Abstract
The biosynthesis of thiamin pyrophosphate in eukaryotes is different from the prokaryotic biosynthesis and is poorly understood to date. Only one thiazole biosynthetic gene has been identified (Thi4 in Saccharomyces cerevisiae). Here we report the identification and characterization of a Thi4-bound metabolite that consists of the ADP adduct of 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid. The unexpected structure of this compound yields the first insights into the mechanism of thiamin thiazole biosynthesis in eukaryotes.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Binding Sites
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Chromatography, High Pressure Liquid
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Eukaryotic Cells / metabolism*
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NAD / metabolism
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Protein Conformation
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Recombinant Fusion Proteins / biosynthesis*
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / metabolism*
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Thiamine / biosynthesis*
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Thiamine Pyrophosphate / metabolism
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Thiazoles / metabolism
Substances
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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THI4 protein, S cerevisiae
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Thiazoles
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NAD
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Thiamine Pyrophosphate
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Thiamine