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dc.contributor.authorStepanova, Rafaella-
dc.contributor.authorInagi, Hayato-
dc.contributor.authorSugawara, Kei-
dc.contributor.authorAsada, Kazuya-
dc.contributor.authorNishi, Tomoyuki-
dc.contributor.authorUeda, Daijiro-
dc.contributor.authorYasuno, Yoko-
dc.contributor.authorShinada, Tetsuro-
dc.contributor.authorMiki, Kunio-
dc.contributor.authorFujihashi, Masahiro-
dc.contributor.authorSato, Tsutomu-
dc.contributor.alternative稲木, 隼人-
dc.contributor.alternative菅原, 啓-
dc.contributor.alternative西, 智之-
dc.contributor.alternative上田, 大次郎-
dc.contributor.alternative保野, 陽子-
dc.contributor.alternative品田, 哲郎-
dc.contributor.alternative三木, 邦夫-
dc.contributor.alternative藤橋, 雅宏-
dc.contributor.alternative佐藤, 努-
dc.description.abstractTerpene synthases (TS) are classified into two broad types, Class I and II, based on the chemical strategy for initial carbocation formation and motif sequences of the catalytic site. We have recently identified a new class of enzymes, Class IB, showing the acceptability of long (C₂₀–C₃₅) prenyl-diphosphates as substrates and no amino acid sequence homology with known TS. Conversion of long prenyl-diphosphates such as heptaprenyl-diphosphate (C₃₅) is unusual and has never been reported for Class I and II enzymes. Therefore, the characterization of Class IB enzymes is crucial to understand the reaction mechanism of the extensive terpene synthesis. Here, we report the crystal structure bound with a substrate surrogate and biochemical analysis of a Class IB TS, using the enzyme from Bacillus alcalophilus (BalTS). The structure analysis revealed that the diphosphate part of the substrate is located around the two characteristic Asp-rich motifs, and the hydrophobic tail is accommodated in a unique hydrophobic long tunnel, where the C₃₅ prenyl-diphosphate, the longest substrate of BalTS, can be accepted. Biochemical analyses of BalTS showed that the enzymatic property, such as Mg^2⁺ dependency, is similar to those of Class I enzymes. In addition, a new cyclic terpene was identified from BalTS reaction products. Mutational analysis revealed that five of the six Asp residues in the Asp-rich motifs and two His residues are essential for the formation of the cyclic skeleton. These results provided a clue to consider the application of the unusual large terpene synthesis by Class IB enzymes.-
dc.publisherAmerican Chemical Society (ACS)-
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in 'ACS Chemical Biology', copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
dc.rightsThe full-text file will be made open to the public on 31 March 2021 in accordance with publisher's 'Terms and Conditions for Self-Archiving'-
dc.rightsThis is not the published version. Please cite only the published version. 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。-
dc.titleCharacterization of Class IB Terpene Synthase: The First Crystal Structure Bound with a Substrate Surrogate-
dc.type.niitypeJournal Article-
dc.identifier.jtitleACS Chemical Biology-
dc.identifier.kaken17H05439 / 19H04652 / 18H02145 / 19K22273 / 19H04648 / 19H04661-
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