The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae

FEMS Yeast Research

Volumn 2, Issue 4, 2002, Pages 481-494

  Leskovac, Vladimir ^a   Trivić, Svetlana ^a   Peričin, Draginja ^a  

^a UNIVERSITY OF NOVI SAD   (Serbia)

Author keywords

Alcohol dehydrogenase; Saccharomyces cerevisiae; Yeast alcohol dehydrogenase

Indexed keywords

ALCOHOL DEHYDROGENASE; FUNGAL ENZYME; ISOENZYME; UNCLASSIFIED DRUG; YEAST ALCOHOL DEHYDROGENASE 1; YEAST ALCOHOL DEHYDROGENASE 2; YEAST ALCOHOL DEHYDROGENASE 3; ZINC;

CATALYSIS; COENZYME; ENANTIOSELECTIVITY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; MUTATION; NONHUMAN; ORGANIC CHEMISTRY; PROTEIN FUNCTION; SACCHAROMYCES CEREVISIAE; SHORT SURVEY; YEAST; BINDING SITE; CHEMISTRY; CLASSIFICATION; ENZYMOLOGY; KINETICS; METABOLISM; REVIEW; STRUCTURE ACTIVITY RELATION;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

ALCOHOL DEHYDROGENASE; BINDING SITES; ISOENZYMES; KINETICS; SACCHAROMYCES CEREVISIAE; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; ZINC;

EID: 0036891388     PISSN: 15671356     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1567-1356(02)00157-5     Document Type: Review

References (79)

