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Mammalian Liver Alcohol Dehydrogenases

  • Chapter
Biochemical Pharmacology of Ethanol

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 56))

Abstract

In mammals, ethanol metabolism takes place mainly in the liver where it is first converted to acetaldehyde and further to acetic acid (1,2,3). In experimental animals and in humans (4), liver alcohol dehydrogenase (ADH) is responsible for the metabolism of at least 80% of administered ethanol, at concentrations below 0.2% the contribution of any other ethanol metabolizing systems being relatively small (5).

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References

  1. Westerfeld, W.W., The metabolism of alcohol. Texas Rep. BioZ. Med., 13: 559–577, 1955.

    CAS  Google Scholar 

  2. Isselbacher, K.J. and Greenberger, N.J., Metabolic effects of alcohol on the liver. New EngZ. J. Med., 270: 351–410, 1964.

    CAS  Google Scholar 

  3. Lundquist, F., Enzymatic pathways of ethanol metabolism. In: International Encyclopedia of Pharmacology and Therapeutics, Section 20, Ch.l, Pergamon, Oxford, pp. 95–116, 1970.

    Google Scholar 

  4. Hawkins, R.D. and Kalant, H., The metabolism of ethanol and its metabolic effects. Pharmacological Reviews. 24: 67–157, 1972.

    PubMed  CAS  Google Scholar 

  5. Isselbacher, K.J. and Carter, E.A., Ethanol metabolism: oxidative and peroxidative mechanisms. Drug Metab. Disposit. 1: 449–454, 1973.

    CAS  Google Scholar 

  6. Sund, H. and Theorell, H., Alcohol dehydrogenases. In: The Enzymes, P.D. Boyer, H.A. Lardy and K. Myrback, (eds.), Vol. 7, Academic Press, New York, pp. 25–83, 1963.

    Google Scholar 

  7. Raskin, N.H. and Sokoloff, L., Enzymes catalyzing ethanol metabolism in neural and somatic tissues of the rat. J. Neurochem., 19: 273–282, 1972.

    PubMed  CAS  Google Scholar 

  8. Moser, K., Papenberg, J. and von Wartburg, J.P., Heteroganitet and Organvertellung der Alkoholdehydrogenase bei verschiedenen Spezies. Enzymol. BioZ. Clin., 9: 447–558, 1969.

    Google Scholar 

  9. Lester, D., The concentration of apparent endogenous ethanol. Quart. J. Stud. Ale., 23: 17–25, 1962, and Lester, D., Endogenous ethanol: a review. Quart. J. Stud. Ale., 22: 554–574, 1961.

    CAS  Google Scholar 

  10. Krebs, H.A. and Perkins, J.R., The physiological role of liver alcohol dehydrogenase. Biochem. J., 118: 635–644, 1970.

    PubMed  CAS  Google Scholar 

  11. Li, T.K. and Theorell, H., Human liver alcohol dehydrogenase: inhibition by pyrazole and pyrazole analogs. Acta Chem. Scand., 23: 892, 1969.

    PubMed  CAS  Google Scholar 

  12. Pietruszko, R., Crawford, K. and Lester, D., Comparison of substrate specificity of alcohol dehydrogenases from human liver, horse liver and yeast towards saturated and 2-enoic alcohols and aldehydes. Arch. Biochem. Biophys., 159: 50–60, 1973.

    PubMed  CAS  Google Scholar 

  13. Reynier, M., Pyrazole inhibition and kinetic studies of ethanol and retinol oxidation catalyzed by rat liver alcohol dehydrogenase. Acta Chem. Scand., 23: 1119–1129, 1969.

    PubMed  CAS  Google Scholar 

  14. A. Lundquist, F. and Wolthers, H., The kinetics of alcohol elimi-

    Google Scholar 

  15. nation in man. Acta Pharm. Tox. Kbh., 14: 265–289, 1958.

    Google Scholar 

  16. Holzer, H., Schneider, S. and Lange, K., Funktion der Leber Alcoholdehydrase. Angew. Chem., 67: 276–277, 1955.

    CAS  Google Scholar 

  17. Lundquist, F., Tygstrup, N., Winkler, K. and Jensen, K.B., Glycerol metabolism in the human liver: inhibition by ethanol. Science, 150: 616–617, 1965.

    PubMed  CAS  Google Scholar 

  18. Bliss, A.F., The equilibrium between vitamin A alcohol and aldehyde in the presence of alcohol dehydrogenase. Arch. Biochem. Biophys.,31: 197–204, 1951

    Google Scholar 

  19. Zachman, R.D. and Olson, Y.A., A comparison of retinene reductase and alcohol dehydrogenase of rat liver. J. BioZ. Chem., 236: 2309–2313, 1961.

