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Evolution of Cooperativity in the Phosphagen Kinase Family
Author(s) -
McGinley Marisa Patryce,
Fraga Dean,
Snider Mark
Publication year - 2008
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.22.1_supplement.1004.3
Subject(s) - cooperativity , isothermal titration calorimetry , biochemistry , kinase , biology , arginine kinase , chemistry , enzyme , arginine , amino acid
The phosphagen kinases (PK) family of enzymes are widely distributed in various animal, protozoan, and bacterial taxa. They catalyze the reversible transfer of a phosphoryl group onto a guanidine acceptor and have an important role in cellular energy homeostasis. Two large groups dominate the PK family; arginine and creatine kinases. Arginine kinases (AK) are found in bacterial and invertebrate organisms and typically function as monomeric enzymes. Conversely, creatine kinases (CK) are found in some invertebrates and all vertebrates and are homodimeric enzymes. Recent studies have indicated that dimeric CKs may display cooperativity between subunits. This study investigated the nature of cooperativity in a broad range of species to better understand the possible evolution of this trait. Measurements of cooperativity using an isothermal titration calorimeter (ITC) have been completed on the dimeric AK found in the sea cucumber, Sticopus japonicus and indicate that this species displays cooperativity. Studies are currently underway comparing these results with any cooperativity seen in two protoflagellar CKs found in the sponge, ( Tethya aurantia ). These are thought to be at the base of the lineage leading to both the cytoplasmic and flagellar CKs and many allow us to hypothesize about the origin of this property. This project was funded by NSF‐RUI #0344432.