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Article

The D14 and R138 ion pair is involved in dimeric arginine kinase activity, structural stability and folding.

International journal of biological macromolecules - 1 May 2014

Geng Hong-Li, Bian Mei-Ru, Liu Yang, Cao Jiang, Chen Chong, Wang Zhi-Yuan, Li Zhen-Yu, Zeng Ling-Yu, Wang Xiao-Yun, Wu Qing-Yun, Xu Kai-Lin

Abstract excerpt

Arginine kinase (AK) is a key enzyme in cellular energy metabolism of invertebrates. There are two conserved amino acid residues D14 and R138 in dimeric AK which form inter-subunit hydrogen bond. In Stichopus japonicus AK, mutations in these residues caused pronounced loss of activity, conformational changes and distinct substrate synergism alteration. Mutations (R138G, R138A and D14G) abolished D14 and R138...

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Source

Identifiers

PMID: 24582938
DOI: 10.1016/j.ijbiomac.2014.02.039

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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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