Impact of intra‐subunit domain–domain interactions on creatine kinase activity and stability
Impact of intra‐subunit domain–domain interactions on creatine kinase activity and stability
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DOI：
10.1016/j.febslet.2006.05.076
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发表时间：
2006-07
期刊：
影响因子：
3.5
通讯作者：
Tong-Jin Zhao;Shan Feng;Yong-liang Wang;Yang Liu;Xuechun Luo;Hai-Meng Zhou;Yong-Bin Yan
中科院分区：
文献类型：
--
作者：
Tong-Jin Zhao;Shan Feng;Yong-liang Wang;Yang Liu;Xuechun Luo;Hai-Meng Zhou;Yong-Bin Yan
Creatine kinase (CK) is a key enzyme in vertebrate excitable tissues. In this research, five conserved residues located on the intra-subunit domain–domain interface were mutated to explore their role in the activity and structural stability of CK. The mutations of Val72 and Gly73 decreased both the activity and stability of CK. The mutations of Cys74 and Val75, which had no significant effect on CK activity and structure, gradually decreased the stability and reactivation of CK. Our results suggested that the mutations might modify the correct positioning of the loop contributing to domain–domain interactions, and result in decreased stability against denaturation.
