Publication: Cloning and characterization of farnesyl diphosphate synthase from the rubber-producing mushroom Lactarius chrysorrheus
Issued Date
2004-11-01
Resource Type
ISSN
09168451
Other identifier(s)
2-s2.0-11144255773
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Mahidol University
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SCOPUS
Bibliographic Citation
Bioscience, Biotechnology and Biochemistry. Vol.68, No.11 (2004), 2360-2368
Suggested Citation
Dararat Mekkriengkrai, Tomoki Sando, Kazutake Hirooka, Jitladda Sakdapipanich, Yasuyuki Tanaka, Ei Ichiro Fukusaki, Akio Kobayashi Cloning and characterization of farnesyl diphosphate synthase from the rubber-producing mushroom Lactarius chrysorrheus. Bioscience, Biotechnology and Biochemistry. Vol.68, No.11 (2004), 2360-2368. doi:10.1271/bbb.68.2360 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/21135
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Title
Cloning and characterization of farnesyl diphosphate synthase from the rubber-producing mushroom Lactarius chrysorrheus
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).