Purification and properties of 4-methyl-5-hydroxyethylthiazole kinase from Escherichia coli.

Biosci. Biotechnol. Biochem.2016;80(3):514-7. doi:10.1080/09168451.2015.1104239. Epub 2015 Dec 03

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摘要

4-Methyl-5-hydroxyethylthiazole kinase (ThiM) participates in thiamin biosynthesis as the key enzyme in its salvage pathway. We purified and characterized ThiM from Escherichia coli. It has broad substrate specificity toward various nucleotides and shows a preference for dATP as a phosphate donor over ATP. It is activated by divalent cations, and responds more strongly to Co(2+) than to Mg(2+).

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Purification and properties of 4-methyl-5-hydroxyethylthiazole kinase from Escherichia coli.

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