1ng3

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{{STRUCTURE_1ng3| PDB=1ng3 | SCENE= }}
{{STRUCTURE_1ng3| PDB=1ng3 | SCENE= }}
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'''Complex of ThiO (glycine oxidase) with acetyl-glycine'''
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===Complex of ThiO (glycine oxidase) with acetyl-glycine===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 12627963 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12627963}}
==About this Structure==
==About this Structure==
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[[Category: Flavoprotein]]
[[Category: Flavoprotein]]
[[Category: Oxidase]]
[[Category: Oxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:47:56 2008''

Revision as of 10:48, 28 July 2008

Image:1ng3.png

Template:STRUCTURE 1ng3

Complex of ThiO (glycine oxidase) with acetyl-glycine

Template:ABSTRACT PUBMED 12627963

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

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