    CAS  Google Scholar 

  20. Christophe, J. and Popjack, G., Studies on the biosynthesis of cholesterol. XIV. The origin of prenoic acids from allyl pyrophosphates in liver enzyme systems. J. Lipid Res., 2: 244–257, 1961.

    Google Scholar 

  21. Koen, A.L. and Shaw, C.R., Retinol and alcohol dehydrogenases in retina and liver. Biochem. Biophys. Acta, 128: 48–54, 1966.

    PubMed  CAS  Google Scholar 

  22. Abiko, Y., Tomikawa, M. and Shimizu, M., Enzymatic conversion of pantothenyl alcohol to pantothenic acid. J. Vitaminology, 15: 59–69, 1969.

    CAS  Google Scholar 

  23. Okuda, K. and Takagawa, N., Rat liver 58-cholestane-3a, 7a, 12a, 26-tetrol dehydrogenase as a liver alcohol dehydrogenase. Biochim. Biophys. Acta, 220: 141–148, 1970.

    PubMed  CAS  Google Scholar 

  24. Waller, G., Theorell, H. and Sjövall, J., Liver alcohol dehydrogenase as a 38-hydroxy-58-cholanic acid dehydrogenase. Arch. Biochem. Biophys., 111: 671–684, 1965.

    PubMed  CAS  Google Scholar 

  25. Björkhem 1., On the role of alcohol dehydrogenase in w-oxidation of fatty acids. Eur. J. Biochem., 30: 441–451, 1972.

    Google Scholar 

  26. Bergström, S., Borgström, B., Tryding, N. and Westöö, G. Intestinal absorption and metabolism of 2:2-dimethylstearic acid in the rat. Biochem. J., 58: 604–608, 1954.

    PubMed  Google Scholar 

  27. Dalziel, K. and Dickinson, F.M., The activity of liver alcohol dehydrogenase with nicotinamide adenine dinucleotide phosphate as coenzyme. Biochem. J., 95: 311–320, 1965.

    PubMed  CAS  Google Scholar 

  28. Bäcklin, K.L., The equilibrium constant of the system ethanol, aldehyde, DPN+, DPNH and H. Acta Chem. Scand., 12: 1279 1285, 1958.

    Google Scholar 

  29. Kendall, L.P. and Ramanathan, A.N., Liver alcohol dehydrogenase and ester formation. Biochem. J., 52: 430–438, 1952.

    Google Scholar 

  30. Abeles, R.H. and Lee, H.A., The dismutation of formaldehyde by liver alcohol dehydrogenase. J. BioZ. Chem., 235: 1499–1503, 1960.

    CAS  Google Scholar 

  31. Dalziel, K. and Dickinson, F.M., Aldehyde mutase. Nature, Lond, 206: 255–257, 1965.

    PubMed  CAS  Google Scholar 

  32. Hinson, J.A. and. Neal, R.A., An examination of the oxidation of aldehydes by horse liver alcohol dehydrogenase. J. BioZ. Chem., 247: 7196–7197, 1972.

    Google Scholar 

  33. Van Eys, J., Aldehyde-ketone isomerisation activity of liver

    Google Scholar 

  34. alcohol dehydrogenase. J. BioZ. Chem., 236: 1531–1533, 1961.

    Google Scholar 

  35. Woodley, C.L. and Gupta, N.K., Coupled oxidoreductase activity of horse liver alcohol dehydrogenase. Arch. Biochem. Biophys., 148: 238–248, 1972.

    PubMed  CAS  Google Scholar 

  36. Vogel, W.H., Snyder, R. and Schulman, M.P., Inhibition of alcohol dehydrogenase by folic acid and several of its analogs. Proc. Soc. Exp. Biol. Med., 115: 545–549, 1964.

    PubMed  CAS  Google Scholar 

  37. Snyder, R., Vogel, W. and Schulman, M.P., Effect of folic acid and analogs on the dehydrogenase and isomerase activities of liver alcohol dehydrogenase. J. Biol. Chem., 240: 471–474, 1965.

    PubMed  CAS  Google Scholar 

  38. Wallenfels, K. and Sund, J., Uber den Mechanismus der Wasserstoffubertragung mit Pyridinnucleotiden. IV. Hemmstoffe fur DPN-abbangige Zinkenzyme. Biochem. Z., 329: 48–58, 1957.

    PubMed  CAS  Google Scholar 

  39. Bonnichsen, R.K. and Wassén, A.M., Crystalline alcohol dehydrogenase from horse liver. Arch. Biochem. Biophys., 18: 36 1363, 1948.

    Google Scholar 

  40. von Wartburg, J.P., Bethune, J.L. and Vallee, B.L., Human liver alcohol dehydrogenase: Kinetic and physicochemical properties. Biochemistry, 3: 1775–1782, 1964.

