ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural basis and evolution of redox regulation in plant adenosine-5'-phosphosulfate kinase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 77 citations in OpenAlex.
- Structural insights into interdomain interactions inJournal of structural biology: X · 2026Article
- Determining the Redox Potential of a Protein Disulfide Bond.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Classification of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Genome-wide identification, molecular docking and expression analysis of enzymes involved in the primary and secondary metabolic branching points of the selenium metabolic pathway in Cardamine hupingshanensis.BMC plant biology · 2025Article
- Adaptive modifications in plant sulfur metabolism over evolutionary time.Journal of experimental botany · 2024Review
- Assimilatory sulfate reduction in the marine methanogen Methanothermococcus thermolithotrophicus.Nature microbiology · 2023Article
- Comparison of Genome and Plasmid-Based Engineering of Multigene Benzylglucosinolate Pathway in Saccharomyces cerevisiae.Applied and environmental microbiology · 2022Article
- Redox regulation of enzymes involved in sulfate assimilation and in the synthesis of sulfur-containing amino acids and glutathione in plants.Frontiers in plant science · 2022Review
- Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes.Antioxidants (Basel, Switzerland) · 2021Review
- Integration of sulfate assimilation with carbon and nitrogen metabolism in transition from C3 to C4 photosynthesis.Journal of experimental botany · 2019Review
- Sulfation pathways from red to green.The Journal of biological chemistry · 2019Review
- Characterization of Entamoeba histolytica adenosine 5'-phosphosulfate (APS) kinase; validation as a target and provision of leads for the development of new drugs against amoebiasis.PLoS neglected tropical diseases · 2019Article
- Allosteric disulphide bonds as reversible mechano-sensitive switches that control protein functions in the vasculature.Biophysical reviews · 2019Review
- SULTR3s Function in Chloroplast Sulfate Uptake and Affect ABA Biosynthesis and the Stress Response.Plant physiology · 2019Article
- Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation.The Journal of biological chemistry · 2019Review
- Sulfur Partitioning between Glutathione and Protein Synthesis Determines Plant Growth.Plant physiology · 2018Article
- Article
- Central Role of Adenosine 5'-Phosphosulfate Reductase in the Control of Plant Hydrogen Sulfide Metabolism.Frontiers in plant science · 2018Review
- Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Recapitulating the Structural Evolution of Redox Regulation in Adenosine 5'-Phosphosulfate Kinase from Cyanobacteria to Plants.The Journal of biological chemistry · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adenosine-5'-phosphosulfate (APS) kinase (APSK) catalyzes the phosphorylation of APS to 3'-phospho-APS (PAPS). In Arabidopsis thaliana, APSK is essential for reproductive viability and competes with APS reductase to partition sulfate between the primary and secondary branches of the sulfur assimilatory pathway; however, the biochemical regulation of APSK is poorly understood. The 1.8-Å resolution crystal structure of APSR from A. thaliana (AtAPSK) in complex with β,γ-imidoadenosine-5'-triphosphate, Mg(2+), and APS provides a view of the Michaelis complex for this enzyme and reveals the presence of an intersubunit disulfide bond between Cys86 and Cys119. Functional analysis of AtAPSK demonstrates that reduction of Cys86-Cys119 resulted in a 17-fold higher k(cat)/K(m) and a 15-fold increase in K(i) for substrate inhibition by APS compared with the oxidized enzyme. The C86A/C119A mutant was kinetically similar to the reduced WT enzyme. Gel- and activity-based titrations indicate that the midpoint potential of the disulfide in AtAPSK is comparable to that observed in APS reductase. Both cysteines are invariant among the APSK from plants, but not other organisms, which suggests redox-control as a unique regulatory feature of the plant APSK. Based on structural, functional, and sequence analyses, we propose that the redox-sensitive APSK evolved after bifurcation of the sulfur assimilatory pathway in the green plant lineage and that changes in redox environment resulting from oxidative stresses may affect partitioning of APS into the primary and secondary thiol metabolic routes by having opposing effects on APSK and APS reductase in plants.
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