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Allosteric Regulation

Enzyme activity is modulated by molecules binding at sites distinct from the active site, altering the enzyme's conformation and kinetics.
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The statement of the theorem

Consider an enzyme EE regulated by an effector AA. The modified rate vAv_A can be expressed by modifying the apparent KmK_m or VmaxV_{max} based on the effector binding equilibrium. For an activator AA, the rate may be approximated as:\nvA=Vmax[S]Km1+[A]/KA1+[A]/KA1+[S]Km11+[A]/KAv_A = \frac{V_{max} \frac{[S]}{K_m} \frac{1 + [A]/K_A}{1 + [A]/K_A}}{1 + \frac{[S]}{K_m} \frac{1}{1 + [A]/K_A}} \nwhere KAK_A is the dissociation constant for the effector AA.