| タイトル |
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Expression, purification, and crystallization of a plant polyketide cyclase from Cannabis sativa
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| 作成者 |
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| 主題 |
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Other
Cannabinoids
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Other
Cannabis sativa
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Other
Cyclase\Olivetolic acid
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| 内容注記 |
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application/pdf
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Abstract
Plant polyketides are a structurally diverse family of natural products. In the biosynthesis of plant polyketides, the construction of the carbocyclic scaffolds is a key step for diversifying the polyketide structure. Olivetolic acid cyclase (OAC) from Cannabis sativa L. is the only known plant polyketide cyclase that catalyzes the C2/C7 intramolecular aldol cyclization of linear pentyl tetra-β-ketide CoA to generate olivetolic acid in the biosynthesis of cannabinoid. The enzyme is also thought to belong to the dimeric α+β barrel (DABB) protein family. However, because of lack of the functional analysis of the other plant DABB proteins and low sequence identity with the functionally and structually characterized bacterial DABB proteins, the catalytic mechanism of OAC has remained unclear. To clarify the intimate catalytic mechanism of OAC, the enzyme was overexpressed in Escherichia coli and crystallized in a vapour-diffusion method. The crystals diffracted X-rays to 1.40 Å resolutions and belonged to space group P3121 or P3221, with unit-cell parameters a = b = 47.3 Å, c = 176.0 Å. Further crystallographic analysis will provide valuable insights into the structure–function relationship and catalytic mechanism of OAC.
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Article
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Acta Crystallogr F Struct Biol Commun, 2015 Dec; 71(Pt 12): 1470-4
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| 出版者 |
International Union of Crystallography
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| 日付 |
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| 言語 |
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| 資源タイプ |
journal article |
| 出版タイプ |
AM |
| 資源識別子 |
HDL
http://hdl.handle.net/10110/00018117
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URI
https://toyama.repo.nii.ac.jp/records/15653
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| 関連 |
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isVersionOf
DOI
https://doi.org/10.1107/S2053230X15020385
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| 収録誌情報 |
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NCID
AA12097708
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ISSN
17443091
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Acta Crystallographica Section F Structural Biology Communications
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巻71
号12
開始ページ1470
終了ページ1474
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| ファイル |
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| コンテンツ更新日時 |
2023-10-01 |