Cloning and analysis of a cDNA encoding farnesyl diphosphate synthase from Artemisia annua

A cDNA encoding farnesyl diphosphate (FPP) synthase (FPPS) has been cloned from a cDNA library of Artemisia annua. The sequence analysis showed that the cDNA encoded a protein of 343 amino acid (aa) residues with a calculated molecular weight of 39 420 kDa. The deduced aa sequence of the cDNA was hi...

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Veröffentlicht in:	Gene 1996-06, Vol.172 (2), p.207-209
Hauptverfasser:	Matsushita, Yasuhiko, Kang, Wonkyung, Charlwood, Barry V.
Format:	Artikel
Sprache:	eng
Schlagworte:	alkyl (aryl) transferases Alkyl and Aryl Transferases Amino Acid Sequence amino acid sequences Artemisia annua Artemisinin Base Sequence cloned gene expression Cloning, Molecular complementary DNA DNA, Complementary enzyme activity Escherichia coli FPP synthase genbank/u36376 gene expression gene transfer genetic transformation Geranyltranstransferase isoprenoid biosynthesis medicinal plant Molecular Sequence Data nucleotide sequences Plants, Medicinal - enzymology Plants, Medicinal - genetics sesquiterpenoid Transferases - genetics Transferases - metabolism
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Beschreibung
Zusammenfassung:	A cDNA encoding farnesyl diphosphate (FPP) synthase (FPPS) has been cloned from a cDNA library of Artemisia annua. The sequence analysis showed that the cDNA encoded a protein of 343 amino acid (aa) residues with a calculated molecular weight of 39 420 kDa. The deduced aa sequence of the cDNA was highly similar to FPPS from other plants, yeast and mammals, and contained the two conserved domains found in polyprenyl synthases including FPPS, geranylgeranyl diphosphate synthases and hexaprenyl diphosphate synthases. The expression of the cDNA in Escherichia coli showed enzyme activity for FPPS in vitro.
ISSN:	0378-1119 1879-0038
DOI:	10.1016/0378-1119(96)00054-6