2017 Fiscal Year Final Research Report
Structural analysis and functional modification of unusual amino acid-forming enzyme, and the application to peptide engineering
| Project/Area Number |
26292040
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Kyushu University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
神田 大輔 九州大学, 生体防御医学研究所, 教授 (80186618)
善藤 威史 九州大学, (連合)農学研究科(研究院), 助教 (50380556)
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| Project Period (FY) |
2014-04-01 – 2018-03-31
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| Keywords | ランチビオティック / 異常アミノ酸 / Nukacin ISK-1 / 翻訳後修飾 / 標的分子 / 細胞壁前駆体lipid II / 核磁気共鳴（NMR）解析 / X線結晶構造解析 |
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| Outline of Final Research Achievements |
The structure of nukacin ISK-1 was found to have two states chemically exchanged by solution NMR. The exchange rate kex was about 1.5 s-1. The high abundance ratio had high affinity to the cell wall peptidoglycan precursor lipid II. The NMR-based model of nukacine ISK-1 in a complex with lipid II indicated that the hydrophobic amino acid side chain in the Ring C region of nukacin ISK-1 participates in binding to the lipid II fat chain region, and the region near Ring A participates in binding with the phosphate group of lipid II. By attaching the leader peptide of the precursor peptide of nukacin ISK-1, the unusual amino acid-forming enzyme NukM also recognized other peptides as a substrate.
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| Free Research Field |
農芸化学・応用微生物学
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