Title

Modeling the Kinetics of an Enzyme System

Document Type

Thesis

Publication Date

2011

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.

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