Abstract:
:Shampoo ginger (Zingiber zerumbet Smith) has a high content and large variety of terpenoids in the essential oil of its rhizome. Here, we report on the isolation of a cDNA clone (ZSS1) encoding alpha-humulene synthase, a possible key enzyme of zerumbone biosynthesis. This clone contains an open reading frame of 1,644 bp and is predicted to encode a protein of 548 amino acids with a calculated molecular mass of 64.5 kDa. The deduced amino acid sequence shows 34-63% identity with known sesquiterpene synthases of other angiosperm species. Based on exon-intron organization, ZSS1 is classified as the terpene synthase-III (TPS-III) subfamily. When expressed in Escherichia coli, the recombinant enzyme catalyzed the formation of a major product, alpha-humulene (95%) and a minor by-product, beta-caryophyllene (5%). Introduction of ZSS1 and the foreign mevalonate pathway involved in FPP synthesis into E. coli results in in vivo production of alpha-humulene. Transcript of ZSS1 was detected almost exclusively in rhizomes and was up-regulated in both leaves and rhizomes after treatment with methyl jasmonate (MeJA), suggesting its ecological function in shampoo ginger.
journal_name
Plantajournal_title
Plantaauthors
Yu F,Okamto S,Nakasone K,Adachi K,Matsuda S,Harada H,Misawa N,Utsumi Rdoi
10.1007/s00425-008-0700-xsubject
Has Abstractpub_date
2008-05-01 00:00:00pages
1291-9issue
6eissn
0032-0935issn
1432-2048journal_volume
227pub_type
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