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S-adenosylhomocysteine hydrolase belongs to the adenosylhomocysteinase family. Additionally we are shipping AHCY Antibodies (116) and AHCY Kits (24) and many more products for this protein.
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Results uncover a H19 (show NCKAP1 Proteins)/SAHH circuit involving gene-methylation alterations by carcinogen BaP (show PHB2 Proteins).
We investigated previously assumed interaction with AHCY-like-1 protein (AHCYL1 (show AHCYL1 Proteins)), a paralog of AHCY. Indeed, significant interaction between both proteins exists. Additionally, silencing AHCYL1 (show AHCYL1 Proteins) leads to moderate inhibition of nuclear export of endogenous AHCY.
We have validated the vectors and confirmed self-association of AHCY, AHCYL1 (show AHCYL1 Proteins), and galectin-3 (show LGALS3 Proteins). In a high-throughput BiFC screen, we identified new AHCY interaction partners: galectin-3 (show LGALS3 Proteins) and PUS7L. We also describe additional steps in protein interaction analysis, applied for AHCY-galectin-3 (show LGALS3 Proteins) interaction
In order to enable the development of small molecule AHCY inhibitors as targeted cancer therapeutics we developed an assay based on a RapidFire high-throughput mass spectrometry detection system, which allows the direct measurement of AHCY enzymatic activity.
SAH (show ACSM3 Proteins) hydrolase deficiency can remain asymptomatic in childhood, and the disorder can be associated with early onset hepatocellular carcinoma.
H19 (show NCKAP1 Proteins) knockdown activates SAHH, leading to increased DNMT3B (show DNMT3B Proteins)-mediated methylation of an lncRNA-encoding gene Nctc1 within the Igf2-H19 (show NCKAP1 Proteins)-Nctc1 locus.
S-adenosylhomocysteine hydrolase is regulated by lysine acetylation
SAHH can promote apoptosis, inhibit migration and adhesion of ESCC cells suggesting that it may be involved in carcinogenesis of the esophagus.
A fluorescence-based assay for the measurement of S-adenosylhomocysteine hydrolase activity in biological samples.
Maintenance of ionizable active-site residues in catalytically suitable protonation states in closed forms of placental AHCY may be assisted by a water chain, stabilized by Asp182, that can import and export protons from and to the environment.
These results indicate that epigenetically mediated inhibition of Ahcy expression may be a driving force in causing SAH (show ACSM3 Proteins) elevation and subsequent downstream disturbances in transsulfuration and transmethylation pathways during the development and progression of nonalcoholic steatohepatitis.
Ahcy was identified from coupling of methylation with gene expression data, shed light on the underlying mechanisms of cytosine demethylation under methyl-deficient conditions.
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.
report that Myc (show MYC Proteins) promotes upregulation of S-adenosyl homocysteine hydrolase.
AHCYL1 (show AHCYL1 Proteins) has a different function from AHCY and plays an important role in embryogenesis by modulating inositol 1,4,5-trisphosphate receptor function for the intracellular calcium release
Hepatic steatosis and liver degeneration are prominent features of the ducttrip (dtp) mutant phenotype. Positional cloning identified a causative mutation in the gene encoding S-adenosylhomocysteine hydrolase (Ahcy).
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.
, S-adenosyl-L-homocysteine hydrolase
, S-adenosyl-L-homocysteine hydrolase B
, adenosylhomocysteinase B
, adoHcyase B
, liver copper-binding protein