Enzyme mechanisms from isotope effects

Isotope Effects in Chemistry and Biology

Volumn , Issue , 2005, Pages 915-930

  Cleland, W Wallace ^a  

^a UNIVERSITY OF WISCONSIN   (United States)

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EID: 85056434067     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420028027     Document Type: Chapter

References (36)

1. 18O equilibrium isotope effects and fractionation factors, Can. J. Chem., 77, 967-977, 1999.
2. Cleland, W. W., Measurement of isotope effects by the equilibrium perturbation technique, Methods Enzymol., 64, 104-125, 1980.
3. Taylor, J. W. and Grimsrud, E. P., Chlorine isotopic ratios by negative ion mass spectrometry, Anal. Chem., 41, 805-810, 1969.
4. Lewandowicz, A., Sicinska, D., Rudzinski, J., Ichiyama, S., Kurihara, T., Esaki, N., and Paneth, P., Chlorine kinetic isotope effect on the fluoroacetate dehalogenase reaction, J. Am. Chem. Soc., 123, 9192-9193, 2001.
5. Hengge, A. C. and Hess, R. A., Concerted or stepwise mechanisms for acyl transfer reactions of p-nitrophenyl acetate? Transition state structures from isotope effects, J. Am. Chem. Soc., 116, 11256-11263, 1994.
6. Schramm, V. L., Enzymatic transition states and transition state analog design, Annu. Rev. Biochem., 67, 693-720, 1998.
7. Schramm, V. L., Enzymatic transition-state analysis and transition-state analogs, Methods Enzymol., 308, 301-355, 1999.
8. Cook, P. F. and Cleland, W. W., pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same, Biochemistry, 20, 1797-1805, 1981.
9. Northrop, D. B., Steady-state analysis of kinetic isotope effects in enzymatic reactions, Biochemistry, 14, 2644-2651, 1975.
10. Swain, C. G., Stivers, E. C., Reuwer, J. F. Jr, and Schaad, L. J., Use of hydrogen isotope effects to identify the attacking nucleophile in the enolization of ketones catalyzed by acetic acid, J. Am. Chem. Soc., 80, 5885-5893, 1958.
11. Table for use with Northrop’s method. In Isotope Effects on Enzyme-Catalyzed Reactions, Cleland, W. W., O’Leary, M. H., and Northrop, D. B., Eds., University Park Press, Baltimore, pp. 280-283, 1977.
12. Hermes, J. D., Roeske, C. A., O’Leary, M. H., and Cleland, W. W., Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose-6-phosphate dehydrogenase, Biochemistry, 21, 5106-5114, 1982.
13. Hermes, J. D., Tipton, P. A., Fisher, M. A., O’Leary, M. H., Morrison, J. F., and Cleland, W. W., Mechanisms of enzymatic and acid-catalyzed decarboxylations of prephenate, Biochemistry, 23, 6263-6275, 1984.
14. Hermes, J. D. and Cleland, W. W., Evidence from multiple isotope effect determinations for coupled hydrogen motion and tunneling in the reaction catalyzed by glucose-6-phosphate dehydrogenase, J. Am. Chem. Soc., 106, 7263-7264, 1984.
15. Hermes, J. D., Morrical, S. W., O’Leary, M. H., and Cleland, W. W., Variation of Transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. Formate dehydrogenase, Biochemistry, 23, 5479-5488, 1984.
16. 13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamoylase, Biochemistry, 31, 6570-6576, 1992.
17. Monod, J., Wyman, J., and Changeux, J.-P., On the nature of allosteric transitions: a plausible model, J. Mol. Biol., 12, 88-118, 1965.
18. Waldrop, G. L., Turnbull, J. L., Parmentier, L. E., O’Leary, M. H., Cleland, W. W., and Schachman, H. K., Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase contining the replacement of Histidine 134 by alanine, Biochemistry, 31, 6585-6591, 1992.
