2UZ1

1.65 Angstrom structure of Benzaldehyde Lyase complexed with 2-methyl- 2,4-pentanediol

2UZ1 の概要

• エントリーDOI: 10.2210/pdb2uz1/pdb
• 関連するPDBエントリー: 2AG0 2AG1
• 分子名称: BENZALDEHYDE LYASE, THIAMINE DIPHOSPHATE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
• 機能のキーワード: thiamine diphosphate, thiamine pyrophosphate, lyase, benzoin, flavoprotein, benzaldehyde
• 由来する生物種: PSEUDOMONAS FLUORESCENS; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 237960.20

構造登録者

Maraite, A.,Schmidt, T.,Ansorge-Schumacher, M.B.,Brzozowski, A.M.,Grogan, G. (登録日: 2007-04-23, 公開日: 2007-07-24, 最終更新日: 2023-12-13)

主引用文献

Maraite, A.,Schmidt, T.,Ansorge-Schumacher, M.B.,Brzozowski, A.M.,Grogan, G.
Structure of the Thdp-Dependent Enzyme Benzaldehyde Lyase Refined to 1.65 A Resolution.
Acta Crystallogr.,Sect.F, 63:546-, 2007

PubMed Abstract: Benzaldehyde lyase (BAL; EC 4.1.2.38) is a thiamine diphosphate (ThDP) dependent enzyme that catalyses the enantioselective carboligation of two molecules of benzaldehyde to form (R)-benzoin. BAL has hence aroused interest for its potential in the industrial synthesis of optically active benzoins and derivatives. The structure of BAL was previously solved to a resolution of 2.6 A using MAD experiments on a selenomethionine derivative [Mosbacher et al. (2005), FEBS J. 272, 6067-6076]. In this communication of parallel studies, BAL was crystallized in an alternative space group (P2(1)2(1)2(1)) and its structure refined to a resolution of 1.65 A, allowing detailed observation of the water structure, active-site interactions with ThDP and also the electron density for the co-solvent 2-methyl-2,4-pentanediol (MPD) at hydrophobic patches of the enzyme surface.

PubMed: 17620706
DOI: 10.1107/S1744309107028576

実験手法

X-RAY DIFFRACTION (1.65 Å)