The metabolism of acetaldehyde and formaldehyde is catalyzed by two distinct enzyme systems. The oxidative metabolism of acetaldehyde to acetate is performed, primarily, by the mitochondrial form of aldehyde dehydrogenase (ALDH2) (Cao, et al., 1988; Svanas & Weiner, 1985). While the oxidative metabolism of formaldehyde to formate can be accomplished through a hydrated glutathione adduct by the glutathione-dependent formaldehyde dehydrogenase located in the cytosol (Uotila & Koivusalo, 1989). The glutathione-dependent formaldehyde dehydrogenase has recently been demonstrated to be identical to the Class 3 form of alcohol dehydrogenase (Koivusalo, et al., 1989).
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References
Ambroziak, W., and Pietrusko, R., 1991, Human aldehyde dehydrogenase: Activity with aldehyde metabolites of monoamines, diamines, and polyamines. J. Biol. Chem., 266: 13011
Burnell, J.C., and Bosron, W.F., 1989, Genetic polymorphism of human liver alcohol dehydrogenase and kinetic properties of the isoenzymes, in “Human metabolism of Alcohol,” Volume II, Crow, K.E. and Batt, R.D., eds., CRC Press, Florida, p. 65.
Cao, Q.-N., Tu, G.-C., and Weiner, H., 1988, Mitochondria as the primary site of acetaldehyde metabolism in beef and pig liver slices. Alcoholism: Clin. Exp. Res., 12: 720.
Crowther, R.A., 1972, The fast rotation function, in “The molecular replacement method.” Rossmann, M.G., ed., Gordon and Breach, New York, p. 174.
Eklund, H., Nordstrom, B., Zeppezauer, E., Soderlund, G., Ohlsson, I., Boiwe, T., Söderberg, B.-O., Tapia, O., Brändén, C.-I., and Åkeson, Å., 1976, Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution. J. Mol. Biol., 102: 27.
Eklund, H., Samama, J.-P., Wallén, L., Brändén, C.-L, Åkeson, Å., and Jones, T.A., 1981, Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution. J. Mol. Biol., 146: 561.
Fitzgerald, P.M.D., 1988, MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement. J. Appl. Cryst., 21: 273.
Hempel, J., and Lindahl, R., 1989, Class III aldehyde dehydrogenase from rat liver: Super family relationship to classes I and II and functional interpretation, in “Enzymology and molecular biology of carbonyl metabolism 2,” Weiner, H. and Flynn, T.G., eds., Alan R. Liss, Inc., New York, p. 3.
Howard, A.J., Gilliland, G.L., Finzel, B.C., Poulos, T.L., Ohlendorf, D.H., and Salemme, F.R., 1987, The use of an imaging proportional counter in macromolecular crystallography. J. Appl. Crystallogr., 20: 383.
Hurley, T.D., Bosron, W.F., Hamilton, J.A., and Amzel, L.M., 1991, Structure of human β1β1 alcohol dehydrogenase: catalytic effects of non-active site substitutions. Proc. Nat. Acad. Sci. USA, 88: 8149.
Lindahl, R., and Hempel, J., 1991, Aldehyde dehydrogenase: What can be learned from a baker’s dozen sequences?, in “Enzymology and molecular biology of carbonyl metabolism 3,” Weiner, H., Wermuth, B., and Crabb, D.W., eds., Plenum Press, New York, p. 1.
Koivusalo, M., Baumann, M., and Uotila, L., 1989, Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III dehydrogenase. FEBS Lett., 257: 105
Matthews, B.M., 1968, Solvent content of protein crystals. J. Mol. Biol., 33: 491.
Rose, J.P., Hempel, J., Kuo, I., Lindahl, R., and Wang, B.-C., 1990, Preliminary crystallographic analysis of class 3 rat liver aldehyde dehydrogenase. Proteins: Structure. Function, and Genetics. 8: 305.
Svanas, G.W., and Weiner, H., 1985, Aldehyde dehydrogenase activity as the rate-limiting factor of acetaldehyde metabolism in rat liver. Arch. Biochem. Biophys., 236: 36.
Tank, A.W., Weiner, H., and Thurman, J.A., 1981, Enzymology and subcellular localization of aldehyde oxidation in rat liver. Biochem. Pharm., 30: 3265.
Utiola, L., and Koivusalo, M., 1989, Glutathione-Dependent Oxidoreductases: Formaldehyde Dehydrogenase, in “Coenzymes and cofactors, Vol. III, glutathione. chemical, biochemical and medical aspects, part A,” Dolphin, D., Poulson, R., and Abramovic, O., eds., John Wiley and Sons, Inc., p. 517.
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Hurley, T.D., Yang, Z., Bosron, W.F., Weiner, H. (1993). Crystallization and Preliminary X-ray Analysis of Bovine Mitochondrial Aldehyde Dehydrogenase and Human Glutathione-Dependent Formaldehyde Dehydrogenase. In: Weiner, H., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 4. Advances in Experimental Medicine and Biology, vol 328. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2904-0_26
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