Inhibition of Transmethylations of Biogenic Amines by S-Adenosylhomocysteine
Journal of Biological ChemistryPublished 1 May 1971Open access
Takeo Deguchi, Jack D. Barchas
Citations242
SJR quartileQ1
SJR score1.71
SNIP1.00
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TL;DR
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-ADenosylHomocysteines.
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.
Keywords
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