EC Number   |
Reaction |
Reference |
|---|
   4.2.1.127 | (3S)-linalool = myrcene + H2O |
- |
- |
| 4.2.1.127 | (3S)-linalool = myrcene + H2O |
catalytic mechanism of enzyme LinD by a combined quantum mechanics and molecular mechanics (QM/MM), computational modeling |
748867 |
| 4.2.1.127 | (3S)-linalool = myrcene + H2O |
reaction mechanism via one acid-base mechanism via a carbocation intermediate. Residues C171, Y45 and D39 act as general acid and base for the protonation of the hydroxyl leaving group of the substrate (S)-linalool and the dehydration at the chiral carbon atom. Water is activated by H129 or C180 and added to the covalent or carbocation intermediate |
-, 747625 |
| 4.2.1.127 | (3S)-linalool = myrcene + H2O |
reaction mechanism, overview |
748734 |
| 4.2.1.127 | (3S)-linalool = myrcene + H2O |
the substrates are embedded inside a hydrophobic channel between two monomers of the (alpha,alpha)6 barrel fold class and flanked by three clusters of polar residues involved in acid-base catalysis. Catalytic mechanism, structure-function analysis, overview |
-, 747771 |