    CAS  Google Scholar 

  41. Mourad, N. and Woronick, C.L., Crystallization of human liver alcohol dehydrogenase. Arch. Biochem. Biophys., 121: 43 1439, 1967.

    Google Scholar 

  42. Schenker, T.M., Teeple and von Wartburg, J.P., Heterogeneity and polymorphism of human-liver alcohol dehydrogenase. Eur. J. Biochem., 24: 271–279, 1971.

    Google Scholar 

  43. Pietruszko, R., Theorell, H. and DeZalenski, C., Heterogeneity of alcohol dehydrogenase from human liver. Arch. Biochem. Biophys., 153: 279–293, 1972.

    PubMed  CAS  Google Scholar 

  44. Markovic, 0., Theorell, H. and Rao, S., Rat liver alcohol dehydrogenase, purification and properties. Acta Chem. Scand., 25: 195–205, 1971.

    Google Scholar 

  45. Arslanian, M.J., Pascoe, E. and Reinhold, J.G., Rat liver alcohol dehydrogenase purification and properties. Biochem. J., 125: 1039–1047, 1971.

    PubMed  CAS  Google Scholar 

  46. Jörnvall, H., Horse liver alcohol dehydrogenase: the primary structure of the protein chain of the ethanol-active isoenzyme. Eur. J. Biochem., 16: 25.. 40, 1970.

    Google Scholar 

  47. Jörnvall, H. and Pietruszko, R., Structural studies of alcohol dehydrogenase from human liver. Eur. J. Biochem., 29: 167174, 1972.

    Google Scholar 

  48. Jörnvall, H. and Markovic, 0., Structural studies of alcohol dehydrogenase from rat liver. Eur. J. Biochem., 29: 167–174, 1972.

    PubMed  Google Scholar 

  49. Hamburg, R.D., The physical properties of horse liver alcohol dehydrogenase. Ph.D. Dies., Univ. California, Berkeley, 1966.

    Google Scholar 

  50. Ehrenberg, A., Determination of molecular weights and diffusion coefficients in the ultracentrifuge. Acta Chem. Scand., 11: 1257 1270, 1957.

    Google Scholar 

  51. Ehrenberg, A. and Dalziel, K., The molecular weight of horse liver alcohol dehydrogenase. Acta Chem. Scand., 12: 405409, 1958.

    Google Scholar 

  52. Blomquist, C.H., Smith, D.A. and Martinez, A.M., Evidence for the dissociation of horse liver alcohol dehydrogenase into subunits in the presence of detergent. Arch. Biochem. Biophys., 123: 248_250, 1967.

    Google Scholar 

  53. Jörnvall, H. and Harris, J.L., Horse liver alcohol dehydrogenase: On the primary structure of the ethanol active isoenzyme. Eur. J. Biochem., 13: 565–576, 1970.

    PubMed  Google Scholar 

  54. Drum, D.P., Harrison, J.H., Li, T.K., Bethune, J.L. and Vallee, B.L., Structural and functional zinc in horse liver alcohol dehydrogenase. Proc. Nat. Acad. Sci., 57: 1434–1440, 1967.

    PubMed  CAS  Google Scholar 

  55. Pietruszko, R. and Theorell, H., Subunit composition of horse liver alcohol dehydrogenase. Arch. Biochem. Biophys., 131: 288–98, 1969.

    PubMed  CAS  Google Scholar 

  56. Jdrnvall, H., Differences in E and S chains from isoenzymes of horse liver alcohold dehydrogenase. Nature, Lond, 225: 1133 1134, 1970.

    Google Scholar 

  57. Jdrnvall, H., Horse liver alcohol dehydrogenase; on the primary structures of the isoenzymes. Eur. J. Biochem., 16: 41–49, 1970.

    Google Scholar 

  58. Ryzewski, C. and Pietruszko, R., A third subunit of horse liver alcohol dehydrogenase. Fed. Proc., 32: 2093, Abs., 1974.

    Google Scholar 

  59. Smith, M., Hopkinson, D.A. and Harris, H., Developmental changes and polymorphism in human alcohol dehydrogenase. Ann. Hum. Genet., Lond, 34: 251–271, 1971.

    PubMed  CAS  Google Scholar 

  60. Smith, M., Hopkinson, D.A. and Harris, H., Alcohol dehydrogenase isoenzymes in adult human stomach and liver: evidence for activity of the ADH locus. Ann. Hum. Genet., Lond, 35: 243253, 1971.

    Google Scholar 

  61. Jdrnvall, H., Functional aspects of structural studies of alcohol dehydrogenases. In: Alcohol and Aldehyde Metabolizing Systems. Thurman, R.G., Yonetani, T., Williamson, J.R., Chance, B., (eds.), Acad. Press Inc., New York and London, pp. 23–32, 1974.

