Biochemistry. How active sites communicate in thiamine enzymes.
Biochemistry. How active sites communicate in thiamine enzymes.
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生物化学。
DOI：
10.1126/science.1105457
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
Jordan,Frank
中科院分区：
文献类型：
--
作者：
Jordan,Frank
819种在细菌中发现更复杂α2β2四聚体（Frank等人在他们的研究中使用），第三种是在哺乳动物细胞中发现的具有激酶/磷酸酶活性的非常复杂的α2β2四聚体。在这个四聚体中，激酶对E1亚基的磷酸化关闭了酶的活性，而随后的磷酸酶作用（去除磷酸基团）又重新开启了活性。
819 more complex α2β2 tetramer found in bacteria (that Frank et al. use in their study), and the third is a very complex α2β2 tetramer with kinase/phosphatase activity that is found in mammalian cells. In this tetramer, phosphorylation of the E1 subunit by the kinase switches off enzyme activity, whereas subsequent phosphatase action, which removes the phosphate groups, switches back on the activity.