Please use this identifier to cite or link to this item:
|Title:||Cloning and characterization of farnesyl diphosphate synthase from the rubber-producing mushroom Lactarius chrysorrheus|
Ei Ichiro Fukusaki
The Institute of Science and Technology for Research and Development, Mahidol University
|Keywords:||Biochemistry, Genetics and Molecular Biology;Chemistry;Immunology and Microbiology|
|Citation:||Bioscience, Biotechnology and Biochemistry. Vol.68, No.11 (2004), 2360-2368|
|Abstract:||Farnesyl diphosphate is involved in rubber biosynthesis as an initiating substrate for both polyprenol and mushroom rubber. So far, we have isolated the cDNA of a farnesyl diphosphate synthase (FPS) for the first time from a rare rubber-producing mushroom, Lactarius chrysorrheus, by the degenerate RT-PCR technique based on sequence information of FPS genes from fungi and yeasts. The open reading frame was clarified to encode a protein of 381 amino acid residues with a calculated molecular weight of 42.9 kDa. The deduced amino acid sequence of L. chrysorrheus FPS showed about 50% identity with those of other fungi and yeasts as well as plants. We expressed the cDNA of L. chrysorrheus FPS in Escherichia coli as a glutathione-S-transferase (GST)-fusion protein. The purified obtained protein showed FPS activity in which geranyl diphosphate (GPP) served as primary substrate, with a 2.4-fold higher kcat/Kmvalue for GPP than for dimethylallyl diphosphate (DMAPP).|
|Appears in Collections:||Scopus 2001-2005|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.