    Google Scholar 

  62. Jdrnvall, H., Differences in thiol groups and multiple forms of rat liver alcohol dehydrogenase. Biochem. Biophys. Res. Comm., 53: 1096–1101, 1973.

    Google Scholar 

  63. Boyer, P.D., Spectrophotometric study of the reaction of protein sulfhydryl groups with organic mercurials. J. Amer. Chem. Soc., 76: 4331–4337, 1954.

    CAS  Google Scholar 

  64. Yonetani, T. and Theorell, H., On the ternary complex of liver alcohol dehydrogenase with reduced coenzyme and isobutyramide: Effect of p-chloromercuriphenyl sulphonate and stability of the complex. Arch. Biochem b Biophys, 99: 433–446, 1962.

    CAS  Google Scholar 

  65. Theorell, H., Taniguchi, S., Åkeson, X. and Skursky, L., Crystallization of a separate steroid-active liver alcohol dehydrogenase. Biochem. Biophys. Res. Commun., 24: 603–610, 1966.

    CAS  Google Scholar 

  66. Li, T.K. and Vallee, B.L., Active center peptides of liver-alcohol dehydrogenase. 1. The sequence surrounding the active cysteinyl residues. Biochemistry, 3: 869–873, 1964, and Harris, I., Structure and catalytic activity of alcohol dehydrogenase. Nature, London, 203: 230–234, 1964.

    Google Scholar 

  67. Jdrnvall, H., On the determination of the N-terminal groups of horse liver alcohol dehydrogenase. Acta Chem. Scand., 19: 1483–1485, 1965.

    Google Scholar 

  68. Jornvall, H., Acetyl group determinations in horse liver alcohol dehydrogenase and in horse myoglobin. Acta Chem. Scand., 0 21: 1805–1811, 1967.

    CAS  Google Scholar 

  69. Åkeson, Å., On the zinc content of horse liver alcohol dehydrogenase. Biochem. Biophys. Res. Comm., 17: 211–214, 1964.

    Google Scholar 

  70. McKinley-McKee, J.S. and Moss, D.W., Heterogeneity of liver alcohol dehydrogenase on starch-gel electrophoresis. Biochem. J., 96: 583–587, 1965.

    PubMed  CAS  Google Scholar 

  71. Pietruszko, R., Clark, A.F., Graves, J. and Ringold, H.J., Steroid activity and multiplicity of crystalline horse liver alcohol dehydrogenase. Biochem. Biophys. Res. Commun., 23: 526–533, 1966.

    PubMed  CAS  Google Scholar 

  72. von Wartburg, J.P. and Papenberg, J., Alcohol dehydrogenase in ethanol metabolism. Psychosom. Med., 28: 405–413, 1966.

    CAS  Google Scholar 

  73. Coleman, P.L., Iweibo, I. and Weiner, H., Role of zinc in horse liver alcohol dehydrogenase; influence on structure and conformational changes. Biochemistry, 11: 1010–1018, 1972.

    PubMed  CAS  Google Scholar 

  74. Iweibo, I. and Weiner, H., Role of zinc in horse liver alcohol dehydrogenase; coenzyme and substrate binding. Biochemistry, 11: 1003–1010, 1972.

    PubMed  CAS  Google Scholar 

  75. Dunn, M.P. and Hutchison, J.S., Roles of zinc ion and reduced coenzyme in the formation of a transient chemical intermediate during the equine liver alcohol dehydrogenase catalyzed reduction of an aromatic aldehyde. Biochemistry, 12: 4882–4892, 1973.

    PubMed  CAS  Google Scholar 

  76. Takahashi, M. and Harvey, R.A., Estimate of minimal distance between rapidly exchanging zinc and nucleotide binding sites in liver alcohol dehydrogenase. Biochemistry, 12: 47434750, 1973.

    Google Scholar 

  77. Bränden, C.T., Eklund, H., Nordstrom, g. Boiweg T., Soderlund, G., Zeppezauer, E., Ohlsson, I. and Åkeson, Å., Structure of liver alcohol dehydrogenase at 2.9 A resolution (crystallographic structure/zinc/coenzyme binding). Proc. Nat. Acad. Sci., 70: 2439–2450, 1973.

    PubMed  Google Scholar 

  78. Bränden, C.I., Zeppezauer, E., Soderberg, B.O., Boiwe, T., Nordstrom, B., Soderlund, G., Zeppezauer, M., Werner, P.É. and Åkeson, Å., The structure of horse liver alcohol dehydrogenase. III. Molecular structure at 5 A resolution. In:. Structure and Function of Oxidation Reduction Enzymes. Å. Åkeson and A. Ehrenberg (eds.), Pergcmton Press, New York, pp. 93–107, 1972.

