BCH210H1 Lecture Notes - Lecture 6: Common Bile Duct, Centroacinar Cell, N-Terminus
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BCH210H1 Full Course Notes
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We will explore enzyme mechanisms with specific reference to the enzyme. In earlier enzyme lectures we surveyed number of diff enzymes and noticed feature of active site, regulation etc and today we will look at one enzyme that carefully and appreciate both its origin and its structure. Exactly just how catalysis work at its active site. The mechanism is of great importance as it critically illustrates how nezymes fascilitates and speeds up reaction. Chymotripson is a protease or proteolitic enzyme that attacks dietary proteins in small intestines. Thus hydrolysis peptide bonds and generates products that have new carboxyl and new amino terminus. The enzyme is first made in an inactive form called chymotrpsinogen. Remember the relationship btw trypsin and trypsinogen as we discussed earlier where trypsin is the active form of trypsinogen. Chymotripson is first made in acinar cells of the pancreas. The enzyme initially assembled using amino acids in ribosomes attached to the er.
