Abstract
S-Adenosylmethionine (AdoMet)-dependent methyltransferases have been shown to play important roles in the biosynthesis and/or degradation of small molecules, e.g. dopamine, norepinephrine, epinephrine, histamine, serotonin (Borchardt, 1980a), and in the modulation of the activity of macromolecules, e.g. proteins, nucleic acids, phospholipids (Borchardt, 1980b). A general feature of most AdoMet-dependent methyltransferases is the inhibition produced by S-adenosylhomocysteine (AdoHcy), a product of biological transmethylation. The product inhibition by AdoHcy appears to constitute part of a biological regulatory mechanism, the other component being AdoHcy hydrolase (EC.3.3.1.1), the enzyme that metabolizes AdoHcy in mammals (Cantoni et al., 1979).
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Borchardt, R.T., Patel, U.G., Bartel, R.L. (1982). Adenosine dialdehyde: A potent inhibitor of S-adenosylhomocysteine hydrolase. In: Biochemistry of S-Adenosylmethionine and Related Compounds. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06343-7_88
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DOI: https://doi.org/10.1007/978-1-349-06343-7_88
Publisher Name: Palgrave Macmillan, London
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Online ISBN: 978-1-349-06343-7
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