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Exploring the Structural Basis for Negative Cooperativity in the Phosphagen Kinase Superfamily
Author(s) -
Kerwood Gentry,
Aryal Manish,
Van Houten Brittany,
Fraga Dean,
Snider Mark
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.724.12
Subject(s) - cooperativity , isothermal titration calorimetry , kinase , arginine kinase , biochemistry , creatine kinase , allosteric regulation , chemistry , enzyme , mutant , biology , arginine , amino acid , gene
Phosphagen kinases (PKs) are a family of enzymes that catalyze a reversible phosphoryl transfer from ATP to various guanidino compounds. While PK substrate specificity is currently well understood, far less is known about negative cooperativity in this family. Structural and comparative analyses have led us to a hypotheses regarding the structural basis for negative cooperativity in PKs. Previous assessment of negative cooperativity in P. sojae hypotaurocyamine kinase (HTK), O. cuniculus creatine kinase (CK), H. diversicolor glycocyamine kinase (GK), and M. brevicollis arginine kinase (AK) via isothermal titration calorimetry (ITC) provided some initial support for this hypothesis. Not only are we extending this comparative analysis, but we are also analyzing specific O. cuniculus CK mutants in an attempt to further validate this hypothesis. This research has been made possible by the Henry J. Copeland Fund.