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[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.
  • Classification : 92C45
  • Format : Talk at Waseda University
  • Author(s) :
    • Hideshi Ooka (RIKEN)
    • Yoko Chiba (RIKEN)
    • Ryuhei Nakamura (RIKEN)