Settembre Ethan C, Dorrestein Pieter C, Park Joo-Heon, Augustine Amy M, Begley Tadhg P, Ealick Steven E
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.
Biochemistry. 2003 Mar 18;42(10):2971-81. doi: 10.1021/bi026916v.
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.
枯草芽孢杆菌的thiO基因编码一种依赖黄素腺嘌呤二核苷酸(FAD)的甘氨酸氧化酶。这种酶是一种同四聚体,单体分子量为42 kDa。在本文中,我们证明硫胺素焦磷酸噻唑部分的生物合成需要ThiO,并描述了活性位点结合N - 乙酰甘氨酸的该酶结构。ThiO最接近的结构同源物是肌氨酸氧化酶和D - 氨基酸氧化酶。ThiO的结构以及N - 环丙基甘氨酸是良好底物这一观察结果支持了该酶的氢化物转移机制。还描述了ThiO在噻唑生物合成中作用的机制推测。