    Google Scholar 

  79. Bränden, C.I., Ekiund, H., Zeppezauer, E., Nordstrom, B., Boiwe, T., Soderlund, G. and Ohlsson, I. Three-dimensional structure of the horse liver alcohol dehydrogenase molecule. Alcohol and Aldehyde Metabolizing Systems. Thurman, R.G., Yonetani, T., Williamson, J.R. Chance, B. (eds.), Acad. Press Inc., New York and London, pp. 7–21, 1974.

    Google Scholar 

  80. Theorell, H. and Chance, B. Studies on liver alcohol dehydrogenase and reduced diphosphopyridine nucleotide. Acta Chem. Scand., 5: 1127–1144, 1951.

    CAS  Google Scholar 

  81. Theorell, H. and Winer, A.D., Dissociation constants of the liver alcohol dehydrogenase coenzyme complexes. Arch. Biochem. Biophys., 83: 291–308, 1959.

    PubMed  CAS  Google Scholar 

  82. Witter, A., The binding of DPNH by liver alcohol dehydrogenase. Acta Chem. Scand., 14: 1717–1728, 1960.

    CAS  Google Scholar 

  83. Theorell, H. and Bonnichsen, R.K., Studies on liver alcohol dehydrogenase. 1. Equilibria and initial reaction velocities. Acta Chem. Scand., 5: 1105–1126, 1951.

    CAS  Google Scholar 

  84. Boyer, P.D. and Theorell, H., The change in reduced diphosphopyridine nucleotide (DPNH) fluorescence upon combination with liver alcohol dehydrogenase (ADH). Acta Chem. Scand., 10: 447–450, 1956.

    CAS  Google Scholar 

  85. Winer, A. and Theorell, H., Dissociation constants of ternary complexes of fatty acids and fatty acid amides with horse liver alcohol dehydrogenase-coenzyme complexes. Acta Chem. Scand., 14: 1729–174i, 1960.

    CAS  Google Scholar 

  86. Theorell, H., Åkeson, Å., Liszka-Kope6, B. and deZalenski, C., Equilibrium and rate constants for the reaction between NADH and horse liver alcohol dehydrogenases “EE,” “ES,” and “SS.” Arch. Biochem. Biophys.,139: i41–247,01970.

    Google Scholar 

  87. Taniguchi, S., Theorell, H. and Åkeson, Å., Dissociation constants of the binary complexes of homogeneous horse liver alcohol dehydrogenase and nicotinamide adenine dinucleotide. Acta Chem. Scand., 21: 1903–1920, 1967.

    PubMed  CAS  Google Scholar 

  88. Theorell, H. and Yonetani, T., Liver alcohol dehydrogenase-DPNpyrazole complex: a model of a ternary intermediate in the enzyme reaction. Biochem. Z., 338: 537–553, 1963.

    CAS  Google Scholar 

  89. Theorell, H., A new allosteric effect in the reaction cycle of liver alcohol dehydrogenase. Molecular Associations in Biology, Academic Press Inc, New York, pp. 471–485, 1968.

    Google Scholar 

  90. Yonetani, T. and Theorell, H., Crystallization of binary and ternary complexes of horse liver alcohol dehydrogenase with DPNH and with DPNH and isobutyramide. Arch. Biochem. Biophys., 100: 554–557, 1963.

    PubMed  CAS  Google Scholar 

  91. Rosenberg, A., Theorell, H. and Yonetani, T., Optical rotary dispersion of liver alcohol dehydrogenase and its complexes with coenzymes and inhibitors. Arch. Biochem. Biophys., 110: 113–121, 1965.

    Google Scholar 

  92. Bränden, C.I., Larsson, L.M., Lindquist, I., Theorell, H. and Yonetani, T., X-ray investigations of horse liver alcohol dehydrogenase and its complexes. Arch. Biochem. Biophys., 109: 1965.

    Google Scholar 

  93. Bränden, C.I., Structure of horse liver alcohol dehydrogenase. 1. Structural symmetry and conformational changes. Arch. Biochem. Biophys., 112: 215–217, 1965.

    Google Scholar 

  94. Zeppezauer, E., Söderberg, B.O., Bränden, C.I., Åkeson, Å. and Theorell, H., Crystallization of horse liver alcohol dehydrogenase complexes from alcohol solutions. Acta Chem. Scand. 21: 1099–1101, 1967.

    CAS  Google Scholar 

  95. Bernhard, S.A., Dunn, M.F., Luisi, P.L. and Schack, P., Mechanistic studies on equine liver alcohol dehydrogenase. 1. The stoichiometry relationship of the coenzyme binding sites to the catalytic sites active in the reduction of aromatic aldehydes in the transient state. Biochemistry, 9: 185–192, 1970.

