4H24
Cytochrome P450BM3-CIS cyclopropanation catalyst
4H24 の概要
| エントリーDOI | 10.2210/pdb4h24/pdb |
| 関連するPDBエントリー | 4H23 |
| 分子名称 | Cytochrome P450-BM3 variant P450BM3-Cis, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| 機能のキーワード | cytochrome p450, enzymatic cyclopropanation, directed evolution, non-natural function, oxidoreductase |
| 由来する生物種 | Bacillus megaterium |
| 細胞内の位置 | Cytoplasm (By similarity): P14779 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 217419.23 |
| 構造登録者 | Coelho, P.S.,Wang, Z.J.,Ener, M.E.,Baril, S.A.,Kannan, A.,Arnold, F.H.,Brustad, E.M. (登録日: 2012-09-11, 公開日: 2013-06-26, 最終更新日: 2023-09-20) |
| 主引用文献 | Coelho, P.S.,Wang, Z.J.,Ener, M.E.,Baril, S.A.,Kannan, A.,Arnold, F.H.,Brustad, E.M. A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo. Nat.Chem.Biol., 9:485-487, 2013 Cited by PubMed Abstract: Whole-cell catalysts for non-natural chemical reactions will open new routes to sustainable production of chemicals. We designed a cytochrome 'P411' with unique serine-heme ligation that catalyzes efficient and selective olefin cyclopropanation in intact Escherichia coli cells. The mutation C400S in cytochrome P450(BM3) gives a signature ferrous CO Soret peak at 411 nm, abolishes monooxygenation activity, raises the resting-state Fe(III)-to-Fe(II) reduction potential and substantially improves NAD(P)H-driven activity. PubMed: 23792734DOI: 10.1038/nchembio.1278 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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