Chapter_11_Catalysis - Chemistry 233 Fundamentals of...

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Chemistry 233 Fundamentals of Biochemistry Enzymes: Catalysis and Kinetics
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ENZYMES Catalysis and Kinetics Aspects of catalysis (Chapter 13 and 14) Kinetics (Chapter 14) ES complex Michaelis-Menten Kinetics Inhibition
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What is a catalyst? increased rate of reaction activation energy is reduced G o is NOT changed catalyst is not consumed by the reaction
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How do they do it? Comparison of reaction rates with and without catalysis for one reaction. Enzymes have reaction rates up to 10 8 X the uncatalyzed reaction
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What is an “active sites”? What is a “substrate”? The binding of substrate to active site initiates catalysis The binding site is complementary to substrate structure
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Enzymes recognize stereoisomers and geometric isomers Enzymes have very high specificity for substrates
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Transition state theory: enzymes stabilize the “transition state” of a reaction For the reaction A B A X B X is the transition state, halfway between A and B
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Strategies that enzymes use to catalyze reactions: use of amino acid side chains for acid-base catalysis, and cofactors binding energy from the bonds made between substrate and enzyme in the active site
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entropy reduction: bringing substrates together in the correct orientation desolvation of substrates: water solvation is replaced by amino acid side chains
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use alternate reaction pathways: multistep reactions
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What is a “rate limiting step”?
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Effect of pH and temperature Enzymes have a temperature optimum
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Enzymes also have a pH optimum What factors influence the shape and position of these curves?
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There are many types of enzymes: EC classification
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