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Results uncover a H19/SAHH circuit involving gene-methylation alterations by carcinogen BaP.
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We investigated previously assumed interaction with AHCY-like-1 protein (AHCYL1), a paralog of AHCY. Indeed, significant interaction between both proteins exists. Additionally, silencing AHCYL1 leads to moderate inhibition of nuclear export of endogenous AHCY.
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We have validated the vectors and confirmed self-association of AHCY, AHCYL1, and galectin-3. In a high-throughput BiFC screen, we identified new AHCY interaction partners: galectin-3 and PUS7L. We also describe additional steps in protein interaction analysis, applied for AHCY-galectin-3 interaction
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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.
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SAH hydrolase deficiency can remain asymptomatic in childhood, and the disorder can be associated with early onset hepatocellular carcinoma.
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H19 knockdown activates SAHH, leading to increased DNMT3B-mediated methylation of an lncRNA-encoding gene Nctc1 within the Igf2-H19-Nctc1 locus.
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S-adenosylhomocysteine hydrolase is regulated by lysine acetylation
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SAHH can promote apoptosis, inhibit migration and adhesion of ESCC cells suggesting that it may be involved in carcinogenesis of the esophagus.
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A fluorescence-based assay for the measurement of S-adenosylhomocysteine hydrolase activity in biological samples.
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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.
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Five active site residues (E156, N181, K186, D190, N191) of AdoHcy hydrolase have been individually mutated to alanine and each engineered enzyme characterized with respect to its redox partial reaction and elimination/addition partial reaction.
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a discussion of its hydrolytic activity (review)
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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.
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AdoHcy is involved in adenosine-induced apoptosis by altering gene expression.
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R38W and G123R amino-acid exchanges did not bring about major changes to the catalytic rates. However, circular dichroism analysis showed that both polymorphisms effect the thermal stability.
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SAHH, which is diffuse in the cytoplasm of nonmotile Dictyostelium amoebae and human neutrophils, concentrates with F-actin in pseudopods at the front of motile, chemotaxing cells
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In the case of Hs-SAHH, the slow-binding phase terminates in micromolar affinity, but over a period of hours, the dissociation rate constant decreases until the final equilibrium affinity is in the nanomolar range.
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We found clinically relevant levels of Hcy (0-500 microM) induced elevation of SAH, declination of SAM and SAM/SAH ratio and reduced expression of SAHH and MBD2, but increased activity of DNMT3a and DNMT3b affecting DNA methylation
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The mechanism of action of copper on this enzyme sugges a regulative role for copper on the intracellular activity.
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consider changes in charge and the sterical incompatibility in mutant p.A89V protein as main reason for enzyme malfunction with AdoHcyase deficiency as consequence
