S‐Adenosylmetliionine and methylation

  title={S‐Adenosylmetliionine and methylation},
  author={Petek K. Chiang and Richard K. Gordon and Jacov Tal and Guang Zeng and Bhupendra P. Doctor and Komanduri Pardhasaradhi and Peter P. McCann},
  journal={The FASEB Journal},
  pages={471 - 480}
S‐Adenosylmethionine (AdoMet or SAM) plays a pivotal role as a methyl donor in a myriad of biological and biochemical events. Although it has been claimed that AdoMet itself has therapeutic benefits, it remains to be established whether it can be taken up intact by cells. S‐Adeno‐ sylhomocysteine (AdoHcy), formed after donation of the methyl group of AdoMet to a methyl acceptor, is then hydrolyzed to adenosine and homocysteine by AdoHcy hydrolase. This enzyme has long been a target for… 

Biological effects of inhibitors of S-adenosylhomocysteine hydrolase.

  • P. Chiang
  • Biology, Chemistry
    Pharmacology & therapeutics
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Role of S-adenosylmethionine cycle in carcinogenesis.

The impact of disturbed SAM cycle on carcinogenesis is linked with molecular changes underlying the transformation of the cells that may underlay the carcinogenesis.

S-adenosylmethionine: nothing goes to waste.

Structural and functional studies of human methionine adenosyltransferases

High to atomic-resolution structures reveal the structural elements of the enzyme involved in the utilization of substrates, methionine and adenosine, and the formation of the product SAMe and suggest a unique mechanism of regulation and provide a gateway for structure-based drug design in anticancer therapies.

The Methyl Donor S-Adenosylmethionine Inhibits Active Demethylation of DNA

The data support an alternative mechanism of action for AdoMet as an inhibitor of intracellular demethylase activity, which results in hypermethylation of DNA.

Phosphoanalogues of amino acids involved in methionine metabolism as a new source of antiviral compounds

The search for specific inhibitors of Met(Ado) exchange and methionine metabolism remains to be a promising direction in the chemotherapy of viral infections.

Functional analysis of an S-adenosylhomocysteine hydrolase homolog of chestnut blight fungus.

It is demonstrated that SAHH is required for virulence and multiple traits of phenotype in C. parasitica, by regulation of the expression of genes involved in key process of the cell.


It is shown thatVanadate, an inhibitor of protein phosphatase, also inhibits cell pairing, and that the effects of vanadate and homocysteine are additive.



Methylation of atypical protein aspartyl residues during the stress response of HeLa cells

The results demonstrate that the PCMT is a constitutive component of cells whose function is required under normal conditions as well as during stress conditions, which accelerate structural damage to cellular proteins.

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Potential inhibitors of S-adenosylmethionine-dependent methyltransferases. 5. Role of the asymmetric sulfonium pole in the enzymatic binding of S-adenosyl-L-methionine.

The results suggest that the (+) enantiomer offers a nonproductive configuration for the methyl-transfer reaction itself; however, this configuration fails to hamper enzymatic binding.

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    The International journal of biochemistry
  • 1992

S‐adenosylmethionine levels in psychiatric and neurological disorders: a review

Intravenous or oral administration of SAMe thus represents a possible treatment for these neurological and metabolic disorders.

Sequence specificity of mRNA N6-adenosine methyltransferase.

Localization of six new N6-methyladenosine sites on Rous sarcoma virus (RSV) virion RNA has confirmed the extended consensus sequence for methylation: RGACU, where R is usually a G (7/12).

Catabolism and lability of S-adenosyl-L-methionine in rat liver extracts.

Excluding nonenzymic decomposition, more than 99% of adenosylmethionine is demethylated and exclusively catabolized further by S-adenosyl-L-homocysteine hydrolase, and less than 1% is decarboxylated and immediately utilized totally for polyamine biosynthesis.