Lecture19

Lecture19 - Lecture 19 11/16/11 Background reading: Berg,...

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Unformatted text preview: Lecture 19 11/16/11 Background reading: Berg, et al: Pages 260 - 263 Garrett and Grisham: Pages 458 - 459 Outline: Mechanism of chymotrypsin catalysis Catalytic triad Substrate binding Oxyanion hole Cleavage of peptide bond Deacylation of enzyme Specificity pocket Mechanism of chymotrypsin catalysis This is the burst phase which produces the colored product.. This acyl-enzyme intermediate complex is then hydrolyzed to release the carboxylic acid component of the substrate and regenerate the free enzyme as shown below. This is the steady-state phase, which takes longer for the enzyme to be released. Catalytic triad S 195 is H-bonded to the imidazole ring of H 57. The NH group of the imidazole ring of H 57 is, in turn, H-bonded to the carboxylate group of D 102. The arrangement of these 3 residues is known as the catalytic triad. The H 57 positions the S 195 to polarize its hydroxyl group so it can be deproton- ated. The D 102 helps orient H 57 and make it a better proton acceptor....
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This note was uploaded on 01/15/2012 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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Lecture19 - Lecture 19 11/16/11 Background reading: Berg,...

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