EC Number   |
Reaction |
Reference  |
|---|
    3.1.1.3 | triacylglycerol + H2O = diacylglycerol + a carboxylate |
- |
- |
| 3.1.1.3 | triacylglycerol + H2O = diacylglycerol + a carboxylate |
Ser207 is an active site serine |
-, 650306 |
| 3.1.1.3 | triacylglycerol + H2O = diacylglycerol + a carboxylate |
enzyme contains the conserved pentapeptide Ala-Xaa-Ser-Xaa-Gly |
-, 650654 |
| 3.1.1.3 | triacylglycerol + H2O = diacylglycerol + a carboxylate |
enzyme form L3: catalytic triad is formed by conserved Ser, His and Asp residues |
650654 |
| 3.1.1.3 | triacylglycerol + H2O = diacylglycerol + a carboxylate |
Phe94 is involved in substrate binding and is responsible for accommodating the acyl chain length of the substrate |
650688 |
| 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 shows high enantioselectivity on racemic substrates |
-, 651025 |
| 3.1.1.3 | triacylglycerol + H2O = diacylglycerol + a carboxylate |
the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases |
651027 |
| 3.1.1.3 | triacylglycerol + H2O = diacylglycerol + a carboxylate |
the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases, enzyme contains the alpha-helical lid structure |
651027 |
| 3.1.1.3 | triacylglycerol + H2O = diacylglycerol + a carboxylate |
the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases, lipase contains no lid structure |
651027 |
