S‐Adenosylmetliionine and methylation

@article{Chiang1996SAdenosylmetliionineAM,
  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},
  year={1996},
  volume={10},
  pages={471 - 480},
  url={https://api.semanticscholar.org/CorpusID:11214528}
}
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,…
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646 Citations
Highly Influential Citations
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646 Citations

Biological effects of inhibitors of S-adenosylhomocysteine hydrolase.

Altered S-AdenosylMethionine availability impacts dNTP pools in Saccharomyces cerevisiae.

It is shown that sam2∆/sam2∆ cells, previously characterized with lower levels of AdoMet and higher genome instability, have a higher level of each dNTP (except dTTP), contributing to a higher overall dNTP pool level when compared to wildtype.

S-adenosylhomocysteine hydrolase, S-adenosylmethionine, S-adenosylhomocysteine: correlations with ribavirin induced anemia.

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.

S-Adenosylmethionine: more than just a methyl donor

Recent advances in the discovery of novel SAM utilizing enzymes that rely on Lewis acid/base chemistry as opposed to radical mechanisms of catalysis are summarized.

S-adenosyl-l-methionine interaction signatures in methyltransferases

A comprehensive analysis of all available SAM-receptor crystal structures at atom, moiety and structure levels to gain deeper insights into the structure and function of SAM found that every interacting atom and its position is crucial in the methyl transfer phenomenon.

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.

The functional roles of S-adenosyl-methionine and S-adenosyl-homocysteine and their involvement in trisomy 21.

This review aims at providing an overview of the biological mechanisms which are altered in response to changes in the levels of SAM and SAH observed in DS.
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101 References

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.

S-adenosylmethionine decarboxylase as an enzyme target for therapy.

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.

The formation of internal 6-methyladenine residues in eucaryotic messenger RNA.

Modification of eukaryotic signaling proteins by C-terminal methylation reactions.

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.

Protein carboxyl methyltransferase selectively modifies an atypical form of calmodulin. Evidence for methylation at deamidated asparagine residues.

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).

Methylations of 70,000-Da heat shock proteins in 3T3 cells: alterations by arsenite treatment, by different stages of growth and by virus transformation.

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.
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