KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0055 | - |
(2E,6E)-farnesyl diphosphate | pH 7.0, 30°C | Solidago canadensis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Solidago canadensis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
48000 | - |
gel filtration | Solidago canadensis |
60000 | - |
1 * 60000, SDS-PAGE | Solidago canadensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Solidago canadensis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Solidago canadensis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
49.9 | - |
pH 7.0, 30°C | Solidago canadensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesyl diphosphate | initial step is the formation of a germacrenyl cation after abstraction of the diphosphate group. Internal shifts of electron pairs lead to the patchoulenyl cation, which then undergoes a double 1,2-hydride shift. Rearrangement leads to the aromadendrenyl cation, which then undergoes a 1,2-hydride shift. Abstraction of a proton by the enzyme yields isoledene, which is reprotonated at the active site of the enzyme. At this junction two proton abstractions are possible, one leading to (-)-alpha-gurjunene and the other to (+)-gamma-gurjunene | Solidago canadensis | (-)-alpha-gurjunene + diphosphate | product ratio 91% (-)-alpha-gurjunene and 9% (+)-gamma-gurjunene | ? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 60000, SDS-PAGE | Solidago canadensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
presence of Mg2+ | Solidago canadensis |