3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	-	-	
3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	a tryptophan residue plays an important role in maintaining the ative conformation of the enzyme	653693	
3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	activation mechanism	664561	
3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	activation of the pancreatic lipase is a mechanism allowing accessibility of the active site to the substrate and resulting in the unmasking of the catalytic triad of the enzyme induced by the motion of the flap	679795	
3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	active site structure, reaction mechanism	664561	
3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	activity required deprotonation of the catalytic His residue	664060	
3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	activity required deprotonation of the catalytic His188 residue, model of electrostatics in the active site, the active site is essentially covered with lipod surface during catalysis	664060	
3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	catalytic serine residue, deeply buried under a domain called the extrusion domain, which is composed of a cap and a lid segmentof 58 amino acids, catalytic reaction mechanism	650899	
3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	enzyme contains an active site serine	-, 653738	
3.1.1.3	triacylglycerol + H2O = diacylglycerol + a carboxylate	enzyme contains the conserved pentapeptide Ala-Xaa-Ser-Xaa-Gly	-, 650654