Calcium activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide

Ca(super 2+) regulation of erythrocyte AMP deaminase [isoform E (AMPD3)] was studied by examining in vitro effects of calmodulin (CaM) on the enzyme and by monitoring the influence of CaM antagonists on purine catabolic flow in freshly prepared erythrocytes under various conditions of energy imbalance. The results suggested a protein-protein interaction between Ca(super 2+) -CaM and isoform E.