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PDBsum entry 1ng4
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Oxidoreductase
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PDB id
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1ng4
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural and mechanistic studies on thio, A glycine oxidase essential for thiamin biosynthesis in bacillus subtilis.
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Authors
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E.C.Settembre,
P.C.Dorrestein,
J.H.Park,
A.M.Augustine,
T.P.Begley,
S.E.Ealick.
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Ref.
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Biochemistry, 2003,
42,
2971-2981.
[DOI no: ]
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PubMed id
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Abstract
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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.
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