06-Guest Lecture Dr Guvener

06-Guest Lecture Dr Guvener - Chapter 6: Enzyme Catalysis...

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Tüzün Güvener, Ph.D. Senior Research Scientist University of Wyoming Chapter 6: Enzyme Catalysis and Regulation
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Overview Enzyme catalysis Organic reactions and transition state The role of amino acids in catalysis The role of cofactors (coenzymes) in catalysis Effects of temperature and pH Enzyme regulation Genetic control Covalent modification phosphorylation dephosphorylation cleavage of proenzymes active enzyme Allosteric regulation Compartmentation
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Why do we care about how enzymes catalyze reactions? Why we want to understand the mechanisms of enzymatic reactions? We can design inhibitors to manipulate the activity of enzymes with medical importance use in clinical therapies. drugs antibiotics food preservatives AIDS patients protease inhibitors disable viral replication Movie Drug: CisPlatin http://il.youtube.com/watch?v=XHCPq9LALnU
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- Enzymes are very important catalysts for chemical reactions in every living organisms. - alter “activation energy ( E a )” or “free energy of activation G ‡” - speed up reactions. Review: Enzyme Properties Heat increasing collisions [A] Enzymes [B] Product C A + B What is “activation energy” of a reaction?
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In enzyme-catalyzed reactions, enzymes provide alternative pathway that requires less energy. - enzymes stabilize the transition state. Substrate-enzyme interactions force the substrate to undergo conformational changes. The induced-fitting favors the “Transition state” Enzyme-substrate complex proceeds with product formation. - enzymes do not affect “the free energy state G °” . - enzymes themselves do not change in the reaction and they are recycled to perform another reaction.
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- Enzyme-catalyzed reactions are highly specific. A specific substrate is recognized by a specific enzyme. Why?
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This note was uploaded on 10/15/2010 for the course MOLB 3610 taught by Professor Gomelsky during the Fall '10 term at Wyoming.

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06-Guest Lecture Dr Guvener - Chapter 6: Enzyme Catalysis...

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