Abstract
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.
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