Trypsin is a digestive enzyme synthesized by the pancreas and secreted into the duodenum. Its purpose is to catalyze the peptide bonds, but with specificity for positively charged residues (lysine and arginine). It also activates hydrolytic enzymes and other enzymes in the pancreas. Its structure is very similar to chymotrypsin and elastase. Its substrate binding site (catalytic triad) contains two glycines and an aspartic acid. It is inactivated by tosyl-l-lysine chloromethylketone and also by enzymes trypsin activates itself.
Serine 195 attacks the scissile bond carbonyl. Ser 195 becomes nucleophilic by base attack from His 57. His 57 will stabilize as a base from aspartic acid and hydrogen bonding. The tetrahedral intermediate collapses back into a carbonyl.
Function
Disease
Relevance
Structural highlights
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