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.
复制标题
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
中科院分区:
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
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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期刊:
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影响因子:
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作者:
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通讯作者:
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影响因子:
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作者:
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通讯作者:
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影响因子:
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影响因子:
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通讯作者:
T. Suzuki;M. Kamidochi;N. Inoue;H. Kawamichi;Y. Yazawa;T. Furukohri;W. Ellington