(112f) Numerical Analysis of Possible Improvements to the Steady-State Approximation in Enzyme Kinetics

The Briggs-Haldane and Michaelis-Menten expressions have been standards in mapping the kinetics of biochemical reactions for nearly 100 years, but the limited valid fitting domain for these functions and the approximations that produce them has led many to search for replacements. Here, two alternative suggestions for the pseudo-steady state approximation, based on relative rates, are explored. A valuable fitting parameter, previously used in quantifying position of the steady state trajectory between the Briggs-Haldane and Michaelis-Menten bounds, is related to other important kinetic parameters and used to evaluate the new steady state approximations. These approximations are also analyzed numerically and found to be superior to the standard steady-state approximation over a wide range of system variables. New fitting equations, based off the results of the previous analysis, are also discussed.