L07 Chem 481 Lecture Notes - Lecture 33: Phosphotransferase, Glycogen Phosphorylase, Carbamoyl Phosphate Synthetase
13 Dec 2016
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Once r subunit binds camp, the interaction surface between c and r changes conformation (allosteric regulation: when c and r associated (at low camp concentrations), pka is inactive and the active site is blocked by r. With high [camp], it binds to r and conformational changes allow release of active. Insulin then active as a hormone, may dimerize or hexamerize: regulating digestive enzyme activity, zymogens of pancreatic proteases are activated by the first proteolytic cleavage, which. Completes the building of the substrate-binding pocket: pancreatic enzymes released as zymogens into small intestine then cleaved. Ex: trypsinogen first is cleaved by enteropeptidase (resident enzyme found in small numbers attached to endothelial membrane in small intestine) This cut is similar for most serine proteases for activation: subsequent removal of the segments shown in pink or black (14/15 and 147/148) yields. Rbc"s get trapped in the insoluble strands of a fibrin clot.
