structure of the class 3 enzyme has recently been determined (Liu, et al., 1997). Other classes of ALDHs are known but those enzymes have not been characterized.