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dc.contributor.authorDararat Mekkriengkraien_US
dc.contributor.authorTomoki Sandoen_US
dc.contributor.authorKazutake Hirookaen_US
dc.contributor.authorJitladda Sakdapipanichen_US
dc.contributor.authorYasuyuki Tanakaen_US
dc.contributor.authorEi Ichiro Fukusakien_US
dc.contributor.authorAkio Kobayashien_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherThe Institute of Science and Technology for Research and Development, Mahidol Universityen_US
dc.contributor.otherOsaka Universityen_US
dc.contributor.otherFukuyama Universityen_US
dc.identifier.citationBioscience, Biotechnology and Biochemistry. Vol.68, No.11 (2004), 2360-2368en_US
dc.description.abstractFarnesyl 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).en_US
dc.rightsMahidol Universityen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleCloning and characterization of farnesyl diphosphate synthase from the rubber-producing mushroom Lactarius chrysorrheusen_US
Appears in Collections:Scopus 2001-2005

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