Protein kinase C catalyzes phosphorylation of the rat skeletal muscle AMP-deaminase in the presence of calcium ions and phosphatidylserine. At the same time, the catalytic subunit of CAMP-dependent protein kinase fails to phosphorylate AMP-deaminase. CaZ', phosphatidylserine-dependent phosphorylation decreases three-fold (from 0.6 to 0.2 mM) the K,,, value and does not affect V,.. Protein kinase C-induced phosphorylation of AMP-deaminase, besides ADP-ribosylation, is suggested to be involved in regulating the AMP-deaminasc activity in vivo.
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