ArticleActa crystallographica. Section D, Biological crystallography2012
High-resolution structures of complexes of plant S-adenosyl-L-homocysteine hydrolase (Lupinus luteus).
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Review
- AHCY: A metabolic gatekeeper at the interface of methylation, redox balance, and cellular stress response.The Journal of biological chemistry · 2026Review
- Homocysteine Metabolites, Endothelial Dysfunction, and Cardiovascular Disease.International journal of molecular sciences · 2025Review
- Engineered reduction of S-adenosylmethionine alters lignin in sorghum.Biotechnology for biofuels and bioproducts · 2024Article
- Structure, function and substrate preferences of archaeal S-adenosyl-L-homocysteine hydrolases.Communications biology · 2024Article
- Whole genome identification, molecular docking and expression analysis of enzymes involved in the selenomethionine cycle in Cardamine hupingshanensis.BMC plant biology · 2024Article
- S-adenosyl-L-homocysteine hydrolase FgSah1 is required for fungal development and virulence inVirulence · 2021Article
- Review
- Methylation deficiency disrupts biological rhythms from bacteria to humans.Communications biology · 2020Article
- Evolutionary conservation and post-translational control of S-adenosyl-L-homocysteine hydrolase in land plants.PloS one · 2020Article
- Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa.Scientific reports · 2018Article
- Article
- S-adenosyl-L-homocysteine hydrolase from a hyperthermophile (Thermotoga maritima) is expressed in Escherichia coli in inactive form - Biochemical and structural studies.International journal of biological macromolecules · 2017Article
- Crystallographic and SAXS studies ofIUCrJ · 2017Article
- Structural insights into the reaction mechanism of S-adenosyl-L-homocysteine hydrolase.Scientific reports · 2015Article
- Crystallization and preliminary X-ray diffraction analysis of the S-adenosylhomocysteine hydrolase (SAHH) from Thermotoga maritima.Acta crystallographica. Section F, Structural biology communications · 2014Article
- S-adenosyl-L-homocysteine hydrolase and methylation disorders: yeast as a model system.Biochimica et biophysica acta · 2013Review
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
S-Adenosyl-L-homocysteine hydrolase (SAHase) catalyzes the reversible breakdown of S-adenosyl-L-homocysteine (SAH) to adenosine and homocysteine. SAH is formed in methylation reactions that utilize S-adenosyl-L-methionine (SAM) as a methyl donor. By removing the SAH byproduct, SAHase serves as a major regulator of SAM-dependent biological methylation reactions. Here, the first crystal structure of SAHase of plant origin, that from the legume yellow lupin (LlSAHase), is presented. Structures have been determined at high resolution for three complexes of the enzyme: those with a reaction byproduct/substrate (adenosine), with its nonoxidizable analog (cordycepin) and with a product of inhibitor cleavage (adenine). In all three cases the enzyme has a closed conformation. A sodium cation is found near the active site, coordinated by residues from a conserved loop that hinges domain movement upon reactant binding. An insertion segment that is present in all plant SAHases is located near a substrate-pocket access channel and participates in its formation. In contrast to mammalian and bacterial SAHases, the channel is open when adenosine or cordycepin is bound and is closed in the adenine complex. In contrast to SAHases from other organisms, which are active as tetramers, the plant enzyme functions as a homodimer in solution.
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