1. Sun H.-W., Plapp B.V. Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family. J. Mol. Evol. 34:1992;522-535.
2. Young, E.T., Williamson, V., Taguchi, A., Smith, M., Sledziewski, A., Russel, D., Ostermann, J., Denis, C., Cox, D. and Beier, D. (1982) The alcohol dehydrogenase genes from the yeast, Saccharomyces cerevisiae: isolation, structure and regulation. In: Genetic Engineering of Microorganisms for Chemicals (Hollaender, A., DeMoss, R.D., Kaplan, S., Konisky, J., Savage, D. and Wolfe, R.S., Eds.), pp. 335-361. Plenum, New York.
3. Wills C. Amino acid substitutions in two functional mutants of yeast alcohol dehydrogenase. Nature. 279:1979;734-736.
4. Young E.T., Pillgrim D. Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae. Mol. Cell Biol. 5:1985;3024-3034.
5. Brändén, C.-I., Jörnvall, H., Eklund, H. and Furugren, B. (1975) Alcohol dehydrogenases. In: The Enzymes, Vol. 11, 3rd edn. (Boyer, P.D., Ed.), pp. 104-190. Academic Press, New York.
6. Klinman J.P. Probes of mechanism and transition-state structure in the alcohol dehydrogenase reaction. CRC Crit. Rev. Biochem. 10:1981;39-78.
7. Cleland W.W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. Biochim. Biophys. Acta. 67:1963;103-137.
8. Negelein E., Wulff H.-J. Diphosphopyridinproteid Alcohol, Acetaldehyd. Biochem. Z. 293:1937;351-389.
9. Ganzhorn A.J., Green D.W., Hershey A.D., Gould R.M., Plapp B.V. Kinetic characterization of yeast alcohol dehydrogenase. Amino acid residue 294 and substrate specificity. J. Biol. Chem. 262:1987;3754-3761.
10. Dickinson F.M., Dack S. The activity of yeast ADH I and ADH II with long chain alcohols and diols. Chem. Biol. Interact. 130-132:2001;417-423.
11. Dickinson F.M., Monger G.P. A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates. Biochem. J. 131:1973;261-270.
12. Schöpp W., Aurich H. Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long chain primary alcohols. Biochem. J. 157:1976;15-22.
13. Trivić S., Leskovac V. Kinetic mechanism of yeast alcohol dehydrogenase activity with secondary alcohols and ketones. Indian J. Biochem. Biophys. 31:1994;387-391.
14. Trivić S., Leskovac V. Novel substrate of yeast alcohol dehydrogenase - 4. Allyl alcohol and ethylene glycol. Biochem. Mol. Biol. Int. 47:1999;1-8.
15. Chen D.-H., Huang T.-C. Oxidation of Tris (hydroxymethyl) aminomethane by yeast alcohol dehydrogenase. J. Chem. Eng. Jpn. 27:1994;547-550.
16. Leskovac V., Trivić S., Zeremski J., Stančić B., Anderson B.M. Novel substrates of yeast alcohol dehydrogenase - 3. 4-Dimethylamino-cinnamaldehyde and chloroacetaldehyde. Biochem. Mol. Biol. Int. 43:(007):1997;365-373.
17. Trivić S., Leskovac V., Peričin D., Winston G.W. A novel substrate for yeast alcohol dehydrogenase - p-nitroso-N,N-dimethylaniline. Biotechnol. Lett. 24:2002;807-812.
18. Mani J.-C., Pietruszko R., Theorell H. Methanol activity of alcohol dehydrogenase from human liver, horse liver, and yeast. Arch. Biochem. Biophys. 140:1970;52-59.
19. Weinhold E.G., Benner S.A. Engineering yeast alcohol dehydrogenase. Replacing Trp 54 by Leu broadens substrate specificity. Protein Eng. 8:1995;457-461.
20. Green D.W., Sun H.-W., Plapp B.V. Inversion of the substrate specificity of yeast alcohol dehydrogenase. J. Biol. Chem. 268:1993;7792-7798.
21. Bergmeyer, H.U. (1970) Alkohol dehydrogenase (aus Hefe). In: Methoden der enzymatischen Analyse, Vol.1, 2nd Edn., pp. 392-393, 1457-1474. Verlag-Chemie, Weinheim.
22. Scharschmidt M., Fisher M.A., Cleland W.W. Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 1. Liver alcohol dehydrogenase with benzyl alcohol and yeast alcohol dehydrogenase with benzaldehyde. Biochemistry. 23:1984;5471-5478.
23. Rucker J., Cha Y., Jonsson T., Grant K.L., Klinman J.P. Role of internal thermodynamics in determining hydrogen tunneling in enzyme-catalyzed hydrogen transfer reactions. Biochemistry. 31:1992;11489-11499.
24. Trivić S., Stančić B., Leskovac V. Oxidation of alcohols by yeast alcohol dehydrogenase (review). Chem. Ind. (Beograd). 51:1997;113-118.
25. Leskovac V., Trivić S., Anderson B.M. Yeast alcohol dehydrogenase catalyzed reduction of p-nitroso-N,N-dimethylaniline by NADH. Ital. J. Biochem. 45:1996;9-18.
26. Trivić S., Leskovac V., Winston G.W. Aldehyde dismutase activity of yeast alcohol dehydrogenase. Biotechnol. Lett. 21:1999;231-234.
