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lecture7&8_9_23&25_08

lecture7&8_9_23&25_08 - Lectures 7 8...

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Homework: 8.2, 8.4, 8.7, 8.11, 8.15 Lectures 7 & 8 Chapter 8: Stryer Overview: structure/classification enzyme thermodynamics transition state stabilization enzyme kinetics Michaelis-Menton kinetic parameters enzyme inhibition Enzymes are proteins (mostly) that are capable of catalyzing covalent bond cleavage and formation. Enzymes are agents of metabolic function. Key attributes: -alter the rate of product formation -specificity -reactivity conditions Components: enzyme (active site) substrate product (cofactor) (coenzyme) e.g., carbonic anhydrase in red blood cells; 10 7 rate acceleration Enzymes Substrate binding to the enzyme active site chymotrypsin (a protease) active site - residues that bind substrate and are involved with the catalytic mechanism Enzymes are organized into six classes based on the type of chemical reaction that they catalyze
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proteolysis: hydrolysis of a peptide bond enzyme = protease substrate = peptide/protein unnatural substrate: ester Enzymes Enzyme specificity trypsin cleaves on the carboxyl side of arginine and lysine residues thrombin cleaves Arg- Gly bonds in particular sequences only Cofactors: metal ions Coenzymes: organic Assist enzymes in their functions Know definitions: -prosthetic group -holoenzyme -apoenzyme -apoprotein
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Free energy and enzyme kinetics A –> B k Rate ( v ) = – d[A]/dt = d[B]/dt v = – d[A]/dt = k [A] 1st order reaction units time -1 A + B –> C k Rate ( v ) = – d[A]/dt = – d[B]/dt = d[C]/dt – d[A]/dt = k [A][B] 2nd order reaction units conc/time -1 mA + nB –> C k d[C]/dt = k [A] m [B] n m+n order reaction Most enzyme reactions are first order reactions. k = rate constant K ! eq = [C][D] [A][B] " ! = – RT ln [C][D] [A][B] 0 = " ! + RT ln [C][D] [A][B] A + B C + D " G = " + RT ln [C][D] [A][B] standard state is pH 7, units are kJ or kcal at equilibrium " G = 0 Free energy and enzyme kinetics " ! = – RT lnK !
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