Inhibition of S-Adenosylmethionine-Dependent Transmethylation as an Approach to the Development of Antiviral Agents

  • Bradley T. Keller
  • Ronald T. Borchardt
Part of the NATO ASI Series book series (NSSA, volume 143)


The enzymatic transfer of methyl groups from S-adenosylmethionine (AdoMet) to an acceptor molecule, i.e. biological transmethylation, is widely recognized as a ubiquitous set of reactions involved in a diverse array of physiological processes (Usdin et al., 1982; Borchardt et al., 1986). In addition to their established role in the metabolism of a variety of small molecules such as histamine, catecholamines and phospholipids, it is now apparent that methylation of proteins and nucleic acids is equally significant as a mechanism for regulating the biochemical activity of these macromolecules. Regardless of the type of substrate, however, one of the most important and unifying features of virtually all AdoMet-dependent methyltransferases studied to date is that they follow a reaction scheme (Figure 1) which results in formation of the product, S-adenosylhomocysteine (AdoHcy). Owing to the fact that AdoHcy is a potent competitive inhibitor of these AdoMet-dependent methyltransferases, the rate of cellular methylation is regulated by the existing intracellular ratio of AdoHcy/AdoMet (Cantoni and Chiang, 1980; Chiang and Cantoni, 1979). Consequently, AdoHcy must be continuously degraded or eliminated in order to maintain some potential for methylation to proceed.


Antiviral Agent Adenosine Deaminase Newcastle Disease Viral mRNA Alcaligenes Faecalis 
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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Bradley T. Keller
    • 1
  • Ronald T. Borchardt
    • 1
  1. 1.Department of Pharmaceutical ChemistryUniversity of KansasLawrenceUSA

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