27. Müller-Hill B., Wallenfels K. Mechanismus der Wasserstoff-übertragung mit Pyridinnucleotiden. XXV. Ist Acetaldehyd oder sein Hydrat Substrat der Alkoholdehydrogenase? Biochem. Z. 339:1964;349-351.
28. Wratten C.C., Cleland W.W. Product inhibition on yeast and liver alcohol dehydrogenase. Biochemistry. 2:1963;935-940.
29. Silverstein E., Boyer P.D. Equilibrium reaction rates and the mechanisms of liver and yeast alcohol dehydrogenase. J. Biol. Chem. 239:1964;3908-3914.
30. Dickenson C.J., Dickinson F.M. Inhibition by ethanol, acetaldehyde and trifluoroethanol of reactions catalysed by yeast and horse liver alcohol dehydrogenases. Biochem. J. 171:1978;613-627.
31. Dickinson F.M., Dickenson C.J. Estimation of rate and dissociation constants involving ternary complexes in reactions catalyzed by yeast alcohol dehydrogenase. Biochem. J. 171:1978;629-637.
32. Gould R.M., Plapp B.V. Substitution of arginine for histidine-47 in the coenzyme binding site of yeast alcohol dehydrogenase. Biochemistry. 29:1990;5463-5468.
33. Trivić S., Leskovac V. Kinetic mechanism of yeast alcohol dehydrogenase with primary aliphatic alcohols and aldehydes. Biochem. Mol. Biol. Int. 32:1994;399-407.
34. Leskovac V., Trivić S., Anderson B.M. Use of pH studies to determine the kinetic and chemical mechanism of yeast alcohol dehydrogenase with primary aliphatic alcohols and aldehydes. Indian J. Biochem. Biophys. 33:1996;177-183.
35. Leskovac V., Trivić S., Anderson B.M. Use of competitive dead-end inhibitors to determine the chemical mechanism of action of yeast alcohol dehydrogenase. Mol. Cell. Biochem. 178:1998;219-227.
36. Leskovac V., Trivić S., Anderson B.M. Comparison of the chemical mechanisms of action of yeast and equine liver alcohol dehydrogenase. Eur. J.Biochem. 264:1999;840-847.
37. Dalziel K. Purification of yeast alcohol dehydrogenase. Trans. Faraday Soc. 54:1958;1247-1253.
38. Segel, I.H. (1975) Steady state kinetics of bisubstrate reactions. In: Enzyme Kinetics, Chapter IX, pp. 560-610. Wiley, New York.
39. Ganzhorn A.J., Plapp B.V. Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenase. J. Biol. Chem. 263:1988;5446-5454.
40. Amiguet, J.P. (1975) Wirkungsmechanismus der Hefe Alkoholdehydrogenase. Ph.D. thesis. Eidgenössische Technische Hochschule, Zürich.
41. Dickenson C.J., Dickinson F.M. A study of the oxidation of butan-1-ol and propan-2-ol by nicotinamide dinucleotide catalyzed by yeast alcohol dehydrogenase. Biochem. J. 147:1975;541-547.
42. Barshop B.A., Wrenn R.F., Frieden C. Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM - A flexible, portable system. Anal. Biochem. 130:1983;134-145.
43. Zimmerle C.T., Frieden C. Analysis of progress curves by simulation generated by numerical integration. Biochem. J. 258:1989;381-387.
44. Frieden C. Analysis of kinetic data: practical application of computer simulation and fitting programs. Methods Enzymol. 240:1994;311-322.
45. Leskovac, V., Trivić, S. and Pericin, D. (2002) Isomerization of enzyme-coenzyme complexes in yeast alcohol dehydrogenase-catalyzed reactions. Unpublished results.
46. Northrop D.B. Effects of high pressure on enzymatic activity. Biochim. Biophys. Acta. 1595:2002;71-79.
47. Eklund, H. and Brändén, C.-I. (1987) Alcohol dehydrogenase. In: Biological Macromolecules and Assemblies: Active Site of Enzymes (Jurnak, F.A. and McPherson, A., Eds.), Vol. 3, pp. 73-142. Wiley, New York.
48. Chandra Sekhar V., Plapp B.V. Rate constant for a mechanism including intermediates in the interconversion of ternary complexes by horse liver alcohol dehydrogenase. Biochemistry. 29:1990;4289-4295.
49. Cho Y.K., Northrop D.B. Effects of pressure on the kinetics of capture by yeast alcohol dehydrogenase. Biochemistry. 38:1999;7470-7475.
50. Leskovac V., Trivić S., Latkovska M. State and accessibility of zinc in yeast alcohol dehydrogenase. Biochem. J. 155:1976;155-161.
51. Havlis J., Studnickova M. Zinc centers in alcohol dehydrogenase from horse liver and from baker's yeast are metal dithiolenes. Bioelectrochem. Bioenerg. 43:1997;157-159.
52. Magonet E., Hayen P., Delforge D., Delaive E., Remacle J. Importance of the structural zinc atom for stability of yeast alcohol dehydrogenase. Biochem. J. 287:1992;361-365.
