EC Number   |
Protein Variants |
Reference |
|---|
  4.2.3.61 | more |
construction of fusion proteins with farnesyl diphosphate synthase FPPS from Artemisia annua. The fusion enzymes produce epi-aristolochene from isopentenyl diphosphate through a coupled reaction. The Km values of FPPS and eAS for isopentenyl diphosphate and farnesyl diphosphate, respectively, are essentially the same for the single and fused enzymes. The bifunctional enzymes show a more efficient conversion of isopentenyl diphosphate to epi-aristolochene than the corresponding amount of single enzymes |
711891 |
| 4.2.3.61 | more |
engineering of a thermostable mutant by SCADS algorithm to suggest mutations based on side-chain interactions consistent with the nearby protein backbone, neighboring sidechains, and the local environment, and by replacement of solvent-exposed hydrophobic residues and the addition of salt bridges on the surface of the mutant enzyme. Contrary to wild-type, mutant is still active to 65°C but produces additional sesquiterpene products |
730893 |
| 4.2.3.61 | more |
heterologous expression of EAS in transgenic rice does not interfere with the activities of endogenous squalene synthase or farnesyl diphosphatase. The induction of EAS enzyme activity is accompanied by an increase in EAS mRNA when challenged by the elicitor. The EAS ectopic expression in transgenic rice plants results in the synthesis of 5-epi-aristolochene in vivo upon elicitor treatment |
713322 |
| 4.2.3.61 | Y520F |
3% of wild-type catalytic efficiency, reaction prooduct is germacrene A |
712234 |
