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- W1532382821 abstract "Abstract The supernatant fraction of brain homogenate stimulates partially purified phenylethanolamine N-methyltransferase, catechol methyltransferase, and acetylserotonin methyltransferase activities in vitro. The stimulating factor was purified, and the mechanism of stimulation was investigated. The results show that S-adenosylhomocysteine, a product from S-adenosylmethionine, is a potent inhibitor of these methyltransferases, and that the stimulating factor in brain is an enzyme which enhances transmethylations by hydrolyzing S-adenosylhomocysteine. The question is raised whether inhibition by S-adenosylhomocysteine or removal of inhibition by adenosylhomocysteinase might control transmethylations of biogenic amines." @default.
- W1532382821 created "2016-06-24" @default.
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- W1532382821 date "1971-05-01" @default.
- W1532382821 modified "2023-10-11" @default.
- W1532382821 title "Inhibition of Transmethylations of Biogenic Amines by S-Adenosylhomocysteine" @default.
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- W1532382821 doi "https://doi.org/10.1016/s0021-9258(18)62211-2" @default.
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