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Biochim Biophys Acta. 2013 Jan;1832(1):204-15. doi: 10.1016/j.bbadis.2012.09.007. Epub 2012 Sep 24.

S-adenosyl-L-homocysteine hydrolase and methylation disorders: yeast as a model system.

Author information

1
Institute of Molecular Biosciences, University of Graz, Graz, Austria. oksana.tehlivets@uni-graz.at

Abstract

S-adenosyl-L-methionine (AdoMet)-dependent methylation is central to the regulation of many biological processes: more than 50 AdoMet-dependent methyltransferases methylate a broad spectrum of cellular compounds including nucleic acids, proteins and lipids. Common to all AdoMet-dependent methyltransferase reactions is the release of the strong product inhibitor S-adenosyl-L-homocysteine (AdoHcy), as a by-product of the reaction. S-adenosyl-L-homocysteine hydrolase is the only eukaryotic enzyme capable of reversible AdoHcy hydrolysis to adenosine and homocysteine and, thus, relief from AdoHcy inhibition. Impaired S-adenosyl-L-homocysteine hydrolase activity in humans results in AdoHcy accumulation and severe pathological consequences. Hyperhomocysteinemia, which is characterized by elevated levels of homocysteine in blood, also exhibits a similar phenotype of AdoHcy accumulation due to the reversal of the direction of the S-adenosyl-L-homocysteine hydrolase reaction. Inhibition of S-adenosyl-L-homocysteine hydrolase is also linked to antiviral effects. In this review the advantages of yeast as an experimental system to understand pathologies associated with AdoHcy accumulation will be discussed.

PMID:
23017368
PMCID:
PMC3787734
DOI:
10.1016/j.bbadis.2012.09.007
[Indexed for MEDLINE]
Free PMC Article
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