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Article

Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability.

FEBS letters - 10 Jul 2006

Zhao Tong-Jin, Feng Shan, Wang Yong-Liang, Liu Yang, Luo Xue-Chun, Zhou Hai-Meng, Yan Yong-Bin

Abstract excerpt

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...

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Identifiers

PMID: 16797013
DOI: 10.1016/j.febslet.2006.05.076

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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