Comparison of the chemical mechanisms of action of yeast and equine liver alcohol dehydrogenase

European Journal of Biochemistry

Volumn 264, Issue 3, 1999, Pages 840-847

  Leskovac, Vladimir ^b   Trivić, Svetlana ^c   Anderson, Bruce M ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^b Faculty of Technology   (Serbia)

^c NONE

Author keywords

Chemical mechanism of action; Yeast alcohol dehydrogenase

Indexed keywords

ALCOHOL DEHYDROGENASE;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DISSOCIATION; ENZYME BINDING; ENZYME KINETICS; LIGAND BINDING; NONHUMAN; PH; PRIORITY JOURNAL; STEADY STATE;

EQUIDAE; EQUUS CABALLUS;

EID: 0038967110     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00675.x     Document Type: Article

References (31)

1. 1. Branden, C.-I., Jomvall, H., Eklund, H. & Furugren, B. (1975) Alcohol dehydrogenases. In The Enzymes (Boyer, P. D., ed.), Vol. XI, 3rd edn, pp. 103-190. Academic Press, New York.
2. 2. Eklund, H. & Branden, C.-I. (1987) Alcohol dehydrogenase. In Biological Macromolecules and Assemblies (Jurnak, F.A. & McPherson, eds), Vol. 3, pp. 75-142. Wiley, New York.
3. 3. Ehring, T., Hurley, T.D., Edenberg, H.J. & Bosron, W.F. (1991) General base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase. Biochemistry 30, 1062-1068.
4. 4. Inoue, J., Tomioka, N., Itai, A. & Harayama, S. (1998) Proton-transfer in benzyl alcohol-dehydrogenase during catalysis - alternate proton-relay routes. Biochemistry 37, 3305-3311.
5. 5. Plapp, B.V., Ganzhorn, A.J., Gould, R.M., Green, D.W., Jacobi, T., Warth, E., Kratzer, D.A. (1990) Catalysis by yeast alcohol dehydrogenase. In Enzymology and Molecular Biology of Carbonyl Metabolism 3 (Weiner, H. et al., eds), pp. 241-251. Plenum Press, New York.
6. 6. Henehan, G.T.M., Chang, S.H. & Oppenheimer, N.J. (1995) Aldehyde dehydrogenase activity of Drosophila melanogaster alcohol-dehydrogenase - burst kinetics at high pH and aldehyde dismutase activity at physiological pH. Biochemistry 34, 12294-12301.
7. 7. Cook, P.F. & Cleland, W.W. (1981) pH variation of isotope effects in enzyme-catalyzed reactions. Biochemistry 20, 1797-1805.
8. 8. Trivić, S. & Leskovac, V. (1994) Kinetic mechanism of yeast alcohol dehydrogenase activity with secondary alcohols and ketones. Ind. J. Biochem. Biophys. 31, 387-391.
9. 9. Trivić, S. & Leskovac, V. (1994) Kinetic mechanism of yeast alcohol dehydrogenase with primary aliphatic alcohols and aldehydes. Biochem. Mol. Biol. Int. 32, 399-407.
10. 10. Leskovac, V., Trivić, S. & Anderson, B.M. (1996a) Yeast alcohol dehydrogenase catalyzed reduction of, p-nitroso-N,N-dimethylaniline by NADH. Ital. J. Biochem. 45, 9-18.
11. 11. Leskovac, V., Trivić, S. & Anderson, B.M. (1996b) Use of pH studies to determine the kinetic and chemical mechanism of yeast alcohol dehydrogenase with primary aliphatic alcohols and aldehydes. Ind. J. Biochem. Biophys. 33, 177-183.
12. + . J. Serb. Chem. Soc. 62, 1239-1243.
13. + 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, 809-812.
14. 14. Leskovac, V., Trivić, S., Zeremski, J., Stančić, B. & Anderson, B.M. (1997) Novel substrates of yeast alcohol dehydrogenase - 3, 4-dimethylamino-cinnamaldehyde and chloroacetaldehyde. Biochem. Molec. Biol. Int. 43, 365-373.
15. 15. Leskovac, V., Trivić Anderson, B.M. (1998) Use of competitive dead-end inhibitors to determine the chemical mechanism of action of yeast alcohol dehydrogenase. Molec. Cell. Biochem. 178, 219-227.
16. 16. Dickenson, C.J. & Dickinson, M.F. (1975) A study of the oxidation of butan-1-ol and propan-2-ol by nicotinamide dinucleotide catalyzed by yeast alcohol dehydrogenase. Biochem. J. 147, 541-547.
17. 17. Bergmeyer, H.U. (1970) In Methoden der Enzymatischen Analyse, pp. 392-393, 1457-1474. Verlag Chemie, Weinheim/Bergstrasse.
18. 18. Hayes, J.H. & Velick, S.F. (1954) Isolation and purification of yeast alcohol dehydrogenase. J. Biol. Chem. 207, 225-232.
19. 19. Leskovac, V., Trivić, S. & Pantelić, M. (1993) A simple fluorimetric method for the estimation of ligand binding parameters in ligand-enzyme complexes. Anal. Biochem. 214, 431-434.
20. 20. Cleland, W.W. (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol. 63, 103-137.
21. 21. Cleland, W.W. (1970) Steady-state enzyme kinetics. In The Enzymes (Boyer, P.D., ed.), Vol. II, pp. 1-65. Academic Press, New York.
22. 22. Segel, I.H. (1975) Enzyme Kinetics, pp. 100-159. Academic Press, New York.
23. 23. Leskovac, V., Peričin, D. & Trivić IV. Binding of reduced coenzyme and its fragments. Int. J. Biochem. 9, 365-371.
24. 24. Dickinson, F.M. & Monger, G.P. (1973) A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates. Biochem. J. 131, 261-270.
25. 25. Dickinson, F.M. & Dickenson, C.J. (1978) Estimation of rate and dissociation constants involving ternary complexes in reactions catalyzed by yeast alcohol dehydrogenase. Biochem. J. 171, 629-637.
26. 26. Cleland, W.W. (1982) The use of pH studies to determine chemical mechanism of enzyme-catalyzed reactions. Methods Enzymol. 87, 391-405.
27. 27. Fersht, A. (1985) The pH dependence of enzyme catalysis. In Enzyme Structure and Mechanism, pp. 155-175. WH Freeman, London.
28. 28. Fromm, H. (1979) Use of competitive inhibitors to study substrate binding order. Methods Enzymol. 63, 467-486.
29. 29. Kvassman, J. & Pettersson, G. (1979) Effect of pH on coenzyme binding to horse liver alcohol dehydrogenase. Eur. J. Biochem. 100, 115-123.
30. 30. Cha, S. (1968) A simple method for derivation of rate equations for enzyme-catalyzed reactions under rapid equilibrium assumption or combined assumptions of equilibrium and steady-state. J. Biol. Chem. 243, 820-825.
31. a values. Biochem. J. 167, 859-862.