Abstract
Medium-chain dehydrogenases/reductases of the liver alcohol dehydrogenase type are zinc metalloenzymes (Vallee and Hoch, 1957; IÅeson, 1964; Drum et al., 1969), with two zinc atoms per subunit, one catalytic at the active site and one structural at a site influencing subunit interactions (Sytkowski and Vallee, 1976; Brändén et al., 1975). In horse liver alcohol dehydrogenase and in all other mammalian liver forms, the structural zinc atom is liganded by four closely spaced Cys residues, at positions 97, 100, 103, and III (Brändén et al., 1975; Vallee and Auld, 1990). The mechanism by which this zinc atom maintains its structural role is largely unknown. To probe the metal-binding characteristics of the structural zinc site of alcohol dehydrogenase, we have analyzed zinc-binding to a synthetic replica of the protein segment containing the four Cys residues and covering residues 93–115 of the parent molecule.
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References
Bergman, T., Jornvall, H., Holmquist, B., and Vallée, B. L., 1992, A synthetic peptide encompassing the binding site of the second zinc atom (the“structural”zinc) of alcohol dehydrogenase, Eur. J. Biochem., 205: 467–470.
Bergman, T., Jörnvall, H., Härd, T., Holmquist, B., and Vallée, B. L., 1993, A synthetic approach to analysis of the structural zinc site of alcohol dehydrogenase, in: Enzymology and Molecular Biology of Carbonyl Metabolism 4, Weiner, H., Crabb, D. W., and Flynn, T. G., eds., Plenum Press, New York, pp. 419–428.
Brändén, C.-L, Jörnvall, H., Eklund, H., and Furugren, B., 1975, Alcohol dehydrogenases, in: The Enzymes 11, Boyer, P. D., ed., Academic Press, New York, pp. 103–190.
Drum, D. E., Li, T.-K., and Vallée, B. L., 1969, Zinc isotope exchange in horse liver alcohol dehydrogenase, Biochemistry, 8: 3792–3797
Gheorghe, M. T., Lindh, I., Griffiths, W. J., Sjövall, J., and Bergman, T., 1995, Analytical approaches to alcohol dehydrogenase structures, in: Enzymology and Molecular Biology of Carbonyl Metabolism 5, Weiner, H, Holmes, R. S., and Wermuth, B., eds., Plenum Press, New York, pp. 417–426.
Holmquist, B., 1988, Elimination of adventitious metals, Methods Enzymol, 158: 6–12.
Hunt, J. B., Neece, S. H., and Ginsburg, A., 1985, The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase, Anal. Biochem., 146: 150–157.
Iwamoto, T., 1961, Acid-base property and metal chelate formation of 4-(2-pyridylazo)-resorcinol, Bull. Chem. Soc. Japan, 34: 605–610.
Pollâk, M., and Kuban, V, 1979, Comparison of spectrophotometric methods of determination of zinc (II) in biological material and study of its complex formation reactions with 4-(2-pyridylazo)resorcinol, Collection Czechoslov. Chem. Commun., 44: 725–741.
Sytkowski, A. J., and Vallée, B. L., 1976, Chemical reactivities of catalytic and noncatalytic zinc or cobalt atoms of horse liver alcohol dehydrogenase: differentiation by their thermodynamic and kinetic properties, Proc. Natl. Acad. Sci. USA, 73: 344–348.
Vallée, B. L., and Auld, D. S., 1990, Zinc coordination, function, and structure of zinc enzymes and other proteins, Biochemistry, 29: 5647–5659.
Vallée, B. L., and Hoch, F. L., 1957, Zinc in horse liver alcohol dehydrogenase, J. Biol. Chem., 225: 185–195.
Åkeson, Å., 1964, On the zinc content of horse liver alcohol dehydrogenase, Biochem. Biophys. Res. Commun., 17: 211–214.
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Bergman, T., Palmberg, C., Jörnvall, H., Auld, D.S., Vallée, B.L. (1999). Zinc Binding Characteristics of the Synthetic Peptide Corresponding to the Structural Zinc Site of Horse Liver Alcohol Dehydrogenase. In: Weiner, H., Maser, E., Crabb, D.W., Lindahl, R. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 7. Advances in Experimental Medicine and Biology, vol 463. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4735-8_41
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DOI: https://doi.org/10.1007/978-1-4615-4735-8_41
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