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- W1666075882 abstract "Abstract The phospholipid N-methyltransferase system in microsomes of normal Neurospora crassa was compared with those in two choline-deficient mutant strains. The normal transferase system catalyzed the three transmethylations leading to the synthesis of lecithin, and the three phosphatide bases involved in this sequence of reactions were isolated as isotope-labeled products. The microsomes of a mutant, strain 34486, proved to have a subnormal phosphatidylethanolamine N-methyltransferase activity. The microsomes of a second mutant, strain 47904, could not catalyze the twostep conversion of phosphatidylmonomethylethanolamine to lecithin at a measurable rate and therefore were deficient in the phosphatidylmonomethylethanolamine N-methyltransferase found in the normal strain. Evidence was presented to corroborate the view based on previous studies that a single enzyme in N. crassa converts phosphatidylmonomethylethanolamine to lecithin." @default.
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- W1666075882 date "1967-01-01" @default.
- W1666075882 modified "2023-09-30" @default.
- W1666075882 title "Methylation of Ethanolamine Phosphatides by Microsomes from Normal and Mutant Strains of Neurospora crassa" @default.
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- W1666075882 doi "https://doi.org/10.1016/s0021-9258(19)81455-2" @default.
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