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Article

Val65 plays an important role in the substrate synergism, structural stability and activity of arginine kinase.

International journal of biological macromolecules - 1 Nov 2009

Wu Qing-Yun, Li Feng, Wang Xiao-Yun

Abstract excerpt

Arginine kinase, a member of phosphagen kinase, is a key enzyme in the cellular energy metabolism of invertebrates. A series mutation of conserved amino acid residue V65 was constructed to investigate its role in AK substrate synergism, structural stability and activity. Our study revealed that mutation in this conserved site could cause pronounced loss of activity, conformational changes and distinct substrate...

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Identifiers

PMID: 19628004
DOI: 10.1016/j.ijbiomac.2009.06.016

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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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