A rat brain cytosolic N-methyltransferase(s) activity converting phosphorylethanolamine into phosphorylcholine.
It had been previously speculated upon but never proved that the methylation of phosphorylethanolamine could contribute to the production of choline containing compounds. However, experimental evidence obtained with neuronal cultures was interpreted as showing that the stepwise methylation of phosphobases may be an important route for this biosynthesis. We demonstrate that cytosolic fraction from rat brain possesses a N-methyltransferase activity capable of methylating phosphorylethanolamine and its mono- and dimethyl-derivatives into phosphorylcholine. The level of activity detectable in rat liver cytosol is only 18% of that found in the brain cytosol.
University of Manitoba, Department of Biochemistry, Winnipeg, Canada.
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C
Andriamampandry
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R
Massarelli
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L
Freysz
J N
JN
Kanfer
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002458:Cell Fractionation; D002794:Choline / Q000031:analogs & derivatives*; D003600:Cytosol / Q000201:enzymology; D004983:Ethanolamines / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008780:Methyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D010767:Phosphorylcholine / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012436:S-Adenosylmethionine / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology
D004983:Ethanolamines; D010767:Phosphorylcholine; C005448:phosphorylethanolamine; D012436:S-Adenosylmethionine; D008780:Methyltransferases; D002794:Choline