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A Single Amino Acid Mutation Converts (R)-5-Diphosphomevalonate Decarboxylase into a Kinase
http://hdl.handle.net/2237/26599
http://hdl.handle.net/2237/26599ec4ca2f1-49a6-41ab-9b8a-2fe35d083ac2
名前 / ファイル | ライセンス | アクション |
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J_Biol_Chem-2017-Motoyama-2457-69.pdf ファイル公開:2018/02/10 (2.8 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2017-06-08 | |||||
タイトル | ||||||
タイトル | A Single Amino Acid Mutation Converts (R)-5-Diphosphomevalonate Decarboxylase into a Kinase | |||||
言語 | en | |||||
著者 |
Motoyama, Kento
× Motoyama, Kento× Unno, Hideaki× Hattori, Ai× Takaoka, Tomohiro× Ishikita, Hiroshi× Kawaide, Hiroshi× Yoshimura, Tohru× Hemmi, Hisashi |
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アクセス権 | ||||||
アクセス権 | open access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||
権利 | ||||||
言語 | en | |||||
権利情報 | This research was originally published in The Journal of Biological Chemistry. Kento Motoyama, Hideaki Unno, Ai Hattori, Tomohiro Takaoka, Hiroshi Ishikita, Hiroshi Kawaide, Tohru Yoshimura and Hisashi Hemmi. A Single Amino Acid Mutation Converts (R)-5-Diphosphomevalonate Decarboxylase into a Kinase. The Journal of Biological Chemistry. 2017; 292:pp.2457-pp.2469. © the American Society for Biochemistry and Molecular Biology. | |||||
抄録 | ||||||
内容記述 | The biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. In this reaction, a conserved aspartate residue has been proposed to be involved in the phosphorylation step as the general base catalyst that abstracts a proton from the 3-hydroxyl group. In this study, the catalytic mechanism of this rare type of decarboxylase is re-investigated by structural and mutagenic studies on the enzyme from a thermoacidophilic archaeon Sulfolobus solfataricus. The crystal structures of the archaeal enzyme in complex with (R)-5-diphosphomevalonate and adenosine 5′-O-(3-thio)triphosphate or with (R)-5-diphosphomevalonate and ADP are newly solved, and theoretical analysis based on the structure suggests the inability of proton abstraction by the conserved aspartate residue, Asp-281. Site-directed mutagenesis on Asp-281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step. These results enable discussion of the catalytic roles of the aspartate residue and provide clear proof of the involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme. | |||||
言語 | en | |||||
内容記述タイプ | Abstract | |||||
出版者 | ||||||
言語 | en | |||||
出版者 | American Society for Biochemistry and Molecular Biology | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプresource | http://purl.org/coar/resource_type/c_6501 | |||||
タイプ | journal article | |||||
出版タイプ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | https://doi.org/10.1074/jbc.M116.752535 | |||||
ISSN | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 0021-9258 | |||||
書誌情報 |
en : The Journal of Biological Chemistry 巻 292, p. 2457-2469, 発行日 2017-02-10 |
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著者版フラグ | ||||||
値 | publisher | |||||
URI | ||||||
識別子 | http://doi.org/10.1074/jbc.M116.752535 | |||||
識別子タイプ | DOI | |||||
URI | ||||||
識別子 | http://hdl.handle.net/2237/26599 | |||||
識別子タイプ | HDL |