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Phosphorylation of the skeletal muscle AMP‐deaminase by protein kinase C
Author(s) -
Tovmasian E.K.,
Hairapetian R.L.,
Bykova E.V.,
Severin S.E.,
Haroutunian A.V.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80037-j
Subject(s) - amp deaminase , protein kinase a , phosphorylation , skeletal muscle , cyclin dependent kinase 2 , chemistry , biochemistry , phosphatidylserine , protein phosphorylation , mitogen activated protein kinase kinase , biology , microbiology and biotechnology , adenosine deaminase , enzyme , endocrinology , phospholipid , membrane
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. Ca 2+ phosphatidylserine‐dependent phosphorylation decreases three‐fold (from 0.6 to 0.2 mM) the K m value and does not affect V max Protein kinase C‐induced phosphorylation of AMP‐deaminase, besides ADP‐ribosylation, is suggested to be involved in regulating the AMP‐deaminase activity in vivo.