Abstract
Farnesyl diphosphate synthase (FPS) catalyzes the biosynthesis of farnesyl diphosphate, a precursor for many important terpenoid products. A cDNA encoding FPS was first isolated from Allium sativum (AsFPS) using rapid amplification of cDNA ends (RACE) PCR. The sequence of AsFPS contains an open reading frame encoding a protein of 341 amino acids with a predicted molecular mass of 39.61 kDa. Alignment of AsFPS deduced amino acid revealed high identities with other plants ranging from 79% to 85% and showed 2-high conserved aspartate-rich motifs known to be important for FPS activity. Furthermore, AsFPS expression was stronger in the green organs such as bulbils, scapes, leaves, stems, but weaker in bulbs and roots than on-green organs of A. sativum.
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