Generation of unnatural amino acids using enzymes for the biosynthesis of antitubercular antibiotic D-cycloserine
Project/Area Number |
15K07997
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Natural medicines
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Research Institution | Hiroshima University |
Principal Investigator |
Matoba Yasuyuki 広島大学, 医歯薬保健学研究科(薬), 准教授 (90363051)
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Project Period (FY) |
2015-04-01 – 2018-03-31
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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Keywords | 抗生物質 / 微生物薬品学 / 構造生物学 / 酵素 / 非天然型アミノ酸 / 光学分割 / ヘムタンパク質 / 共鳴ラマンスペクトル / X線結晶構造解析 / D-サイクロセリン / 変異体 |
Outline of Final Research Achievements |
Our group has recently cloned a gene cluster containing the biosynthetic genes for an antituberculosis antibiotic, D-cycloserine (D-CS) from D-CS-producing Streptomyces lavendulae. The aim of this study is to generate unnatural amino acids by using the enzymes in the D-CS-biosynthetic pathway. Based on the crystal structures of DcsD and DcsG, previously determined by us, mutational analyses were performed to identify the important residues for the catalytic activity and the substrate preference. In addition, crystal structure of DcsA was determined using the single anomalous dispersion method. Catalytic mechanism of DcsA was proposed based on the structural, mutational, and resonance Raman spectroscopic analyses.
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Report
(4 results)
Research Products
(22 results)
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[Journal Article] Activation mechanism of the Streptomyces tyrosinase assisted by the caddie protein2017
Author(s)
Matoba Y, Kihara S, Muraki Y, Bando N, Yoshitsu H, Kuroda T, Sakaguchi M, Kayama K, Tai H, Hirota S, Ogura T, Sugiyama M
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Journal Title
Biochemistry
Volume: 56
Issue: 41
Pages: 5593-5603
DOI
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Peer Reviewed
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[Presentation] Catalytic mechanism of a heme-binding arginine hydroxylase responsible for the biosynthesis of D-cycloserine2017
Author(s)
Shimotani N, Furukawa Y, Uda N, Kuroda T, Yanagisawa S, Ogura T, Mizohata E, Inoue T, Kamachi T, Yoshizawa K, Matoba Y
Organizer
第27回金属の関与する生体関連反応シンポジウム
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