Phosphatidylethanolamine methyltransferase activity in chick liver microsomes.
The synthesis of phosphatidylcholine from phosphatidylethanolamine is carried out by chick liver microsomes (Gallus domesticus). Different concentrations of PE, NPE and NNPE were used as exogenous substrates. Saturation of the S-adenosylmethionine has been found for the three different reactions with or without exogenous substrate. Kinetic parameters have been determined for this enzyme system in chick liver microsomes. The three methyl reactions had a similar pH profile with an optimum at pH = 8. Divalent ions such as Ca2+ or Mg2+ did not stimulate the enzyme activity. The results suggest that the synthesis of phosphatidylcholine from phosphatidylethanolamine by chick liver microsomes exhibits a kinetic pattern with different aspects than that described for other animal or human preparations.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002467:Cell Nucleus / Q000201:enzymology; D002645:Chickens; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008780:Methyltransferases / Q000378:metabolism*; D008862:Microsomes, Liver / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology; D050918:Phosphatidylethanolamine N-Methyltransferase
D008780:Methyltransferases; D050918:Phosphatidylethanolamine N-Methyltransferase; D008274:Magnesium; D002118:Calcium