1ng3
From Proteopedia
Complex of ThiO (glycine oxidase) with acetyl-glycine
Overview
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.
About this Structure
1NG3 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis., Settembre EC, Dorrestein PC, Park JH, Augustine AM, Begley TP, Ealick SE, Biochemistry. 2003 Mar 18;42(10):2971-81. PMID:12627963 Page seeded by OCA on Sat May 3 02:29:23 2008
