Phosphorylation of the skeletal muscle AMP-deaminase by protein kinase C |
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| Authors: | E K Tovmasian R L Hairapetian E V Bykova S E Severin A V Haroutunian |
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| Institution: | Institute of Biochemistry, Academy of Sciences of Arm, SSR, Yerevan. |
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| Abstract: | 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. |
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