Ontology highlight
ABSTRACT:
SUBMITTER: Bragg J
PROVIDER: S-EPMC3347173 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
Bragg Jonathan J Rajkovic Andrei A Anderson Chance C Curtis Rachael R Van Houten Jason J Begres Brittany B Naples Colin C Snider Mark M Fraga Dean D Singer Mitchell M
Journal of bacteriology 20120302 10
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 bacterium Myxococcus xanthus. It is still unclear what role these proteins play in ba ...[more]