3WEV

Crystal structure of the Schiff base intermediate of L-Lys epsilon-oxidase from Marinomonas mediterranea with L-Lys

3WEV の概要

• エントリーDOI: 10.2210/pdb3wev/pdb
• 関連するPDBエントリー: 3WEU
• 分子名称: L-lysine 6-oxidase, LYSINE, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: amino acid oxidase, arm, beta barrel, three be-ta sheets, amine oxidase, l-lys binding, oxidoreductase
• 由来する生物種: Marinomonas mediterranea
• 細胞内の位置: Secreted: F2JXJ3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 163564.08

構造登録者

Okazaki, S.,Nakano, S.,Matsui, D.,Akaji, S.,Inagaki, K.,Asano, Y. (登録日: 2013-07-12, 公開日: 2013-09-04, 最終更新日: 2023-11-08)

主引用文献

Okazaki, S.,Nakano, S.,Matsui, D.,Akaji, S.,Inagaki, K.,Asano, Y.
X-Ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in L-lysine {varepsilon}-oxidase from Marinomonas mediterranea
J.Biochem., 154:233-236, 2013

PubMed Abstract: We have determined the x-ray crystal structure of L-lysine ε-oxidase from Marinomonas mediterranea in its native and L-lysine-complex forms at 1.94- and 1.99-Å resolution, respectively. In the native enzyme, electron densities clearly indicate the presence of cysteine tryptophylquinone (CTQ) previously identified in quinohemoprotein amine dehydrogenase. In the L-lysine-complex, an electron density corresponding to the bound L-lysine shows that its ε-amino group is attached to the C6 carbonyl group of CTQ, suggesting the formation of a Schiff-base intermediate. Collectively, the present crystal structure provides the first example of an enzyme employing a tryptophylquinone cofactor in an amine oxidase.

PubMed: 23908359
DOI: 10.1093/jb/mvt070

実験手法

X-RAY DIFFRACTION (1.98 Å)