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Estimating Enzyme Kinetic Parameters from Apparent KMs and Vmaxs
Abstract:The kinetic properties of enzymes are often reported using the apparent KM and Vmax appropriate to the standard Michaelis-Menten enzyme. However, this model is inappropriate to enzymes that have more than one substrate or where the rate expression does not apply for other reasons. Consequently, it is desirable to have a means of estimating the appropriate kinetic parameters from the apparent values of KM and Vmax reported for each substrate. We provide a means of estimating the range within which the parameters should lie and apply the method to data for glutamate dehydrogenase from the nematode parasite of sheep Teladorsagia circumcincta.
Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1075865Procedia APA BibTeX Chicago EndNote Harvard JSON MLA RIS XML ISO 690 PDF Downloads 1701
 L. Michaelis and M. L. Menten, "Die Kinetik der Invertinwirkung," Biochemische Zeitschrift, vol. 49, pp. 333-369, 1913.
 N. Muhamad, D. C. Simcock, K. C. Pedley, H. V. Simpson, and S. Brown, "The kinetics of glutamate dehydrogenase of Teladorsagia circumcincta and the lifestyle of the parasite," Comparative Biochemistry and Physiology, submitted for publication, 2011.
 C. M. Hill, R. D. Waight, and W. G. Bardsley, "Does any enzyme follow the Michaelis-Menten equation?," Molecular and Cellular Biochemistry, vol. 15, pp. 173-178, 1977.
 K. Dalziel, "The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates," Biochemical Journal, vol. 114, pp. 547-556, 1969.
 K. R. F. Elliott and K. F. Tipton, "A kinetic analysis of enzyme systems involving four substrates," Biochemical Journal, vol. 141, pp. 789-805, 1974.
 A. Chang, M. Scheer, A. Grote, I. Schomburg, and D. Schomburg, "BRENDA, AMENDA and FRENDA the enzyme information system: new content and tools in 2009," Nucleic Acids Research, vol. 37, pp. D588-D592, 2009.
 G. E. Briggs and J. B. S. Haldane, "A note on the kinetics of enzyme action," Biochemical Journal, vol. 19, pp. 338-339, 1925.
 U. Borgmann, K. J. Laidler, and T. W. Moon, "Four- and five-step kinetic models of lactate dehydrogenase," Canadian Journal of Biochemistry, vol. 54, pp. 915-918, 1976.
 J. A. Urbina and V. Azavache, "Regulation of energy metabolism in Trypanosoma (Schizotrypanum) cruzi epimastigotes. II. NAD+- dependent glutamate dehydrogenase," Molecular and Biochemical Parasitology, vol. 11, pp. 241-255, 1984.
 R. E. Moore, Methods and applications of interval analysis. Philadelphia: Society for Industrial and Applied Mathematics, 1979.
 W. G. Bardsley, P. Leff, J. Kavanagh, and R. D. Waight, "Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine oxidase, chymotrypsin, fumarase, galactose dehydrogenase, ß-galactosidase, lactate dehydrogenase, peroxidase and xanthine oxidase," Biochemical Journal, vol. 187, pp. 739-765, 1980.
 J. Mayer, K. Khairy, and J. Howard, "Drawing an elephant with four complex parameters," American Journal of Physics, vol. 78, pp. 648- 649, 2010.
 J. R. Kinghorn and J. A. Pateman, "NAD and NADP L-glutamate dehydrogenase activity and ammonium regulation in Aspergillus nidulans," Journal of General Microbiology, vol. 78, pp. 39-46, 1973.
 G. L. Abrahams and V. R. Abratt, "The NADH-dependent glutamate dehydrogenase enzyme of Bacteroides fragilis Bf1 is induced by peptides in the growth medium," Microbiology, vol. 144, pp. 1659- 1667, 1998.
 C. Frieden, "Glutamic dehydrogenase. III. The order of substrate addition in the enzymatic reaction," Journal of Biological Chemistry, vol. 234, pp. 2891-2896, 1959.
 J. E. Rife and W. W. Cleland, "Kinetic mechanism of glutamate dehydrogenase," Biochemistry, vol. 19, pp. 2321-2328, 1980.
 D. P. Hornby, M. J. Aitchison, and P. C. Engel, "The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate," Biochemical Journal, vol. 223, pp. 161-168, 1984.
 NC-IUB Nomenclature Committee of the International Union of Biochemistry, "Symbolism and terminology in enzyme kinetics. Recommendations 1981," European Journal of Biochemistry, vol. 128, pp. 281-291, 1982.
 S. Brown, "Developing the enzyme-machine analogy: a nonmathematical approach to teaching Michaelis-Menten kinetics," Orbital, vol. 2, pp. 92-100, 2010.
 D. P. Bertsekas, Constrained optimization and Lagrange multiplier methods. Belmont: Athena Scientific, 1996.