    PubMed  CAS  Google Scholar 

  96. McFarland, J.T. and Bernhard, S.A., Catalytic steps during the single-turnover reduction of aldehydes by alcohol dehydrogenase. Biochemistry,11: 1486–1493

    Google Scholar 

  97. Theorell, H., Yonetani, T. and Sjöberg, B., On the effects of some heterocyclic compounds on the enzymic activity of liver alcohol dehydrogenase. Acta Chem. Scand., 23: 255–260, 1969.

    PubMed  CAS  Google Scholar 

  98. Theorell, H. and McKinley-McKee, J., Liver alcohol dehydrogenase.II. Equilibrium constants of binary and ternary complexes of enzyme coenzyme, isobutyramide and imidazole. Acta Chem. Scand., 15: 1811–1833, 1961.

    CAS  Google Scholar 

  99. Theorell, H. and McKinley-McKee, J., Liver alcohol dehydrogenase.III. Kinetics in the presence of caprate, isobutyramide and imidazole. Acta Chem. Scand., 15: 185–195, 1957.

    Google Scholar 

  100. Vallee, B.L. and Hoch, F.L., Zinc in horse liver alcohol dehydrogenase. J. Biol. Chem., 225: 185–195, 1957.

    PubMed  CAS  Google Scholar 

  101. Yonetani, T., Studies on liver alcohol dehydrogenase complexes. II. The interaction of the enzyme with o-phenanthroline and crystallization of complexes of phenanthroline-enzyme, enzyme-adenosine diphosphate ribose, and phenanthroline-enzyme-adenosine diphosphate ribose. Biochem. Z., 338: 300–316, 1963.

    CAS  Google Scholar 

  102. Theorell, H. and Yonetani, T., Studies on liver alcohol dehydrogenase complexes. IV. Spectrophotometric observation of the enzyme complexes. Arch. Biochem. Biophys., 106: 252–258, 1964.

    PubMed  CAS  Google Scholar 

  103. Theorell, H., Recent results on complexes between liver alcohol dehydrogenase coenzymes and inhibitors of substrates. New perspectives in Biology, M. Sela, (ed.), Elsevier Amsterdam, pp. 147–165, 1964.

    Google Scholar 

  104. Winer, A.D., A note on the substrate specificity of horse liver alcohol dehydrogenase. Acta Chem. Scand., 12: 1695–1696, 1958.

    CAS  Google Scholar 

  105. Dickinson, F.M. and Dalziel, K., The specificities and configurations of ternary complexes of yeast and liver alcohol dehydrogenase. Biochem. J., 104: 165–172, 1967.

    PubMed  CAS  Google Scholar 

  106. Tsai, C.S., Relative reactivities of primary alcohols as substrates of liver alcohol dehydrogenase. Canad. J. Biochem., 46: 381–386, 1968.

    CAS  Google Scholar 

  107. Blair, A.H. and Vallee, B.L., Some catalytic properties of human liver alcohol dehydrogenase. Biochem, 5: 2026–2034, 1966.

    CAS  Google Scholar 

  108. Mani, J.C., Pietruszko, R. and Theorell, H., Methanol activity of alcohol dehydrogenases from human liver, horse liver, and yeast. Arch. Biochem. Biophys., 140: 52–59, 1970.

    PubMed  CAS  Google Scholar 

  109. Waller, G., Dehydrogenation of trans-trans farnesol by horse liver alcohol dehydrogenase. Nature, 207: 1389–1390, 1965.

    PubMed  CAS  Google Scholar 

  110. Merritt, A.D. and Tomkins, J., Reversible oxidation of cyclic secondary alcohols by liver alcohol dehydrogenase. J. BioZ. Chem., 234: 2778–2782, 1959.

    CAS  Google Scholar 

  111. Gillette, J.R., Side chain oxidation of alkyl substituted ring compounds. 1. Enzymatic oxidation of p-nitrotoluene. J. BioZ. Chem., 234: 139–143, 1959.

    CAS  Google Scholar 

  112. Lin, G.W.C. and Lester, D., Dimethylaminoethanol: an improbable in vivo substrate for alcohol dehydrogenase in the rat. Biochem. PharmacoZ., In Press: 1974.

    Google Scholar 

  113. Unger, F., 3-Hydroxysteroid dehydrogenase activity in mammalian liver. Univ. Minnesota, Med. BuZ., 31: 226–242, 1960.

    Google Scholar 

  114. Graves, J.M., Clark, A. and Ringold, H.J., The 3-hydroxysteroid dehydrogenase associated with crystalline horse liver alcohol dehydrogenase (LAD). Sixth Pan American Congress of Endocrinology, Mexico, D.F., E86, Abs., 1965.

    Google Scholar 

  115. Owens, A.H. and Marshall, E.K., A comparison of the metabolism of ethanol and trichloroethanol. Bull. Johns Hopkins, 97: 395–404, 1955.

