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Article

Mutation of the conserved G66 residue in GS region decreased structural stability and activity of arginine kinase.

International journal of biological macromolecules - 1 May 2018

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

Abstract excerpt

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...

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Identifiers

PMID: 29325742
DOI: 10.1016/j.ijbiomac.2018.01.039

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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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