Abstract：
:Creatine kinase (CK) is a key enzyme for cellular energy metabolism, catalyzing the reversible phosphoryl transfer from phosphocreatine to ADP in vertebrates. CK contains a pair of highly conserved amino acids (H66 and D326) which might play an important role in sustaining the compact structure of CK by linking its N- and C- terminal domains; however the mechanism is still unclear. In this study, spectroscopic, structural modeling and protein folding experiments suggested that D326A, H66P and H66P/D326A mutations led to disruption of the hydrogen bond between those two amino acid residues and form the partially unfolded state which made it easier to be inactivated and unfolded under environmental stresses, and more prone to form insoluble aggregates. The formation of insoluble aggregates would decrease levels of active CKs which may provide clues in CK deficiency disease. Moreover, these results indicated that the degree of synergism had closely relationship to the conformational changes of CK. Thus, our results provided clues for understanding the mechanism of amino acid residues outside the active site in regulating substrate synergism.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Wu QY,Wei F,Zhu YY,Tong YX,Cao J,Zhou P,Li ZY,Zeng LY,Li F,Wang XY,Xu KLdoi
10.1016/j.ijbiomac.2017.09.020subject
Has Abstractpub_date
2018-02-01 00:00:00pages
512-520issue
Pt Aeissn
0141-8130issn
1879-0003pii
S0141-8130(17)32607-7journal_volume
107pub_type
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abstract：:This article has been withdrawn at the request of the author(s) and/or editor. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at http://www.elsevier.com/locate/withdrawalpolicy. ...
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