    CAS  Google Scholar 

  116. Friedman, P.J. and Cooper, J.R., The role of alcohol dehydrogenase in the metabolism of chloral hydrate. J. Pharmacol. Exp. Ther., 129: 373–376, 1960.

    PubMed  CAS  Google Scholar 

  117. Cabana, B.E. and Gessner, P.K., The kinetics of chloral hydrate metabolism in mice and the effect thereon of ethanol. J. PharmacoZ. Exp. Ther., 174: 260–275, 1970.

    CAS  Google Scholar 

  118. Bessman, S.P. and McCabe, E.R.B. III, 1,4-Butanediol; a substrate for rat liver and horse liver alcohol dehydrogenases. Biochem. Pharmacol., 21: 1135–1142, 1972.

    PubMed  CAS  Google Scholar 

  119. Pietruszko, R. and Lester D., Kinetic constants of human and horse liver ADH towards glycols. Fed. Proc., 32: Abs. 1933, 1974.

    Google Scholar 

  120. Theorell, H. and McKinley-McKee, J., Liver alcohol dehydrogenase. 1. Kinetics and equilibria without inhibitors. Acta Chem. Scand., 15: 1797–1810, 1961.

    CAS  Google Scholar 

  121. Wratten, C.C. and Cleland, W.W., Product inhibition studies on yeast and liver alcohol dehydrogenases. Biochemistry, 2: 935–941, 1963.

    PubMed  CAS  Google Scholar 

  122. Wratten, C.C. and Cleland, W.W., Kinetic studies with liver alcohol dehydrogenase. Biochemistry, 4: 2442–2451, 1965.

    CAS  Google Scholar 

  123. Wong, J.T. and Williams, G.R., The mechanism of alcohol dehydrogenase. Arch. Biochem. Biophys., 124: 344–348, 1968.

    PubMed  CAS  Google Scholar 

  124. Theorell, H. and Yonetani, T., The complexes of NADH and NAD with liver alcohol dehydrogenase at pH 10. Acta Biochim. Pol., 21: 355–361, 1964.

    Google Scholar 

  125. Pietruszko, R., Activity of horse liver alcohol dehydrogenase SS with NADP (H) as coenzyme and its sensitivity to barbiturates. Biochem. Biophys. Res. Comm., 54: 1046–1052, 1973.

    PubMed  CAS  Google Scholar 

  126. Shore, J.D. and Gutfreund, H., Transients in the reactions of

    Google Scholar 

  127. liver alcohol dehydrogenase. Biochemistry, 9: 4655–4659, 1970.

    Google Scholar 

  128. Brooks, R.L. and Shore, J.D., Effects of substrate structure on the rate of the catalytic step in the liver alcohol dehydrogenase mechanism. Biochemistry, 10: 3855–3858, 1971.

    PubMed  CAS  Google Scholar 

  129. Shore, J.D. and Gutfreund, H., The analysis of transients in NAD+-linked dehydrogenases. In: Oxidation Reduction Enzymes, A. Åkeson and A. Ehrenberg, (eds.), Pergamon Press, Oxford and New York, 1972.

    Google Scholar 

  130. von Wartburg, J.P., Papenberg, J. and Aebi, H., An atypical human alcohol dehydrogenase. Canad. J. Biochem. Physiol., 43: 889–898, 1965.

    Google Scholar 

  131. von Wartburg, J.P. and Schurch, P.M., Atypical human liver alcohol dehydrogenase. Ann. Acad. Sci., 151: 936–946, 1968.

    Google Scholar 

  132. Dalziel, K., On the purification of liver alcohol dehydrogenase. Acta Chem. Scand., 12: 459–464, 1958.

    CAS  Google Scholar 

  133. Lutstorf, U.M., Schurch, P.M. and von Wartburg, J.P., Heterogeneity of horse liver alcohol dehydrogenase. Eur. J. Biochem., 17: 497–508, 1970.

    PubMed  CAS  Google Scholar 

  134. Pietruszko, R. and Ringold, H.J., Antibody studies with multiple forms of horse liver alcohol dehydrogenase. 1. Biochem. Biophys. Res. Commun., 33: 497–502, 1968.

    PubMed  CAS  Google Scholar 

  135. Pietruszko, R., Ringold, H.J., Kaplan, N.O. and Everse, J., Antibody studies with multiple forms of horse liver alcohol dehydrogenase. 11. Biochem. Biophys. Res. Commun.,33: 503–507, 1968. O

    Google Scholar 

  136. Pi truszko, R., Ringold, H.J., Li, T.K., Vallee, B.L., Åkeson, A. and Theorell, H., Structure and function relationships of isoenzymes of horse liver alcohol dehydrogenase. Nature, 221: 440–443, 1969.

