[00429] Mathematical Theory to Maximize Enzymatic Activity Under Thermodynamic Constraints
Session Time & Room : 1C (Aug.21, 13:20-15:00) @D515
Type : Contributed Talk
Abstract : Understanding the relationship between enzymatic activity is critical not only for bioengineering, but also for rationalizing enzyme optimization in nature. Here, we applied the Arrhenius and Bronsted-Evans-Polanyi equations to the Michaelis-Menten model of enzyme catalysis, and show that enzymatic activity is maximized when the binding affinity between the enzyme and the substrate (Km) is equal to the substrate concentration.
