3D2D

Structure of berberine bridge enzyme in complex with (S)-reticuline

3D2D の概要

• エントリーDOI: 10.2210/pdb3d2d/pdb
• 関連するPDBエントリー: 3D2H 3D2J
• 分子名称: berberine bridge-forming enzyme, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: bi-covalent flavinylation, n-glycosylation, substrate complex, alakloid biosynthesis, oxidoreductase
• 由来する生物種: Eschscholzia californica (California poppy)
• 細胞内の位置: Cytoplasmic vesicle: P30986
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62456.10

構造登録者

Winkler, A.,Lyskowski, A.,Macheroux, P.,Gruber, K. (登録日: 2008-05-08, 公開日: 2008-10-28, 最終更新日: 2024-11-06)

主引用文献

Winkler, A.,Lyskowski, A.,Riedl, S.,Puhl, M.,Kutchan, T.M.,Macheroux, P.,Gruber, K.
A concerted mechanism for berberine bridge enzyme
Nat.Chem.Biol., 4:739-741, 2008

PubMed Abstract: Berberine bridge enzyme catalyzes the conversion of (S)-reticuline to (S)-scoulerine by formation of a carbon-carbon bond between the N-methyl group and the phenolic ring. We elucidated the structure of berberine bridge enzyme from Eschscholzia californica and determined the kinetic rates for three active site protein variants. Here we propose a catalytic mechanism combining base-catalyzed proton abstraction with concerted carbon-carbon coupling accompanied by hydride transfer from the N-methyl group to the N5 atom of the FAD cofactor.

PubMed: 18953357
DOI: 10.1038/nchembio.123

実験手法

X-RAY DIFFRACTION (2.796 Å)