    Google Scholar 

  137. Lutstorf, U.M. and von Wartburg, J.P., Subunit composition of horse liver alcohol dehydrogenase isoenzymes. FEBS Letters, 5: 202–206, 1969.

    PubMed  CAS  Google Scholar 

  138. Schenker, T.M., Teeple, L.J. and von Wartburg, J.P., Heterogeneity and polymorphism of human liver alcohol dehydrogenase. Eur. J. Biochem., 24: 271–279, 1971.

    PubMed  CAS  Google Scholar 

  139. Pikkarainen, P.H. and Räihä, N.C.R., Development of alcohol dehydrogenase activity in the human liver. Pediat. Res., 1: 165–168, 1967.

    PubMed  CAS  Google Scholar 

  140. Pikkarainen, P. and Räihä, N.C.R., Isoenzyme pattern of liver alcohol dehydrogenase during human development. Scand. J. Clin. Lab. Invest., 21, Suppl. 101, 6, 1968.

    Google Scholar 

  141. Pikkarainen, P. and Räihä, N.C.R., Change in alcohol dehydrogenase isoenzyme pattern during development of human liver. Nature, 222: 563–564, 1969.

    PubMed  CAS  Google Scholar 

  142. Murray, R.F., Jr. and Motulsky, A.G., Developmental variation in the isoenzymes of human liver and gastric alcohol dehydrogenase. Science, 171: 71–73, 1971.

    PubMed  CAS  Google Scholar 

  143. Murray, R.F., Jr. and Price, P.H., Ontogenetic, polymorphic and interethnic variation in the isoenzymes of human alcohol dehydrogenase. Ann. N.Y. Acad. Sci., 197: 68–72, 1972.

    PubMed  CAS  Google Scholar 

  144. Mezey, E. and Holt, P.R., Loss of the characteristic features of a typical human liver alcohol dehydrogenase during purification. Life Sci, (Part II ) 8: 245–251, 1969.

    CAS  Google Scholar 

  145. Reynier, M., Theorell, H. and Sjövall, J., Studies on the stereo-specificity of liver alcohol dehydrogenase (LADH) for 3E-hydroxy-5ß-steroids, inhibition effects of pyrazole and 3a-hydroxy-cholanoic acid. Acta Chem. Scand., 23: 1130–1136, 1969.

    PubMed  CAS  Google Scholar 

  146. Räihä, N.C.R., Koskinen, M. and Pikkarainen, P., Developmental changes in alcohol dehydrogenase activity in rat and guinea-pig liver. Biochem. J., 103: 623–626, 1967.

    PubMed  Google Scholar 

  147. Papenberg, J., von Wartburg, J.P. and Aebi, H., Die Heterogenitat der Alkoholdehydrogenase aus Rhesusaffenleber. Biochem. Z., 342: 95–107, 1965.

    CAS  Google Scholar 

  148. Dorfman, R.I. and Ungar, F., Metabolism of steroid hormones. Academic Press, New York, 1965.

    Google Scholar 

  149. Cronholm, T., Makino, I. and Sjövall, J., Steroid metabolism in rats given 12H2 ethanol. Biosynthesis of bile acids and reduction of 3-keto-Sß-cholanoic acid. Eur. J. Biochem., 24: 507–519, 1972.

    PubMed  CAS  Google Scholar 

  150. Norman, A. and Sjövall, J., Formation of lithocholic acid from chenodeoxycholic acid in the rat. Acta Chem. Scand., 14: 1815–1818, 1960.

    CAS  Google Scholar 

  151. Ohno, S., Stenius, C. and Christian L.C., Sex differences in alcohol metabolism; androgenic steroid as an inducer of kidney alcohol dehydrogenase. Clin. Genet., 1: 35–44, 1970.

    CAS  Google Scholar 

  152. Ohno, S., Dofuku, R. and Tettenborn, U., More about x-linked testicular feminization of the mouse as a noninducible (1) mutation of a regulatory locus: 5a-androstan-3a-17ß-diol as the true inducer of kidney alcohol dehydrogenase and ß-glucuronidase. Clin. Genet., 2: 128–138, 1971.

    PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Center of Alcohol Studies, Rutgers University, New Brunswick, New Jersey, USA

    Regina Pietruszko

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  1. Laboratory of Alcohol Research, National Institute on Alcohol Abuse and Alcoholism, Washington, D.C., USA

    Edward Majchrowicz

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Pietruszko, R. (1975). Mammalian Liver Alcohol Dehydrogenases. In: Majchrowicz, E. (eds) Biochemical Pharmacology of Ethanol. Advances in Experimental Medicine and Biology, vol 56. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7529-6_1

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  • DOI: https://doi.org/10.1007/978-1-4684-7529-6_1

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