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

Yasushi Tani; Keisuke Kimura; Hisaaki Mihara

doi:10.1080/09168451.2015.1104239

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 3.

Authors

Yasushi Tani^{1

2}, Keisuke Kimura¹, Hisaaki Mihara¹

Affiliations

¹ a Department of Biotechnology , College of Life Sciences, Ritsumeikan University , Kusatsu , Japan.
² b Ritsumeikan Global Innovation Research Organization , Ritsumeikan University , Kusatsu , Japan.

PMID: 26634770
DOI: 10.1080/09168451.2015.1104239

Abstract

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+).

Keywords: 4-methyl-5-hydroxyethylthiazole; Escherichia coli; ThiM; thiamin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Chromatography, Gel
Crystallography, X-Ray
Escherichia coli / enzymology*
Molecular Sequence Data
Phosphotransferases (Alcohol Group Acceptor) / chemistry
Phosphotransferases (Alcohol Group Acceptor) / isolation & purification*
Phosphotransferases (Alcohol Group Acceptor) / metabolism
Sequence Homology, Amino Acid

Substances

Phosphotransferases (Alcohol Group Acceptor)
hydroxyethylthiazole kinase