EC Number   |
General Information |
Reference |
|---|
   2.5.1.69 | evolution |
Artemisia tridentata chrysanthemyl diphosphate synthase is an example of an enzyme that has evolved recently from a highly specialized parent. The origins of farnesyl diphosphate synthase date back to the very beginning of cellular life, and the enzyme has perfected its ability to catalyze chain-elongation. In contrast, Artemisia tridentata chrysanthemyl diphosphate synthase has recently evolved from Artemisia tridentata diphosphate synthase, presumably by gene duplication and random mutagenesis but is still a promiscuous inefficient catalyst in comparison with farnesyl diphosphate synthase |
759401 |
| 2.5.1.69 | more |
enzyme structure comparisons, ligand binding structure analysis, residue H78 is essential for catalysis, modelling, overview |
737452 |
| 2.5.1.69 | more |
the enzyme structure is similar to that of the bacterial cis-prenyl synthase, undecaprenyl diphosphate synthase, and contains an allylic site (S1) in which dimethylallyl diphosphate ionizes and a second site (S2) which houses the dimethylallyl diphosphate nucleophile. Both S-thiolo-dimethylallyl diphosphate and S-thiolo-isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product, structure-based mechanism, overview |
737452 |
| 2.5.1.69 | physiological function |
geranyl diphosphate synthase small subunit SSU1 can modify the chain-length specificity of geranylgeranyl diphosphate synthase GGPPS, but has no effect on lavandulyl diphosphate synthase LPPS activity |
759970 |
| 2.5.1.69 | physiological function |
the enzyme catalyzes the formation of C10 mononterpene lavandulyl diphosphate, the precursor of the fragrances (R)-lavandulol and (R)-lavandulyl acetate |
737452 |
