Article
Identification and characterization of a putative arginine kinase homolog from Myxococcus xanthus required for fruiting body formation and cell differentiation.
Journal of bacteriology - 1 May 2012
Bragg Jonathan, Rajkovic Andrei, Anderson Chance, Curtis Rachael, Van Houten Jason, Begres Brittany, Naples Colin, Snider Mark, Fraga Dean, Singer Mitchell
Abstract excerpt
Arginine kinases catalyze the reversible transfer of a high-energy phosphoryl group from ATP to l-arginine to form phosphoarginine, which is used as an energy buffer in insects, crustaceans, and some unicellular organisms. It plays an analogous role to that of phosphocreatine in vertebrates. Recently, putative arginine kinases were identified in several bacterial species, including the social Gram-negative soil...
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