title: Purification and properties of 4-methyl-5-hydroxyethylthiazole kinase from Escherichia coli.
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+).
authors.affiliation: a Department of Biotechnology , College of Life Sciences, Ritsumeikan University , Kusatsu , Japan.|b Ritsumeikan Global Innovation Research Organization , Ritsumeikan University , Kusatsu , Japan.
authors.forename: Yasushi
authors.initials: Y
authors.lastname: Tani
authors.affiliation: a Department of Biotechnology , College of Life Sciences, Ritsumeikan University , Kusatsu , Japan.
authors.forename: Keisuke
authors.initials: K
authors.lastname: Kimura
authors.affiliation: a Department of Biotechnology , College of Life Sciences, Ritsumeikan University , Kusatsu , Japan.
authors.forename: Hisaaki
authors.initials: H
authors.lastname: Mihara
mesh_terms: D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D008969:Molecular Sequence Data; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
chemical_list: D017853:Phosphotransferases (Alcohol Group Acceptor); C051254:hydroxyethylthiazole kinase
keywords: 4-methyl-5-hydroxyethylthiazole; Escherichia coli; ThiM; thiamin