Enzyme Kinetics

Citation
In: Jaeger, KE., Liese, A., Syldatk, C. (eds) Introduction to Enzyme Technology. Learning Materials in Biosciences. Springer, Cham. (2024) 61-90
Publisher DOI
10.1007/978-3-031-42999-6_4
Publisher
Springer International Publishing
ISBN
9783031429989
9783031429996
In this chapter, you will learn the fundamental concepts of chemical and enzyme catalysis as well as kinetics such as the lock and key and the induced-fit models, the idea of an enzyme-substrate complex, the Michaelis-Menten equation, or the steady-state assumption. Key basic concepts such as catalysts and their classification, reaction rate, enzyme inhibition, and the order of a reaction are also explained. A fundamental point to evaluate enzyme-catalyzed reactions is the determination of kinetic parameters such as the Michaelis-Menten constant and the maximum reaction rate. Their calculation using linearization, numeric, and combined methods is explained in this chapter. Here you will also find the necessary equations and models to determine other relevant parameters such as the turnover frequency and the specificity constant.