EC Number   |
Reaction |
Reference |
|---|
    4.2.3.146 | geranylgeranyl diphosphate + H2O = cyclooctat-9-en-7-ol + diphosphate |
- |
- |
| 4.2.3.146 | geranylgeranyl diphosphate + H2O = cyclooctat-9-en-7-ol + diphosphate |
cyclization reaction mechanism analysis using three regiospecifically deuterated samples of geranylgeranyl diphosphate, the reaction proceeds via several cationic intermediates, detailed overview. Enzyme CotB2 catalyzes an unusually complex regiospecific and stereospecific cyclization that involves a unique carbon-carbon bond rearrangement and multiple hydride shifts, which all take place at a single active site |
-, 746744 |
| 4.2.3.146 | geranylgeranyl diphosphate + H2O = cyclooctat-9-en-7-ol + diphosphate |
proposed cyclization mechanism for CotB2. Bound to the enzyme, geranylgeranyl dithiophosphate (GGSPP) is folded into a unique S-shaped conformation in the active site pocket. GGSPP cannot undergo ionization and generate a reactive carbocation intermediate due to the C-S bond that links the thiodiphosphate moiety and the C20 chain. Therefore, the observed conformation of bound GGSPP is thought to represent the preionization state of the natural CotB2 substrate geranylgeranyl diphosphate |
-, 746593 |
