1NG4

Structure of ThiO (glycine oxidase) from Bacillus subtilis

1NG4 の概要

• エントリーDOI: 10.2210/pdb1ng4/pdb
• 関連するPDBエントリー: 1NG3
• 分子名称: Glycine oxidase, FLAVIN-ADENINE DINUCLEOTIDE, HYDROGEN PEROXIDE, ... (5 entities in total)
• 機能のキーワード: flavoprotein, oxidase, oxidoreductase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : O31616
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88833.16

構造登録者

Settembre, E.C.,Dorrestein, P.C.,Park, J.,Augustine, A.,Begley, T.P.,Ealick, S.E. (登録日: 2002-12-16, 公開日: 2003-04-08, 最終更新日: 2024-02-14)

主引用文献

Settembre, E.C.,Dorrestein, P.C.,Park, J.,Augustine, A.,Begley, T.P.,Ealick, S.E.
Structural and Mechanistic Studies on ThiO, a Glycine Oxidase Essential for Thiamin Biosynthesis in Bacillus subtilis
Biochemistry, 42:2971-2981, 2003

PubMed Abstract: The thiO gene of Bacillus subtilis encodes an FAD-dependent glycine oxidase. This enzyme is a homotetramer with a monomer molecular mass of 42 kDa. In this paper, we demonstrate that ThiO is required for the biosynthesis of the thiazole moiety of thiamin pyrophosphate and describe the structure of the enzyme with N-acetylglycine bound at the active site. The closest structural relatives of ThiO are sarcosine oxidase and d-amino acid oxidase. The ThiO structure, as well as the observation that N-cyclopropylglycine is a good substrate, supports a hydride transfer mechanism for the enzyme. A mechanistic proposal for the role of ThiO in thiazole biosynthesis is also described.

PubMed: 12627963
DOI: 10.1021/bi026916v

実験手法

X-RAY DIFFRACTION (2.3 Å)