Abstract
S-Adenosylhomocysteine (AdoHcy), first isolated as one of the products of transmethylation reactions from S-adenosylmethionine (AdoMet) (Cantoni & Scarano, 1954) has been shown to be a competitive inhibitor of all methyltransferases. This was first shown by Gibson et al. (1961) for phosphatidylethanolamine methyltransferase and later extended to other methyltransferases (Borchardt, 1977). Of special interest is the fact that AdoHcy is a competitive inhibitor of most of the reactions in which AdoMet participates, both those where it serves as a methyl or an alkyl donor, and those where it functions as an allosteric effector.
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Cantoni, G.L. (1986). The Centrality of S-Adenosylhomocysteinase in the Regulation of the Biological Utilization of S-Adenosylmethionine. In: Borchardt, R.T., Creveling, C.R., Ueland, P.M. (eds) Biological Methylation and Drug Design. Experimental Biology and Medicine, vol 12. Humana Press. https://doi.org/10.1007/978-1-4612-5012-8_19
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DOI: https://doi.org/10.1007/978-1-4612-5012-8_19
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