Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis. Academic Article uri icon

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.

published proceedings

  • Biochemistry

author list (cited authors)

  • Settembre, E. C., Dorrestein, P. C., Park, J., Augustine, A. M., Begley, T. P., & Ealick, S. E.

citation count

  • 105

complete list of authors

  • Settembre, Ethan C||Dorrestein, Pieter C||Park, Joo-Heon||Augustine, Amy M||Begley, Tadhg P||Ealick, Steven E

publication date

  • March 2003