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Article

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

Biochemistry - 18 Mar 2003

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

Abstract excerpt

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...

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PMID: 12627963
DOI: 10.1021/bi026916v

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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