9TM7
Unspecific Peroxygenase from Daldinia childiae
9TM7 の概要
| エントリーDOI | 10.2210/pdb9tm7/pdb |
| 分子名称 | Unspecific Peroxygenase, MAGNESIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| 機能のキーワード | oxidoreductase, heme, unspecific peroxygenase |
| 由来する生物種 | Daldinia childiae |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 62484.05 |
| 構造登録者 | |
| 主引用文献 | McKenzie, A.,Clark, C.,Cornish, K.A.S.,Li, J.,Domenech, J.,Melling, B.,Ralston, M.P.H.,Cartwright, J.,Mulholland, N.P.,Unsworth, W.P.,Grogan, G. Structure, characterisation and application of an unspecific peroxygenase from Daldinia childiae. Rsc Chem Biol, 2026 Cited by PubMed Abstract: Unspecific peroxygenases (UPOs) have emerged as useful biocatalysts for the scalable and selective oxygenation of a large variety of organic molecules. UPOs have been divided into family I and family II enzymes, dependent upon sequence similarity and molecular weight, with family I being shorter in sequence. Here we report the characterisation and application of the family I UPO from (UPO). The enzyme was expressed in both and , yielding protein for kinetic and structural studies and biocatalytic application respectively. The structure of the enzyme revealed notable differences in the active site tunnel, compared with the well-studied family I artUPO, including F79 for V69 and F171 for I160. Notably, these differences were manifested in selectivity divergent from other UPOs when UPO was applied to preparative biotransformations; for example, (-)-menthol was converted exclusively into -6-hydroxymenthol in contrast to artUPO, which gave exclusively the tertiary alcohol 2,8-menthanediol. PubMed: 42328014DOI: 10.1039/d6cb00141f 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.88 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






