Allosteric ACTion: the varied ACT domains regulating enzymes of amino-acid metabolism
Allosteric ACTion: the varied ACT domains regulating enzymes of amino-acid metabolism
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DOI：
10.1016/j.sbi.2014.10.007
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发表时间：
2014-12-01
影响因子：
6.8
通讯作者：
Parker, Emily J.
中科院分区：
文献类型：
--
作者：
Lang, Eric J. M.;Cross, Penelope J.;Parker, Emily J.
酶活性的别构调节在代谢中起着重要的作用。在这里，我们审查的变构酶的氨基酸代谢所赋予的离散域称为ACT域。这个60-70个残基的结构域具有β α β β α β拓扑结构，导致一个四链β（4）β（1）β（3）β（2）反平行片层，在一个面上具有两个反平行螺旋。广泛的序列变异需要组合的序列/结构/功能分析来鉴定ACT结构域。共同的特征包括ACT结构域的高度变化的自缔合模式、在结构域界面处的配体结合、以及通过构象变化和/或操纵四级平衡来传递变构信号。最近的一个例子说明了通过基因融合相对容易地采用这种多功能的变构模块。
Allosteric regulation of enzyme activity plays important metabolic roles. Here we review the allostery of enzymes of amino-acid metabolism conferred by a discrete domain known as the ACT domain. This domain of 60-70 residues has a beta alpha beta beta alpha beta topology leading to a four-stranded beta(4)beta(1)beta(3)beta(2) antiparallel sheet with two antiparallel helices on one face. Extensive sequence variation requires a combined sequence/ structure/function analysis for identification of the ACT domain. Common features include highly varied modes of self-association of ACT domains, ligand binding at domain interfaces, and transmittal of allosteric signals through conformational changes and/or the manipulation of quaternary equilibria. A recent example illustrates the relatively facile adoption of this versatile module of allostery by gene fusion.