Control of phosphatidylcholine synthesis and the regulatory role of choline kinase in rat liver. Evidence from essential-fatty acid-deficient rats.
Choline kinase and phosphocholine cytidylytransferase catalyse the rate-limiting steps of the cytidine pathway for the synthesis of phosphatidylcholine [Infante (1977) Biochem. J. 167, 847--849]. Essential-fatty acid deficiency induces a 3.5-fold increase in the specific activity of choline kinase, whereas the specific activity of the cytidylytransferase remains unchanged in rat liver. This change in specific activity accounts for the calculated increase in flux through the cytidine pathway produced in vivo by the same dietary state [Trewhella & Collins (1973 Biochim. Biophys. Acta 296, 34--50], thus confirming the fact that choline kinase has a regulatory role in the cytidine pathway for the synthesis of phosphatidylcholine.
D000818:Animals; D002797:Choline Kinase / Q000378:metabolism*; D003566:Cytidine Diphosphate Choline; D005228:Fatty Acids, Essential / Q000172:deficiency*; D008099:Liver / Q000201:enzymology*; D008297:Male; D009713:Nucleotidyltransferases / Q000378:metabolism; D010713:Phosphatidylcholines / Q000096:biosynthesis*; D010770:Phosphotransferases / Q000378:metabolism*; D051381:Rats
D005228:Fatty Acids, Essential; D010713:Phosphatidylcholines; D003566:Cytidine Diphosphate Choline; D010770:Phosphotransferases; D002797:Choline Kinase; D009713:Nucleotidyltransferases