EC Number   |
Reaction |
Reference |
|---|
    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 |
