1OAC

CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF ESCHERICHIA COLI AT 2 ANGSTROEMS RESOLUTION

1OAC の概要

• エントリーDOI: 10.2210/pdb1oac/pdb
• 分子名称: COPPER AMINE OXIDASE, COPPER (II) ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, copper, tpq, periplasmic
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P46883
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 163020.86

構造登録者

Parsons, M.R.,Convery, M.A.,Wilmot, C.M.,Phillips, S.E.V. (登録日: 1995-09-27, 公開日: 1996-04-03, 最終更新日: 2025-03-26)

主引用文献

Parsons, M.R.,Convery, M.A.,Wilmot, C.M.,Yadav, K.D.,Blakeley, V.,Corner, A.S.,Phillips, S.E.,McPherson, M.J.,Knowles, P.F.
Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
Structure, 3:1171-1184, 1995

PubMed Abstract: Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).

PubMed: 8591028
DOI: 10.1016/S0969-2126(01)00253-2

実験手法

X-RAY DIFFRACTION (2 Å)