2009 Fiscal Year Final Research Report
Structural study of D-Ala-D-Ala ligase to develop new antibiotics
| Project/Area Number |
20790035
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Physical pharmacy
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| Research Institution | Hiroshima University |
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Principal Investigator |
MATOBA Yasuyuki Hiroshima University, 大学院・医歯薬学総合研究科, 准教授 (90363051)
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| Project Period (FY) |
2008 – 2009
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| Keywords | 構造生物 / 抗生物質 / 酵素 / ドラッグデザイン |
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| Research Abstract |
The aim of this study is to clarify the structural basis of D-cycloserine (DCS) resistance of DCS-resistant D-Ala-D-Ala ligase. From the amino acid sequence analysis, it was found that Tyr residue in the substrate-binding pocket, which is conserved among DCS-sensitive D-Ala-D-Ala ligases, is replaced by Phe residue in the DCS-resistant D-Ala-D-Ala ligase. In this study, it was proved that the Phe residue contributes to the DCS-resistance.
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Research Products
(13 results)
