2009-10-02_-_Lecture_12

2009-10-02_-_Lecture_12 - Biochemistry 461 FS 2009 Michigan...

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Biochemistry 461 FS 2009 Michigan State University Catalytic Strategies October 2, 2009 Lecture 12 Irreversible inhibition refers to the formation of a (usually) covalent bond between inhibitor and enzyme that prevents activity. Irreversible inhibitors often modify a functional group that is essential for activity. • A subclass of irreversible inhibitors are mechanism-based or suicide inhibitors, pseudosubstrates that undergo the preliminary steps of catalysis before combining irreversibly. • These can be very informative in mechanistic studies. Irreversible Inhibition (from previous lecture) 2
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Transition State Analogs (from previous lecture) • Transition state analogs can be potent enzyme inhibitors • Some TS analogs bind 10 2 -10 6 more tightly than the substrate • Principle can be used in pharmaceuticals -- HIV protease inhibitors 3 Enzymes Participating in Catalysis • Strategies enzymes utilize when participating directly in catalysis ¾ General acid-base catalysis ¾ Covalent catalysis ¾ Metal ion catalysis • What are the “reactive” groups utilized by enzymes? 4
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This note was uploaded on 01/17/2012 for the course NSC 461 taught by Professor Benning during the Fall '11 term at Michigan State University.

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2009-10-02_-_Lecture_12 - Biochemistry 461 FS 2009 Michigan...

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