Purification and properties of 4-methyl-5-hydroxyethylthiazole kinase from Escherichia coli
Purification and properties of 4-methyl-5-hydroxyethylthiazole kinase from Escherichia coli
复制标题
大肠杆菌4-甲基-5-羟乙基噻唑激酶的纯化及性质
DOI：
10.1080/09168451.2015.1104239
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
H.
中科院分区：
文献类型：
--
作者：
Tani;Y.;Kimura;K.;and Mihara;H.
4-甲基-5-羟乙基噻唑激酶（ThiM）是硫胺素生物合成途径中的关键酶。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，并显示出对dATP作为磷酸供体的偏好超过ATP。它被二价阳离子激活，对Co 2+的响应比对Mg 2+的响应更强。
4-Methyl-5-hydroxyethylthiazole kinase (ThiM) participates in thiamin biosynthesis as the key enzyme in its salvage pathway. We purified and characterized ThiM fromEscherichia 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 Co2+than to Mg2+.