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6JKO

Crystal structure of sulfoacetaldehyde reductase from Bifidobacterium kashiwanohense

6JKO の概要
エントリーDOI10.2210/pdb6jko/pdb
分子名称Methanol dehydrogenase, ZINC ION (3 entities in total)
機能のキーワードmiddle chain sulfoacetaldehyde reductase, nadh, oxidoreductase
由来する生物種Bifidobacterium kashiwanohense PV20-2
タンパク質・核酸の鎖数4
化学式量合計163811.50
構造登録者
Zhou, Y.,Xu, T.,Lin, L.,Zhang, Y.,Yuchi, Z. (登録日: 2019-03-01, 公開日: 2019-06-12, 最終更新日: 2023-11-22)
主引用文献Zhou, Y.,Wei, Y.,Nanjaraj Urs, A.N.,Lin, L.,Xu, T.,Hu, Y.,Ang, E.L.,Zhao, H.,Yuchi, Z.,Zhang, Y.
Identification and characterization of a new sulfoacetaldehyde reductase from the human gut bacteriumBifidobacterium kashiwanohense.
Biosci.Rep., 39:-, 2019
Cited by
PubMed Abstract: Hydroxyethylsulfonate (isethionate (Ise)) present in mammalian tissues is thought to be derived from aminoethylsulfonate (taurine), as a byproduct of taurine nitrogen assimilation by certain anaerobic bacteria inhabiting the taurine-rich mammalian gut. In previously studied pathways occurring in environmental bacteria, isethionate is generated by the enzyme sulfoacetaldehyde reductase IsfD, belonging to the short-chain dehydrogenase/reductase (SDR) family. An unrelated sulfoacetaldehyde reductase SarD, belonging to the metal-dependent alcohol dehydrogenase superfamily (M-ADH), was recently discovered in the human gut sulfite-reducing bacterium (SarD). Here we report the structural and biochemical characterization of a sulfoacetaldehyde reductase from the human gut fermenting bacterium (TauF). TauF belongs to the M-ADH family, but is distantly related to SarD (28% sequence identity). The crystal structures of TauF in the apo form and in a binary complex with NAD were determined at 1.9 and 3.0 Å resolution, respectively. Mutagenesis studies were carried out to investigate the involvement of active site residues in binding the sulfonate substrate. Our studies demonstrate the presence of sulfoacetaldehyde reductase in , with a possible role in isethionate production as a byproduct of taurine nitrogen assimilation.
PubMed: 31123167
DOI: 10.1042/BSR20190715
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 6jko
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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