Both native conformers of rabbit muscle adenylate kinase are active
Both native conformers of rabbit muscle adenylate kinase are active
复制标题
DOI：
10.1016/s0014-5793(00)01947-5
复制
发表时间：
2000-09
期刊：
影响因子：
3.5
通讯作者：
X. Li;X. Pan
中科院分区：
文献类型：
--
作者：
X. Li;X. Pan
在平衡溶液中，8-苯基-1-萘磺酸(ANS)结合性质不同的兔肌腺苷酸激酶(AK)有两种形式。一种形式(约70%，表示为N1)与ANS快速结合，而另一种形式(约30%，表示为N1)不能与ANS快速结合。此外，天然形式的AK应该采用不同的构象与底物和产物结合，这些构象应该是预先存在的，以发挥其催化功能。目前的实验证明ANS探针区分的两种形式的AK都是活跃的。N2的活性约为N1的0.8倍，对胰酶具有较高的敏感性。这意味着AK的天然状态可能是动力学上可获得的构象的集合，AK折叠的能量景观应该具有不止一个局部最小值。
There are two forms of rabbit muscle adenylate kinase (AK) with different 8-anilino-1-naphthalenesulfonic acid (ANS) binding properties in equilibrium solution. One form (about 70%, denoted N1) binds rapidly with ANS, whereas the other (about 30%, denoted N2) does not. Furthermore, native forms of AK should adopt different conformations for binding with substrates and products, which should be pre-existing for performing its catalytic function. The present experiments demonstrate both forms of AK distinguished by ANS probe are active. The activity of N2is about 0.8 fold higher than N1and shows higher susceptibility to proteolysis by trypsin. This means that the native state of AK might be an ensemble of kinetically attainable conformers and the energy landscapes of AK folding should be rugged with more than one local minimum.