Chemical modification studies on arginine kinase: Essential cysteine and arginine residues at the active site
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,General Medicine,Biochemistry,Structural Biology
Reference27 articles.
1. Sequence homology and structure predictions of the creatine kinase isoenzymes
2. The use of arginine analogues for investigating the functional organization of the arginine-binding site in lobster muscle arginine kinase. Role of the ‘essential’ thiol group
3. Creatine kinase is modified by 2-chloromercuri-4-nitrophenol at the active site thiols with complete inactivation
4. Evidence for proximal cysteine and lysine residues at or near the ative site of arginine kinase of Stichopus japonicus
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1. Mutation of residue arginine 330 of arginine kinase results in the generation of the oxidized form more susceptible;International Journal of Biological Macromolecules;2013-03
2. Evidence that the amino acid residue Ile121 is involved in arginine kinase activity and structural stability;International Journal of Biological Macromolecules;2012-11
3. Thermodynamic analysis of ionizable groups involved in the catalytic mechanism of human matrix metalloproteinase 7 (MMP-7);Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2011-12
4. Impact of intra-subunit interactions on the dimeric arginine kinase activity and structural stability;International Journal of Biological Macromolecules;2011-11
5. Val65 plays an important role in the substrate synergism, structural stability and activity of arginine kinase;International Journal of Biological Macromolecules;2009-11
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