Tovmasian E K, Hairapetian R L, Bykova E V, Severin S E, Haroutunian A V
Institute of Biochemistry, Academy of Sciences of Arm, SSR, Yerevan.
FEBS Lett. 1990 Jan 1;259(2):321-3. doi: 10.1016/0014-5793(90)80037-j.
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. Ca2+, phosphatidylserine-dependent phosphorylation decreases three-fold (from 0.6 to 0.2 mM) the Km value and does not affect Vmax. Protein kinase C-induced phosphorylation of AMP-deaminase, besides ADP-ribosylation, is suggested to be involved in regulating the AMP-deaminase activity in vivo.
