Artemisinin is a novel effective antimalarial drug extracted from the medicinal plant Artemisia annua L. Owing to the tight market and low yield of artemisinin, there is great interest in enhancing the production of artemisinin. In the present study, farnesyi diphosphate synthase （FPS） was overexpressed in high-yield A. annua to Increase the artemisinin content. The FPS activity in transgenic A. ennue was twoto threefold greater than that In non-transgenic A. annua. The highest artemisinin content in transgenic A. annua was approximately 0.9% （dry weight）, which was 34.4% higher than that in non-transgenic A. annua. The results demonstrate the regulatory role of FPS in artemisinin biosynthesis.
Jun-Li HanBen-Ye LiuHe-Chun YeHong WangZhen-Qlu LiGuo-Feng Li
A cDNA(af1) encoding farnesyl pyrophosphate synthase AaFPS1 (FPS, EC2.5.1.1/EC2.5.1.10) from a high yield Artemisia annua strain 025 has been cloned from its cDNA library. Sequence analysis showed that the cDNA en-coded a protein of 343 amino acid (aa) residues with mo-lecular weight of 39 kD. Deduced aa sequence of the cDNA was similar to FPS from other plants, yeast and mammals, containing 5 conserved domains found in both prenyl trans-ferase and polyprenyl synthase. The expression of the cDNA in Escherichia coli showed measurable specific activity of FPS in vitro. The enzyme was purified by ion exchange chromatography and its kinetics was measured. These re-sults would further promote the molecular regulation of ar-temisinin biosynthesis.
