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Adenosylhomocysteinase, S-adenosylhomocysteine hydrolase, S-adenosyl-L-homocysteine hydrolase
S-adenosylhomocysteine hydrolase belongs to the adenosylhomocysteinase family. It catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). Thus, it regulates the intracellular S-adenosylhomocysteine (SAH) concentration thought to be important for transmethylation reactions. Deficiency in this protein is one of the different causes of hypermethioninemia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2009] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, V1a, fibrillin-1
Papers on Adenosylhomocysteinase
Molecular insights into the function of the viral RNA silencing suppressor HCPro.
Mäkinen et al., Helsinki, Finland. In Plant J, Jan 2016
This approach led to identification of various HCPro interactors, including two key enzymes of the methionine cycle, S-adenosyl-l-methionine synthase and S-adenosyl-l-homocysteine hydrolase.
Inexpensive Method for Selecting Receptor Structures for Virtual Screening.
Wong et al., Saint Louis, United States. In J Chem Inf Model, Jan 2016
We evaluated the performance of the SPI by applying it to study eight protein systems: fatty acid binding protein adipocyte FABP4, serine/threonine-protein kinase BRAF, beta-1 adrenergic receptor ADRB1, TGF-beta receptor type I TGFR1, adenosylhomocysteinase SAHH, thyroid hormone receptor beta-1 THB, phospholipase A2 group IIA PA2GA, and cytochrome P450 3a4 CP3A4.
An enzyme captured in two conformational states: crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii.
Jaskolski et al., Poznań, Poland. In Acta Crystallogr D Biol Crystallogr, Jan 2016
S-Adenosyl-L-homocysteine hydrolase (SAHase) is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions.
Curious discoveries in antiviral drug development: the role of serendipity.
De Clercq, Leuven, Belgium. In Med Res Rev, Jul 2015
The S-adenosylhomocysteine hydrolase inhibitors (ix), while active against a broad range of (-)RNA viruses and poxviruses may be particularly effective against Ebola virus, and for (x) the O-ANP derivatives, the potential application range encompasses virtually all DNA viruses.
Structural insights into the reaction mechanism of S-adenosyl-L-homocysteine hydrolase.
Tanaka et al., Tokyo, Japan. In Sci Rep, 2014
S-adenosyl-L-homocysteine hydrolase (SAH hydrolase or SAHH) is a highly conserved enzyme that catalyses the reversible hydrolysis of SAH to L-homocysteine (HCY) and adenosine (ADO).
H19 lncRNA alters DNA methylation genome wide by regulating S-adenosylhomocysteine hydrolase.
Huang et al., New Haven, United States. In Nat Commun, 2014
Here we report that the developmentally regulated H19 lncRNA binds to and inhibits S-adenosylhomocysteine hydrolase (SAHH), the only mammalian enzyme capable of hydrolysing S-adenosylhomocysteine (SAH).
S-adenosyl-L-homocysteine hydrolase and methylation disorders: yeast as a model system.
Keller et al., Graz, Austria. In Biochim Biophys Acta, 2013
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.
[Structural biology for developing antimalarial compounds].
Nakamura et al., In Yakugaku Zasshi, 2012
One example is the structural studies for S-adenosyl-L-homocysteine hydrolase from Plasmodium falciparum (PfSAHH) and the other example is those for 1-deoxy-D-xylulose reductoisomerase from Plasmodium falciparum (PfDXR).
Link between allosteric signal transduction and functional dynamics in a multisubunit enzyme: S-adenosylhomocysteine hydrolase.
Hyeon et al., Seoul, South Korea. In J Am Chem Soc, 2012
The simulations of ligand-induced transition revealed that the signal of intrasubunit closure dynamics is transmitted to form intersubunit contacts, which in turn invoke a precise alignment of active site.
Epigenetic mechanisms in senescence, immortalisation and cancer.
Lleonart et al., Sevilla, Spain. In Biol Rev Camb Philos Soc, 2011
We and others have identified S-adenosylhomocysteine hydrolase in a high-throughput genetic screen focused on discovering novel genes whose inhibition induces immortalisation of primary cells.
Coupling global methylation and gene expression profiles reveal key pathophysiological events in liver injury induced by a methyl-deficient diet.
Pogribny et al., United States. In Mol Nutr Food Res, 2011
Ahcy was identified from coupling of methylation with gene expression data, shed light on the underlying mechanisms of cytosine demethylation under methyl-deficient conditions.
Crystallization of mouse S-adenosyl-L-homocysteine hydrolase.
Nakamura et al., Tokyo, Japan. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010
report the crystallization of mouse SAHH in the presence of the reaction product adenosine. The crystals diffracted to at least 1.55 A degrees resolution and are suitable for X-ray structure analysis at high resolution.
S-adenosyl homocysteine hydrolase is required for Myc-induced mRNA cap methylation, protein synthesis, and cell proliferation.
Cowling et al., Dundee, United Kingdom. In Mol Cell Biol, 2009
report that Myc promotes upregulation of S-adenosyl homocysteine hydrolase.
Human S-adenosylhomocysteine hydrolase: common gene sequence variation and functional genomic characterization.
Weinshilboum et al., Rochester, United States. In J Neurochem, 2009
S-adenosylhomocysteine hydrolase
Cladribine: not just another purine analogue?
Epner et al., Portland, United States. In Expert Opin Investig Drugs, 2009
Emerging data show that in addition to its known purine nucleoside analogue activity, cladribine possesses epigenetic properties, inhibiting S-adenosylhomocysteine hydrolase and DNA methylation.
16 Inhibition of mammalian protein methyltransferases by 5'-methylthioadenosine (MTA): A mechanism of action of dietary same?
Clarke, Los Angeles, United States. In Enzymes, 2005
It appears now that MTA is at best a poor direct inhibitor of methyltransferases and that its effectiveness in intact cells may depend on its ability to inhibit S-adenosyl-l-homocysteine hydrolase.
Adenosine-deaminase-deficient mice die perinatally and exhibit liver-cell degeneration, atelectasis and small intestinal cell death.
Valerio et al., Leiden, Netherlands. In Nat Genet, 1995
Adenine deoxyribonucleotides are only modestly elevated, whereas S-adenosylhomocysteine hydrolase activity is reduced more than 85%.
Treatment of adenosine deaminase deficiency with polyethylene glycol-modified adenosine deaminase.
Kobayashi et al., In N Engl J Med, 1987
The activity of S-adenosylhomocysteine hydrolase, which is inactivated by deoxyadenosine, increased to normal in red cells and nucleated marrow cells.
The human genes for S-adenosylhomocysteine hydrolase and adenosine deaminase are syntenic on chromosome 20.
Francke et al., In Science, 1982
Human-Chinese hamster cell hybrids and a monoclonal antibody to human S-adenosylhomocysteine hydrolase were used to identify chromosome 20 as the location of the human gene for this enzyme.
S-adenosylhomocysteine hydrolase is an adenosine-binding protein: a target for adenosine toxicity.
Krodich et al., In Science, 1978
Such a protein was identified in extracts of human lymphoblasts and placenta as the enzyme S-adenosylhomocysteine hydrolase.
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