Chem4711%28NoteSet6%29-1

Chem4711%28NoteSet6%29-1 - Chymotrypsin Bovine pancreatic...

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Unformatted text preview: Chymotrypsin Bovine pancreatic chymotrypsin- MW = 25,191- catalyzes the hydrolytic cleavage of peptide bonds- specific for bonds adjacent to Trp, Phe, and Tyr- rate acceleration = 10 9-fold- uses covalent catalysis (Ser195)- two step reaction with an intermediate- uses acid/base catalysis (His57, Asp102) Serine proteases hymotrypsin regulation Amount of enzyme Synthesize as an inactive precursor (Other mechanisms that can be used with other enzymes) Covalent modification of enzyme Allosteric regulator Inhbitors Chymotrypsin - zymogen Chymotrypsin - catalytic triad Chymotrypsin - active site Chymotrypsin - active site Asp102 Ser195 His57 Chymotrypsin - active site Chymotrypsin - pH-dependence V max K m His57 His57 Ile16 Ile16 Chymotrypsin - burst kinetics Chymotrypsin - burst kinetics Burst kinetics Used to: - titrate enzyme active sites- prove formation of an intermediate Experiment: Use sufficient enzyme so that you can detect single turnover Use excess substrate Initial exponential phase characterized by sum of rates Linear phase follows (should equal k ss ) E + A B C k 1 [A] k 2 slope = [ E ] k 1 ' k 2 k 1 ' + k 2 ae time product burst = [ E ] k 1 ' k 1 ' + k 2 ae 2 1/ t = k 1 ' + k 2 Chymotrypsin - active site labeling Chymotrypsin - catalytic triad Chymotrypsin - mechanism (extrinsic binding energy) (intrinsic binding energy, nucleophilic catalysis, acid/base catalysis, electrostatic catalysis, t.s. stabilization) (intrinsic binding energy, acid/base catalysis) (acid/base catalysis, electrostatic catalysis, t.s. stabilization) (acid/base catalysis) Chymotrypsin - Michaelis complex...
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Chem4711%28NoteSet6%29-1 - Chymotrypsin Bovine pancreatic...

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