Structural Insights into the Function of the Thiamin Biosynthetic Enzyme Thi4 from Saccharomyces cerevisiae
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- 作者：Christopher T. Jurgenson ; Abhishek Chatterjee ; Tadhg P. Begley ; Steven E. Ealick
- 刊名：Biochemistry
- 出版年：2006
- 出版时间：September 19, 2006
- 年：2006
- 卷：45
- 期：37
- 页码：11061 - 11070
- 全文大小：1218K
- 年卷期：v.45,no.37(September 19, 2006)
- ISSN：1520-4995
文摘
The structure of thiazole synthase (Thi4) from Saccharomyces cerevisiae was determined to1.8 Å resolution. Thi4 exists as an octamer with two monomers in the asymmetric unit. The structurereveals the presence of a tightly bound adenosine diphospho-5-(
-ethyl)-4-methylthiazole-2-carboxylicacid at the active site. The isolation of this reaction product identifies NAD as the most likely precursorand provides the first mechanistic insights into the biosynthesis of the thiamin thiazole in eukaryotes.Additionally, the Thi4 structure reveals the first protein structure with a GR2 domain that binds NADinstead of FAD, raising interesting questions about how this protein evolved from a flavoenzyme to aNAD binding enzyme.
-ethyl)-4-methylthiazole-2-carboxylicacid at the active site. The isolation of this reaction product identifies NAD as the most likely precursorand provides the first mechanistic insights into the biosynthesis of the thiamin thiazole in eukaryotes.Additionally, the Thi4 structure reveals the first protein structure with a GR2 domain that binds NADinstead of FAD, raising interesting questions about how this protein evolved from a flavoenzyme to aNAD binding enzyme.