BIOL 2021 Lecture Notes - Lecture 5: Non-Competitive Inhibition, Uncompetitive Inhibitor, Hiv-1 Protease
Document Summary
Inhibitors: decrease the rates of their catalysis. Irreversible inhibitors: enzyme is covalently modified after interaction with inhibitor, derivatized enzyme is no longer a catalyst loses enzymatic activity, original activity cannot be regenerated, also called suicide inhibitors. Acetylates ser in active site of cyclooxygenase (cox) enzyme: reversible inhibitors, bind to enzyme and are subsequently released, leave enzyme in original condition, three subclasses: Uncompetitive inhibitors: can be distinguished by their kinetics of inhibition. How are inhibitors characterized experimentally: first, perform experiment without inhibitor, measure velocity at different substrate concentrations, keeping [e] constant. Chm333 lectures 16 & 17: 2/22 25/13 spring 2013 professor christine hrycyna: competitive inhibitors, shape and structure of inhibitor is very similar to substrate. Inhibitor mimic substrate (or transition state) and fits into the active site: physically blocks substrate"s access into the active site. Competitive inhibitors which mimic the transition state of an enzyme catalyzed reaction (e. g. hiv protease inhibitors such a saquinavir and viracept).
