Aldehyde Dehydrogenases: What can be Learned from a Baker’s Dozen Sequences?
Aldehyde dehydrogenases (E. C. 220.127.116.11, ALDH) exist in multiple molecular forms which differ in their physical and/or their functional properties (Weiner, 1979). Aldehyde dehydrogenase has been identified in virtually every organism and tissue examined. Distinct ALDHs have been identified in the mitochondrial, microsomal and cytosolic compartments of the cell (Tottmar et al., 1973; Greenfield and Pietruszko, 1977; Lindahl and Evces, 1984). Some forms are constitutive, some inducible (Deitrich, 1971; Deitrich et al., 1977). Tetrameric and dimeric functional forms are known. Some forms display broad substrate specificity, oxidizing a variety of aliphatic and aromatic aldehydes. Other forms possess much narrower substrate preferences, utilizing small aliphatic aldehydes. Kinetic studies have indicated that acetaldehyde derived from ethanol oxidation, medium chain length aliphatic aldehydes derived from membrane lipid peroxidation and perhaps some aldehydes generated from neurotransmitter metabolism are potential physiological substrates for one or more ALDH forms (Tank et al., 1981; Esterbauer, 1982; Weiner, 1982; Mitchell and Petersen, 1989). While all aldehyde dehydrogenases likely use NAD+ as coenzyme in vivo, some forms can utilize NADP+ in vitro.
KeywordsAldehyde Dehydrogenase Aliphatic Aldehyde Positional Identity Horse Liver Multiple Molecular Form
Unable to display preview. Download preview PDF.
- Anonymous 1989 Nomenclature of mammalian aldehyde dehydrogenases. In Progress in Clinical and Biological Research, vol. 290, H. Weiner and T. G. Flynn, eds. Alan. R. Liss, New York, pp. xix–xxi.Google Scholar
- Dunn, T. J., Koleske, A. J., Lindahl, R. and Pitot, H. C. 1989 Phenobarbital-inducible aldehyde dehydrogenase in the rat. cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats. J. Biol. Chem. 2 64: 13057–13065.Google Scholar
- Esterbauer, H. 1982 Aldehydic products of lipid peroxidation. In Free Radicals, Lipid Peroxidation and Cancer, D. C. H. McBrien and T. F. Slater, eds., Academic Press, New york, pp 101–128.Google Scholar
- Hempel, J., Harper, K. and Lindahl, R. 1989 Inducible (Class 3) aldehyde dehydrogenase from rat hepatocellular cinoma and 2,3,7,8-tetrachlorodibenzo -p-dioxin-treated liver. Distant relationship to the Class 1 and 2 enzymes from mammalian liver cytosol/mitochondria. Biochemistry 28:1160–1167.PubMedCrossRefGoogle Scholar
- Johansson, J., von Bahr-Lindstrom, H., Jeck, R., Woenckhaus, C. and Jornvall, H. 1988 Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants for both the cytosolic and the mitochondrial forms of an enzyme. Eur. J. Biochem. 172:527–533.PubMedCrossRefGoogle Scholar
- Lindahl, R. and Evces, S. 1984 Comparative subcellular distribution of aldehyde dehydrogenase in rat, mouse and rabbit liver. Biochem. Pharmacol. 33:3383–3389.Google Scholar
- Saigal, D. and Weiner, H., submitted for publication.Google Scholar
- Tank, A. W., Weiner, H. and Thurman, J. A. 1981 Enzymology and subcellular localization of aldehyde oxidation in rat liver. Oxidation of 3,4-dihydroxy-phenylacetaldehyde derived from dopamine to 3,4-dihydroxyphenylacetic acid. Biochem. Pharmacol. 30:3265–3275.Google Scholar
- Weiner, H., 1979 Aldehyde dehydrogenase: mechansism of action and possible physiological role. In Biochemistry and Pharmacology of Ethanol, E. Majchrowicz and E. P. Noble eds., Alan R. Liss, New York, pp 107–124.Google Scholar
- Weiner, H. 1982 Aldehyde dehydrogenase. In Progress in Clinical and Biological Research, vol. 114, H. Weiner and B. Wermuth, eds., Alan R. Liss, New York, pp 1–10.Google Scholar