9EIS
Ethylene forming enzyme in complex with manganese and 2-oxoglutarate from Penicillium digitatum
9EIS の概要
| エントリーDOI | 10.2210/pdb9eis/pdb |
| 分子名称 | 2-oxoglutarate-dependent ethylene/succinate-forming enzyme, 2-OXOGLUTARIC ACID, MANGANESE (II) ION, ... (6 entities in total) |
| 機能のキーワード | 2-oxoglutarate-dependent ethylene/succinate-forming enzyme, oxidoreductase |
| 由来する生物種 | Penicillium digitatum Pd1 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 183872.17 |
| 構造登録者 | Chatterjee, S.,Rankin, J.A.,Farrugia, M.A.,Hu, J.,Hausinger, R.P. (登録日: 2024-11-26, 公開日: 2025-04-02, 最終更新日: 2025-05-14) |
| 主引用文献 | Chatterjee, S.,Rankin, J.A.,Farrugia, M.A.,J S Rifayee, S.B.,Christov, C.Z.,Hu, J.,Hausinger, R.P. Biochemical, Structural, and Conformational Characterization of a Fungal Ethylene-Forming Enzyme. Biochemistry, 64:2054-2067, 2025 Cited by PubMed Abstract: The ethylene-forming enzyme (EFE) from the fungus strain Pd1 was heterologously produced in and its properties were compared to the extensively characterized bacterial enzyme from strain PK2. Both enzymes catalyze four reactions: the conversion of 2-oxoglutarate (2OG) to ethylene and CO, oxidative decarboxylation of 2OG coupled to l-arginine (l-Arg) hydroxylation, uncoupled oxidative decarboxylation of 2OG, and the production of 3-hydroxypropionate (3-HP) from 2OG. The strain Pd1 enzyme exhibited a greater ratio of ethylene production over l-Arg hydroxylation than the PK2 strain EFE. The uncoupled decarboxylation of 2OG and 3-HP production are minor reactions in both cases, but they occur to a greater extent using the fungal enzyme. Additional distinctions of the fungal versus bacterial enzyme are noted in the absorbance maxima and l-Arg dependence of their anaerobic electronic spectra. The structures of the Pd1 EFE apoprotein and the EFE·Mn(II)·2OG complex resembled the corresponding structures of the PK2 enzyme, but notable structural differences were observed in the computationally predicted Pd1 EFE·Fe(II)·2OG·l-Arg complex versus the PK2 EFE·Mn(II)·2OG·l-Arg crystal structure. These studies extend our biochemical understanding and represent the first structural and conformational characterization of a eukaryotic EFE. PubMed: 40052306DOI: 10.1021/acs.biochem.5c00038 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






