3NBB

Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha

3NBB の概要

• エントリーDOI: 10.2210/pdb3nbb/pdb
• 関連するPDBエントリー: 1A2V
• 分子名称: Peroxisomal primary amine oxidase, COPPER (II) ION (3 entities in total)
• 機能のキーワード: amine oxidase, quinoprotein, oxidoreductase
• 由来する生物種: Pichia angusta (yeast)
• 細胞内の位置: Peroxisome: P12807
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 466560.98

構造登録者

Chen, Z.,Datta, S.,DuBois, J.L.,Klinman, J.P.,Mathews, F.S. (登録日: 2010-06-03, 公開日: 2010-08-25, 最終更新日: 2023-11-22)

主引用文献

Chen, Z.W.,Datta, S.,Dubois, J.L.,Klinman, J.P.,Mathews, F.S.
Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.
Biochemistry, 49:7393-7402, 2010

PubMed Abstract: The copper amine oxidases carry out two copper-dependent processes: production of their own redox-active cofactor (2,4,5-trihydroxyphenylalanine quinone, TPQ) and the subsequent oxidative deamination of substrate amines. Because the same active site pocket must facilitate both reactions, individual active site residues may serve multiple roles. We have examined the roles of a strictly conserved active site tyrosine Y305 in the copper amine oxidase from Hansenula polymorpha kinetically, spetroscopically (Dubois and Klinman (2006) Biochemistry 45, 3178), and, in the present work, structurally. While the Y305A enzyme is almost identical to the wild type, a novel, highly oxygenated species replaces TPQ in the Y305F active sites. This new structure not only provides the first direct detection of peroxy intermediates in cofactor biogenesis but also indicates the critical control of oxidation chemistry that can be conferred by a single active site residue.

PubMed: 20684524
DOI: 10.1021/bi100643y

実験手法

X-RAY DIFFRACTION (2.05 Å)