ArticleIUCrJ2014
Structure and function study of the complex that synthesizes S-adenosylmethionine.
Article in IUCrJ, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 50 citations in OpenAlex.
- Article
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- Serum proteomic profiling of sepsis patients reveals a protein-based diagnostic model, with metabolomic insights into carbapenem-resistantFrontiers in immunology · 2026Article
- IGF2BP3 redirects glycolytic flux to promote one-carbon metabolism and RNA methylation.Cell reports · 2025Article
- Selective chemical tracking of DNA methylomes in live cells.Epigenomics · 2025Article
- Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism.International journal of molecular sciences · 2025Review
- MAT2B regulates the protein level of MAT2A to preserve RNA N6-methyladenosine.Cell death & disease · 2024Article
- Targeting allosteric regulation of cancer metabolism.Nature chemical biology · 2022Review
- Methionine adenosyltransferase 1a antisense oligonucleotides activate the liver-brown adipose tissue axis preventing obesity and associated hepatosteatosis.Nature communications · 2022Article
- Polar Interactions at the Dimer-Dimer Interface of Methionine Adenosyltransferase MAT I Control Tetramerization.International journal of molecular sciences · 2021Article
- Human Mat2A Uses an Ordered Kinetic Mechanism and Is Stabilized but Not Regulated by Mat2B.Biochemistry · 2021Article
- Mechanism and Inhibition of Human Methionine Adenosyltransferase 2A.Biochemistry · 2021Article
- Research progress and perspective in metabolism and metabolomics of psoriasis.Chinese medical journal · 2020Article
- Structural basis of the dominant inheritance of hypermethioninemia associated with the Arg264His mutation in the MAT1A gene.Acta crystallographica. Section D, Structural biology · 2020Article
- S-adenosylmethionine synthases in plants: Structural characterization of type I and II isoenzymes from Arabidopsis thaliana and Medicago truncatula.International journal of biological macromolecules · 2020Article
- Methionine adenosyltransferases in liver cancer.World journal of gastroenterology · 2019Review
- Control and regulation of S-Adenosylmethionine biosynthesis by the regulatory β subunit and quinolone-based compounds.The FEBS journal · 2019Article
- MicroRNA-203 impacts on the growth, aggressiveness and prognosis of hepatocellular carcinoma by targetingOncotarget · 2019Article
- Structure of a critical metabolic enzyme: S-adenosylmethionine synthetase from Cryptosporidium parvum.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Identification of a natural inhibitor of methionine adenosyltransferase 2A regulating one-carbon metabolism in keratinocytes.EBioMedicine · 2019Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
S-Adenosylmethionine (SAMe) is the principal methyl donor of the cell and is synthesized via an ATP-driven process by methionine adenosyltransferase (MAT) enzymes. It is tightly linked with cell proliferation in liver and colon cancer. In humans, there are three genes, mat1A, mat2A and mat2B, which encode MAT enzymes. mat2A and mat2B transcribe MATα2 and MATβ enzyme subunits, respectively, with catalytic and regulatory roles. The MATα2β complex is expressed in nearly all tissues and is thought to be essential in providing the necessary SAMe flux for methylation of DNA and various proteins including histones. In human hepatocellular carcinoma mat2A and mat2B genes are upregulated, highlighting the importance of the MATα2β complex in liver disease. The individual subunits have been structurally characterized but the nature of the complex has remained elusive despite its existence having been postulated for more than 20 years and the observation that MATβ is often co-localized with MATα2. Though SAMe can be produced by MAT(α2)4 alone, this paper shows that the V max of the MATα2β complex is three- to fourfold higher depending on the variants of MATβ that participate in complex formation. Using X-ray crystallography and solution X-ray scattering, the first structures are provided of this 258 kDa functional complex both in crystals and solution with an unexpected stoichiometry of 4α2 and 2βV2 subunits. It is demonstrated that the N-terminal regulates the activity of the complex and it is shown that complex formation takes place surprisingly via the C-terminal of MATβV2 that buries itself in a tunnel created at the interface of the MAT(α2)2. The structural data suggest a unique mechanism of regulation and provide a gateway for structure-based drug design in anticancer therapies.
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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.