Abstract

Creatine kinase (CK), a key enzyme in maintaining the intracellular energetic homeostasis, contains two domains connected by a long linker. In this research,we found that the mutations of the conserved Asp122 in the linker slightly affected CK activity, structure and stability. The hydrogen bonding and the ion pair contributed 2-5 kJ/mol to the conformational stability of CK. Interestingly, the ability of CK reactivation from the denatured state was completely removed by the mutations. These results suggested that the electrostatic interactions were crucial to the action of the linker in CK reactivation. Study holds ProTherm entries: 25282, 25283, 25284, 25285, 25286, 25287, 25288, 25289, 25290, 25291, 25292, 25293 Extra Details: Creatine kinase reactivation; Linker; Electrostatic interactions

Submission Details

ID: YDQSuSPn

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:55 p.m.

Version: 1

Publication Details

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