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Article

Impact of intra-subunit interactions on the dimeric arginine kinase activity and structural stability.

International journal of biological macromolecules - 1 Nov 2011

Wu Qing-Yun, Jin Kai-Zhou, Li Feng, Hu Zhi-Qian, Wang Xiao-Yun

Abstract excerpt

Arginine kinase (AK) catalyzes the reversible phosphorylation of arginine by ATP, yielding the phosphoarginine. In this research, six conserved residues located on the intra-subunit domain-domain interfaces were mutated to explore their roles in the activity and structural stability of dimer AK. The mutations D69A, E70A, E71A and F80A led to pronounced loss of AK activity and structural stability. Although the...

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Identifiers

PMID: 21839768
DOI: 10.1016/j.ijbiomac.2011.07.020

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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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