53. Jörnvall H. Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects. Eur. J. Biochem. 72:1977;443-452.
54. Benetzen J.L., Hall B.D. The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase I. J. Biol. Chem. 257:1982;3018-3025.
55. Russel D.W., Smith M., Williamson V.M., Young E.T. Nucleotide sequence of the yeast alcohol dehydrogenase II gene. J. Biol. Chem. 258:1983;2674-2682.
56. Ramaswamy S., Kratzer D.A., Hershey A.D., Rogers P.H., Arnone A., Eklund H., Plapp B.V. Crystallization and preliminary crystallographic studies of Saccharomyces cerevisiae alcohol dehydrogenase I. J. Mol. Biol. 235:1994;777-779.
57. Jörnvall H., Eklund H., Brändén C.-I. Subunit conformation of yeast alcohol dehydrogenase. J. Biol. Chem. 253:1978;8414-8419.
58. Plapp, B.V., Ganzhorn, A.J., Gould, R.M., Green, D.W., Jacobi, T., Warth, E. and Kratzer D.A. (1990) Catalysis by yeast alcohol dehydrogenase. In: Enzymology and Molecular Biology of Carbonyl Metabolism 3 (Weiner, H., Wermuth, B. and Crabb, D.V., Eds.), pp. 241-251. Plenum Press, New York.
59. Eklund H., Plapp B.V., Samama J.-P., Brändén C.-I. Binding of substrate in a ternary complex of horse liver dehydrogenase. J. Biol. Chem. 257:1982;14349-14358.
60. Cook P.F., Cleland W.W. pH Variation of isotope effects in enzyme-catalyzed reactions. Biochemistry. 20:1981;1797-1816.
61. Plapp, B.V., Ganzhorn, A.J., Gould, R.M., Green, D.W. and Hershey, A.D. (1987) Structure and function in yeast alcohol dehydrogenases. In: Enzymology and Molecular Biology of Carbonyl Metabolism 3 (Weiner, H. and Flynn, T.G., Eds.), pp. 227-236, Alan R. Liss, New York.
62. Fan Fan, Plapp B.V. Probing the affinity and specificity of yeast alcohol dehydrogenase I for coenzymes. Arch. Biochem. Biophys. 367:1999;240-249.
63. Fan Fan, Lorenzen J.A., Plapp B.V. An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme. Biochemistry. 30:1991;6397-6401.
64. Weinhold E.G., Glasfeld A., Ellington A.D., Benner S.A. Structural determinants of stereospecificity in yeast alcohol dehydrogenase. Proc. Natl. Acad. Sci. USA. 88:1991;8420-8424.
65. + binding by yeast alcohol dehydrogenase in the presence of pyrazole and a new method for the determination of the enzyme active site concentrations. Biotechnol. Lett. 19:1997;809-811.
66. Cleland W.W. The use of pH studies to determine chemical mechanism of enzyme-catalyzed reactions. Methods Enzymol. 87:1982;391-405.
67. 2+-bound water in alcohol dehydrogenase. Eur. J. Biochem. 247:1997;914-919.
68. Fischer H.F., Conn E.E., Vennesland B., Westheimer F.H. The enzymatic transfer of hydrogens. 1. The reaction catalyzed by alcohol dehydrogenase. J. Biol. Chem. 202:1953;687-697.
69. Westheimer, F.H. (1987) Mechanism of action of pyridine nucleotides. In: Pyridine Nucleotide Coenzymes (Jurnak, F.A., McPherson, A. and Avramovic, J., Eds.), Part A, pp. 253-322. Wiley, New York.
70. Cook P.F., Oppenheimer N.J., Cleland W.W. Secondary deuterium and nitrogen-15 isotope effects in enzyme-catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenase. Biochemistry. 20:1981;1817-1825.
71. Klinman, J.P. (1978) Kinetic isotope effects in enzymology. In: Advances in Enzymology and Related Areas of Molecular Biology (Meister, A., Ed.), Vol. 46, pp. 415-440. Wiley, New York.
72. Klinman, J.P. (1993) Hydrogen tunneling and coupled motion in enzyme reactions. In: Enzyme Mechanism from Isotope Effects (Cook, P.F., Ed.), pp. 127-147. Academic Press, New York.
73. Bahnson B.J., Colby T.D., Chin J.K., Goldstein B.M., Klinman J.P. A link between protein structure and enzyme catalyzed hydrogen tunneling. Proc. Natl. Acad. Sci. USA. 94:1997;12797-12802.
74. Cha Y., Murray C.J., Klinman J.P. Hydrogen tunneling in enzyme reactions. Science. 243:1989;1325-1330.
75. Klinman J.P. Isotope effects and structure-reactivity correlations in the yeast alcohol dehydrogenase reaction. A study of the enzyme-catalyzed oxidation of aromatic alcohols. Biochemistry. 15:1976;2018-2026.
76. + and substituted benzyl alcohols. Biochemistry. 33:1994;5230-5237.
77. Bahnson B.J., Klinman J.P. Hydrogen tunneling in enzyme catalysis. Methods Enzymol. 349:1995;373-397.
78. Kohen A., Klinman J.P. Hydrogen tunneling in biology. Chem. Biol. 6:1999;R191-R198.
79. + and NADH models. Bioorg. Chem. 25:1997;1-10.