19. 15N isotope effects on nonenzymatic and aspartate transcarbamylase catalyzed reactions of carbamyl phosphate, J. Am. Chem. Soc., 114, 5941-5945, 1992.
20. Weiss, P. M., Gavva, S. R., Harris, B. G., Urbauer, J. L., Cleland, W. W., and Cook, P. F., Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction, Biochemistry, 30, 5755-5763, 1991.
21. Edens, W. A., Urbauer, J. L., and Cleland, W. W., Determination of the chemical mechanism of malic enzyme by isotope effects, Biochemistry, 36, 1141-1147, 1997.
22. Karsten, W. E. and Cook, P. F., Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation, Biochemistry, 33, 2096-2103, 1994.
23. Karsten, W. E., Gavva, S. R., Park, S.-H., and Cook, P. F., Metal ion activator effects on intrinsic isotope effects for hydride transfer and decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum, Biochemistry, 34, 3253-3260, 1995.
24. Urbauer, J. L., Bradshaw, D. E., and Cleland, W. W., Determination of the kinetic and chemical mechanism of malic enzyme using (2R,3R)-erythro-fluoromalate as a slow alternate substrate, Biochemistry, 37, 18026-18031, 1998.
25. Reinhardt, L. A., Svedruzic, D., Chang, C. H., Cleland, W. W., and Richards, N. G. J., Heavy atom isotope effects on the reaction catalyzed by the oxalate decarboxylase from Bacillus subtilis, J. Am. Chem. Soc., 125, 1244-1252, 2003.
26. Gustin, D. J., Mattei, P., Kast, P., Wiest, O., Lee, L., Cleland, W. W., and Hilvert, D., Heavy atom isotope effects reveal a highly polarized transition state for chorismate mutase, J. Am. Chem. Soc., 121, 1756-1757, 1999.
27. Wright, S. K., DeClue, M. S., Mandal, A., Lee, L., Wiest, O., Cleland, W. W., and Hilvert, D., Isotope effects on the enzymatic and non-enzymatic reactions of chorismate, J. Am. Chem. Soc., in press.
28. 13C and deuterium isotope effects suggest an aldol cleavage mechanism for L-ribulose-5-phosphate 4-epimerase, Biochemistry, 39, 4808-4820, 2000.
29. Hermes, J. D., Weiss, P. M., and Cleland, W. W., Use of nitrogen-15 and deuterium isotope effects to determine the chemical mechanism of phenylalanine ammonia-lyase, Biochemistry, 24, 2959-2967, 1985.
30. Blanchard, J. S. and Cleland, W. W., Use of isotope effects to deduce the chemical mechanism of fumarase, Biochemistry, 19, 4506-4513, 1980.
31. 15N kinetic isotope effects on the reaction of aspartate aminotransferase and the tyrosine-225 to phenylalanine mutant, Biochemistry, 39, 7546-7551, 2000.
32. 15N kinetic isotope effects on the reaction of the ammonia-rescued K258A mutant of aspartate aminotransferase, Biochemistry, 42, 8369-8376, 2003.
33. Tipton, P. A. and Cleland, W. W., Carbon-13 and deuterium isotope effects on the catalytic reactions of biotin carboxylase, Biochemistry, 27, 4325-4331, 1988.
34. Attwood, P. V., Tipton, P. A., and Cleland, W. W., Carbon-13 and deuterium isotope effects on oxalacetate decarboxylation by pyruvate carboxylase, Biochemistry, 25, 8197-8205, 1986.
35. Weiss, P. M., Cook, P. F., Hermes, J. D., and Cleland, W. W., Evidence from nitrogen-15 and solvent deuterium isotope effects on the chemical mechanism of adenosine deaminase, Biochemistry, 26, 7378-7384, 1987.
36. Rishavy, M. A. and Cleland, W. W., Determination of the mechanism of orotidine 50-monophosphate decarboxylase by isotope effects, Biochemistry, 39, 4569-4574, 2000.