Evaluation of the roles of the conserved residues of aldehyde dehydrogenase.

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Aspect of the mechanism of action of mammalian liver aldehyde dehydrogenase have b studied since the first mammalian liver enzyme was purified in our laboratory. The initial studies suggested that the enzyme functioned with covalent catalysis and that a cysteine might be the nucleophile (Feldman and Weiner, 1972). It was later shown by chemical modifications that cysteine 302 was at the active site and it most likely functioned as the nucleophile (Hempel and Pietruszko, 1981). Later, it was shown that glutamate 268 appeared also to be involved in the catalytic process (Abriola et al., 1990). Once a number of sequences of diverse ALDHs were aligned it was found that all possessed cystei302 and most contained the glutamate residue (Vasiliou et al., 1995). The few that did not possess a glutamate were enzymes that did not produce a free acid as the final productKeywordsAldehyde DehydrogenaseGeneral BaseHydride TransferRibose RingDime PairThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.