Chapter_9 - Common Enzyme Strategies(Chapter 9 Enzymes act...

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Common Enzyme Strategies (Chapter 9) Enzymes act by binding substrate with free energy from weak interactions and by stabilizing the transition state 1. Covalent catalysis. Active site modification (chymotrypsin) 2. General acid-base catalysis (chymotrypsin) 3. Metal ion catalysis. Stabilization of charged intermediate (polymerases), increase acidity of another molecule (carbonic anhydrase), contribute to binding energy (NMP kinase) 4. Catalysis by approximation. Physical proximity of 2 substrates (NMP kinase)
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Chapter 9 Read Section 9.1, 9.4
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N O H R 1 R 2 + R2      NH3+ + H2O O O R 1 - N H O R 1 R 2 N H O R 1 R 2 Proteolysis is thermodynamically favored but slow Hydrolysis at pH 7 10-1000  years Hydrolysis facilitates recycling of amino acids and digestion of proteins from food in the gut C=N double bond is stable to hydrolysis Chymotrypsin cleaves c-terminal to  W, Y, F, & M Reactive serine provides  nucleophile to attack carbonyl DIPF deactivates the enzyme Only 1 of 28 serines modified!
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