ArticleThe Journal of biological chemistry2014
Regulation of S-adenosylhomocysteine hydrolase by lysine acetylation.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Review
- Keeping Wavering Bonds: Deactivation-Induced Signaling by Reactive Electrophiles.Biochemistry · 2026Review
- AHCY: A metabolic gatekeeper at the interface of methylation, redox balance, and cellular stress response.The Journal of biological chemistry · 2026Review
- The AHCY-adenosine complex rewires mRNA methylation to enhance fatty acid biosynthesis and tumorigenesis.Cell research · 2026Article
- Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism.International journal of molecular sciences · 2025Review
- Ultrasound-targeted microbubble technology facilitates SAHH gene delivery to treat diabetic cardiomyopathy by activating AMPK pathway.iScience · 2024Article
- Emerging roles of dysregulated adenosine homeostasis in brain disorders with a specific focus on neurodegenerative diseases.Journal of biomedical science · 2021Review
- Ketogenesis impact on liver metabolism revealed by proteomics of lysine β-hydroxybutyrylation.Cell reports · 2021Article
- Functional and Pathological Roles of AHCY.Frontiers in cell and developmental biology · 2021Review
- The Chemical Biology of Reversible Lysine Post-translational Modifications.Cell chemical biology · 2020Review
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Analysis of the uterine lumen in fertility-classified heifers: II. Proteins and metabolites†.Biology of reproduction · 2020Article
- DJ-1 suppresses ferroptosis through preserving the activity of S-adenosyl homocysteine hydrolase.Nature communications · 2020Article
- Metabolite and gene expression profiles suggest a putative mechanism through which high dietary carbohydrates reduce the content of hepatic betaine in Megalobrama amblycephala.Metabolomics : Official journal of the Metabolomic Society · 2018Article
- Benzoxaborole treatment perturbs S-adenosyl-L-methionine metabolism in Trypanosoma brucei.PLoS neglected tropical diseases · 2018Article
- Article
- A molecular engineering toolbox for the structural biologist.Quarterly reviews of biophysics · 2017Review
- Label-free LC-MS/MS shotgun proteomics to investigate the anti-inflammatory effect of rCC16.Molecular medicine reports · 2016Article
- Empirical power laws for the radii of gyration of protein oligomers.Acta crystallographica. Section D, Structural biology · 2016Article
- Acetylation of C/EBPα inhibits its granulopoietic function.Nature communications · 2016Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
S-Adenosylhomocysteine hydrolase (SAHH) is an NAD(+)-dependent tetrameric enzyme that catalyzes the breakdown of S-adenosylhomocysteine to adenosine and homocysteine and is important in cell growth and the regulation of gene expression. Loss of SAHH function can result in global inhibition of cellular methyltransferase enzymes because of high levels of S-adenosylhomocysteine. Prior proteomics studies have identified two SAHH acetylation sites at Lys(401) and Lys(408) but the impact of these post-translational modifications has not yet been determined. Here we use expressed protein ligation to produce semisynthetic SAHH acetylated at Lys(401) and Lys(408) and show that modification of either position negatively impacts the catalytic activity of SAHH. X-ray crystal structures of 408-acetylated SAHH and dually acetylated SAHH have been determined and reveal perturbations in the C-terminal hydrogen bonding patterns, a region of the protein important for NAD(+) binding. These crystal structures along with mutagenesis data suggest that such hydrogen bond perturbations are responsible for SAHH catalytic inhibition by acetylation. These results suggest how increased acetylation of SAHH may globally influence cellular methylation patterns.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.