大肠杆菌4-甲基-5-羟乙基噻唑激酶的纯化及性质
Purification and properties of 4-methyl-5-hydroxyethylthiazole kinase from Escherichia coli.
作者信息
Tani Yasushi, Kimura Keisuke, Mihara Hisaaki
机构信息
a Department of Biotechnology , College of Life Sciences, Ritsumeikan University , Kusatsu , Japan.
b Ritsumeikan Global Innovation Research Organization , Ritsumeikan University , Kusatsu , Japan.
出版信息
Biosci Biotechnol Biochem. 2016;80(3):514-7. doi: 10.1080/09168451.2015.1104239. Epub 2015 Dec 3.
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+).
4-甲基-5-羟乙基噻唑激酶（ThiM）作为硫胺素补救途径中的关键酶参与硫胺素的生物合成。我们从大肠杆菌中纯化并鉴定了ThiM。它对各种核苷酸具有广泛的底物特异性，并且相对于ATP更倾向于选择dATP作为磷酸供体。它被二价阳离子激活，对Co(2+)的反应比对Mg(2+)更强烈。
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