BCH 2333 Lecture Notes - Lecture 15: Glycogen Phosphorylase, Competitive Inhibition, Phosphofructokinase

• School: University of Ottawa
• Department: Biochemistry
• Course: BCH 2333
• Professor: Christopher Boddy

Document Summary

This enzyme can exist in 2 structural states. Follows the symmetry model (mwc) 2 states in equilibrium, binding impacts the equilibrium of t and r states. Highly cooperative system, all subunits change conformation together. R state, when bound to substrate, is more stable than. Only 1 monomer of trimer is shown. Ctp binds t state, stabilizes t state and prevents equilibrium to r state. Atp binds to r state, stabilizing it, activating the enzyme. Activator will bind preferentially to the r state. Inhibitor will bind preferentially to the t state. Allosteric activity is the fastest way for enzymes to respond to changes. They can immediately change the activity of enzymes to change things like in metabolic pathways. Activity of an enzyme can be slowed by binding of effector. ** see lab manual for all these equations (lab 3 appendix) **