Premium
Phosphorylation of pig brain diacylglycerol kinase by endogenous protein kinase
Author(s) -
Kanoh Hideo,
Ono Teruo
Publication year - 1986
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(86)80577-4
Subject(s) - autophosphorylation , diacylglycerol kinase , mitogen activated protein kinase kinase , cyclin dependent kinase 2 , protein kinase c , biochemistry , map2k7 , protein kinase a , phosphorylation , cyclin dependent kinase 9 , kinase , map kinase kinase kinase , chemistry , biology , microbiology and biotechnology
Pig brain diacylglycerol kinase did not catalyze autophosphorylation. However, the kinase was phosphorylated on serine, when immunoprecipitated from the partially purified enzyme preparation preincubated with Mg 2+ and [γ‐ 32 P]ATP. The action of the endogenous protein kinase phosphorylating diacylglycerol kinase was independent of cyclic nucleotides and Ca 2+ , and became maximum at pH 5.5. Although the extent of enzyme phosphorylation was limited (maximally about 0.25 mol P i incorporated per mol kinase), the results show that diacylglycerol kinase can be a phosphoprotein.