Trypsin is a digestive enzyme synthesized by the pancreas which acts as a serine protease. The mechanism by which this occurs involves the hydrolysis of peptide bonds using the chemical properties of Histidine, Aspartic Acid, and Serine, which are all polar amino acids. When these amino acids are combined in the trypsin actives-site, they form a catalytic triad, which is a charge relay that interacts with the serine active site and increases the nucleophilic interaction between the enzyme and substrate. This results in a thermodynamically favorable reaction, allowing the hydrolysis of the peptide bonds to occur. In order to initiate the attack, the His 57 group activates the serine group through base catalysis. This forms a tetrahedral intermediate which is immediately altered by acid catalysis of the NH2, resulting in a broken peptide bond within the substrate polypeptide. Once the peptide bond has been broken and the enzyme-substrate complex has been formed, a bond forms between the water molecule and the carbonyl group of the enzyme-substrate complex. Finally, one of the carbon-oxygen bond breaks and the enzyme is reproduced as a side product of the peptide hydrolysis.
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Structural highlights
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