Mutation of the conserved G66 residue in GS region decreased structural stability and activity of arginine kinase.

Mutation of the conserved G66 residue in GS region decreased structural stability and activity of arginine kinase.
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GS 区域保守的 G66 残基的突变降低了精氨酸激酶的结构稳定性和活性。

DOI:
10.1016/j.ijbiomac.2018.01.039
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发表时间:
2018-05
影响因子:
8.2
通讯作者:
Xu Kai-Lin
Xu Kai-Lin
中科院分区:
化学1区
文献类型:
--
作者:
Wu Qing-Yun;Zhu Yuan-Yuan;Wei Fang;Tong Yu-Xue;Cao Jiang;Zhou Ping;Li Zhen-Yu;Zeng Ling-Yu;Li Feng;Wang Xiao-Yun;Xu Kai-Lin

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精氨酸激酶 (AK) 催化 ATP 对精氨酸进行可逆磷酸化,产生磷酸精氨酸。胍特异性 (GS) 区域的氨基酸残基在胍识别中发挥重要作用。然而,人们对 GS 区氨基酸残基 G66 在蛋白质折叠、活性和结构稳定性中的作用知之甚少。在本研究中,构建了一系列 G66 突变来研究其在 AK 结构稳定性和活性中的作用。我们的研究表明,这个保守位点的突变可能导致活性、构象变化和结构稳定性的明显丧失。光谱实验表明G66突变影响AK在折叠过程中从熔球中间体向天然状态的转变。本文提供的这些结果可能表明氨基酸残基G66可能在AK的活性和结构稳定性中发挥相对重要的作用。
Arginine kinase (AK) catalyzes the reversible phosphorylation of arginine by ATP, yielding the phosphoarginine. Amino acid residues in the guanidine specificity (GS) region play important roles in the guanidine-recognition. However, little is known about roles of amino acid residue G66 in the GS region in proteins folding, activity and structural stability. In this study, a series of G66 mutations were constructed to investigate its roles in AK's structural stability and activity. Our studies revealed that mutations in this conserved site could cause pronounced loss of activity, conformational changes and structural stability. Spectroscopic experiments indicate that G66 mutations influences AK transition from the molten globule intermediate to the native state in folding process. These results provided herein may suggest that amino acid residue G66 may play a relatively important role in AK's activity and structural stability.
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发表时间: 1989-12
期刊: European journal of biochemistry
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