Modeling the Kinetics of an Enzyme System
Document Type
Thesis
Publication Date
2011
Disciplines
Chemistry | Mathematics | Physical Sciences and Mathematics
Advisor
Henry Jakubowski, Chemistry; Tom Sibley, Mathematics
Abstract
The enzyme catalyzed hydrolysis of para-nitrophenylphosphate was studied using progress curve analysis techniques. The product of this reaction is a known enzyme inhibitor for this system. The system was assumed to follow Michaelis-Menten kinetics. From modified Michaelis-Menten differential equations, Lambert function models for competitive, uncompetitive, mixed inhibition, and their respective product inhibition versions were determined. These models can be used to fit progress curve data in order to determine the Michaelis constant, inhibition constants, and the maximal velocity of the system.
Recommended Citation
Kokkila, Sara, "Modeling the Kinetics of an Enzyme System" (2011). Honors Theses, 1963-2015. 130.
https://digitalcommons.csbsju.edu/honors_theses/130