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dc.contributor.author | Sato-Masumoto, Naoko | en |
dc.contributor.author | Ito, Michiho | en |
dc.contributor.alternative | 佐藤(増本) , 直子 | ja |
dc.contributor.alternative | 伊藤, 美千穂 | ja |
dc.date.accessioned | 2014-06-03T00:41:51Z | - |
dc.date.available | 2014-06-03T00:41:51Z | - |
dc.date.issued | 2014-06 | - |
dc.identifier.issn | 0031-9422 | - |
dc.identifier.uri | http://hdl.handle.net/2433/187741 | - |
dc.description.abstract | Geraniol and linalool are acyclic monoterpenes found in plant essential oils that have attracted much attention for their commercial use and in pharmaceutical studies. They are synthesized from geranyl diphosphate (GDP) by geraniol and linalool synthases, respectively. Both synthases are very similar at the amino acid level and share the same substrate; however, the position of the GDP to which they introduce hydroxyl groups is different. In this study, the mechanisms underlying the regiospecific hydroxylation of geraniol and linalool synthases were investigated using a domain swapping approach and site-directed mutagenesis in perilla. Sequences of the synthases were divided into ten domains (domains I to IV-4), and each corresponding domain was exchanged between both enzymes. It was shown that different regions were important for the formation of geraniol and linalool, namely, domains IV-1 and -4 for geraniol, and domains III-b, III-d, and IV-4 for linalool. These results suggested that the conformation of carbocation intermediates and their electron localization were seemingly to be different between geraniol and linalool synthases. Further, five amino acids in domain IV-4 were apparently indispensable for the formation of geraniol and linalool. According to three-dimensional structural models of the synthases, these five residues seemed to be responsible for the different spatial arrangement of the amino acid at H524 in the case of geraniol synthase, while N526 is the corresponding residue in linalool synthase. These results suggested that the side-chains of these five amino acids, in combination with several relevant domains, localized the positive charge in the carbocation intermediate to determine the position of the introduced hydroxyl group. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Elsevier Ltd. | en |
dc.rights | © 2014 Elsevier Ltd. | en |
dc.rights | この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 | ja |
dc.rights | This is not the published version. Please cite only the published version. | en |
dc.subject | Perilla | en |
dc.subject | Labiatae | en |
dc.subject | Geraniol synthase | en |
dc.subject | Linalool synthase | en |
dc.subject | Domain swapping | en |
dc.subject | Site-directed mutagenesis | en |
dc.subject | Chimeric enzymes | en |
dc.subject | Regiospecific hydroxylation | en |
dc.subject | Essential oil | en |
dc.title | A domain swapping approach to elucidate differential regiospecific hydroxylation by geraniol and linalool synthases from perilla. | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.ncid | AA00774558 | - |
dc.identifier.jtitle | Phytochemistry | en |
dc.identifier.volume | 102 | - |
dc.identifier.spage | 46 | - |
dc.identifier.epage | 54 | - |
dc.relation.doi | 10.1016/j.phytochem.2014.03.020 | - |
dc.textversion | author | - |
dc.identifier.pmid | 24725978 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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