Lec24 - Serine proteases Trypsin (cleaves after positively...

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Serine proteases Trypsin (cleaves after positively Chymotrypsin (bulky hydrophobic; Elastase (small neutral; Val, Ala, Gly)
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How do these enzymes work? We learn from --- Enzymology inhibitors kinetics Crystallography
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Inhibitors of Proteases Organic fluorophosphates (Ser) Tosyl chloromethylketones (His)
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Diisopropylphosphofluoridate (DIPF) Irreversibly inactivates chymotrypsin (and other family members) Modifies Ser 195 Suggests that Ser 195 is important for catalysis
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Inhibitors of Ser Proteases
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Tosyl-L-phenylalanine chloromethylketone Specific inhibitor of Chymotrypsin Forms a covalent bond with His 57 Suggests that His 57 is involved in catalysis
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DIPF is a nerve poison Inhibits esterases (catalytic mechanism similar to serine proteases) Acetylcholine esterase Block this enzyme interferes with nerve function
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X-Ray Structure of Trypsin Structure allowed researcher to carryout mutational studies to identify residues involved in catalysis
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This note was uploaded on 10/28/2010 for the course CHEM 114A taught by Professor Viadhiu during the Fall '08 term at UCSD.

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Lec24 - Serine proteases Trypsin (cleaves after positively...

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