title: Activation of partially purified rat liver lipid methyltransferase by phosphorylation.
abstract: Incubation of partially purified rat liver lipid methyltransferase with MgATP and the catalytic subunit of the cyclic AMP dependent protein kinase results in up to 4-fold activation of the methylation reaction. When (gamma-32p) MgATP is included in the assay mixture, the analysis of the phosphoprotein products by electrophoresis shows the incorporation of 32p into a single protein band of about 50K and pI 4.75. It is concluded that rat liver lipid methyltransferase can be converted from a low activity dephosphorylated form to a high activity phosphorylated form.
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D004789:Enzyme Activation; D047908:Intracellular Signaling Peptides and Proteins; D007700:Kinetics; D008745:Methylation; D008780:Methyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D008862:Microsomes, Liver / Q000201:enzymology*; D008970:Molecular Weight; D050918:Phosphatidylethanolamine N-Methyltransferase; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
chemical_list: D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; C015482:protein kinase modulator; D000255:Adenosine Triphosphate; D008780:Methyltransferases; D050918:Phosphatidylethanolamine N-Methyltransferase; D011494:Protein Kinases