3WFI

The crystal structure of D-mandelate dehydrogenase

3WFI の概要

• エントリーDOI: 10.2210/pdb3wfi/pdb
• 関連するPDBエントリー: 3WFJ
• 分子名称: 2-dehydropantoate 2-reductase (2 entities in total)
• 機能のキーワード: rosmann fold, dehydrogenase, nadh binding, oxidoreductase
• 由来する生物種: Enterococcus faecium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68744.97

構造登録者

Miyanaga, A.,Fujisawa, S.,Furukawa, N.,Arai, K.,Nakajima, M.,Taguchi, H. (登録日: 2013-07-19, 公開日: 2014-07-23, 最終更新日: 2023-11-08)

主引用文献

Miyanaga, A.,Fujisawa, S.,Furukawa, N.,Arai, K.,Nakajima, M.,Taguchi, H.
The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase.
Biochem.Biophys.Res.Commun., 439:109-114, 2013

PubMed Abstract: D-Mandelate dehydrogenases (D-ManDHs), belonging to a new d-2-hydroxyacid dehydrogenase family, catalyze the conversion between benzoylformate and d-mandelate using NAD as a coenzyme. We determined the first D-ManDH structure, that of ManDH2 from Enterococcus faecalis IAM10071. The overall structure showed ManDH2 has a similar fold to 2-ketopantoate reductase (KPR), which catalyzes the conversion of 2-ketopantoate to d-pantoate using NADP as a coenzyme. They share conserved catalytic residues, indicating ManDH2 has the same reaction mechanism as KPR. However, ManDH2 exhibits significant structural variations in the coenzyme and substrate binding sites compared to KPR. These structural observations could explain their different coenzyme and substrate specificities.

PubMed: 23954635
DOI: 10.1016/j.bbrc.2013.08.019

実験手法

X-RAY DIFFRACTION (1.997 Å)