By James M. Lee
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And D. Burk, “The Determination of Enzyme Dissociation Constants,” J. Amer. Chem. Soc. 56 (1934):658–666. Michaelis, L. and M. L. Menten, “Die Kinetik der Invertinwirkung,” Bio-chem. Zeitschr. 49 (1913):333–369. ), pp. 576–606. , 1985. Scott, T. , C. G. Hill, and C. H. Amundson, “Determination of the Steady-state Behavior of Immobilized beta-Galactosidase Utilizing an Integral Reactor Scheme,” Biotechnol. Bioeng. Symp. 15 (1985):431– 445. Thomas, C. R. and P. Dunnill, “Action of Shear on Enzymes: Studies with Catalase and Urease,” Biotechnol.
B. If the concentration of S1 is much higher than that of S2, how can the rate equation be simplified? 3 In some enzyme-catalyzed reactions, multiple complexes are involved as follows: Enzyme Kinetics 2-37 k 1 """ # ES E + S $"" k " 2 ( ES) k3 """ #( ) $"" 1 k4 " ES 2 k5 ( ES)2 →E+P Develop a rate expression using (a) the Michaelis-Menten approach and (b) the Briggs-Haldane approach. 4 Suppose that two substrates are required for an enzymatic conversion according to the following mechanism: k1 """ # ES1 E+S1 $"" k2 " k3 """ # ES2 E+S2 $"" k4 " k3 """ # ES1S2 ES1 +S2 $"" k4 " k 5 →E+P ES1S2 Develop suitable rate expression using (a) the Michaelis-Menten approach and (b) Briggs-Haldane approach.
6. The rate predicted from the Eadie-Hofstee plot shows the similar tendency as that from the Lineweaver-Burk plot, but in a lesser degree. The rates predicted from the Langmuir plot and nonlinear regression technique are almost the same which give the best line fit because of the even weighting of the data. 3. 50 ; PROC NLIN METHOD=GAUSS; /* Gaussian method is default. KM=-RMAX*CS/((KM+CS)*(KM+CS));/* with respect to each parameter. */ Computer Output: PARAMETER RMAX KM ESTIMATE ASYMPTOTIC STD.