ArticleThe Journal of biological chemistry2009
Direct Mg(2+) binding activates adenylate kinase from Escherichia coli.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Molecular bases of circadian magnesium rhythms across eukaryotes.FEBS letters · 2026Article
- Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome.bioRxiv : the preprint server for biology · 2025Article
- Conformation state-specific monobodies regulate the functions of flexible proteins through conformation trapping.Protein science : a publication of the Protein Society · 2023Article
- Frustration and the Kinetic Repartitioning Mechanism of Substrate Inhibition in Enzyme Catalysis.The journal of physical chemistry. B · 2022Article
- Rational Design of Adenylate Kinase Thermostability through Coevolution and Sequence Divergence Analysis.International journal of molecular sciences · 2021Article
- Cryo-EM Analyses Permit Visualization of Structural Polymorphism of Biological Macromolecules.Frontiers in bioinformatics · 2021Review
- Single-Molecule Fluorescence Methods to Study Plant Hormone Signal Transduction Pathways.Frontiers in plant science · 2017Article
- Architectural plasticity of AMPK revealed by electron microscopy and X-ray crystallography.Scientific reports · 2016Article
- The energy landscape of adenylate kinase during catalysis.Nature structural & molecular biology · 2015Article
- Biomolecular dynamics: order-disorder transitions and energy landscapes.Reports on progress in physics. Physical Society (Great Britain) · 2012Article
- Observation of protein folding/unfolding dynamics of ubiquitin trapped in agarose gel by single-molecule FRET.European biophysics journal : EBJ · 2012Article
- On the roles of substrate binding and hinge unfolding in conformational changes of adenylate kinase.Biophysical journal · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
We report evidence that adenylate kinase (AK) from Escherichia coli can be activated by the direct binding of a magnesium ion to the enzyme, in addition to ATP-complexed Mg(2+). By systematically varying the concentrations of AMP, ATP, and magnesium in kinetic experiments, we found that the apparent substrate inhibition of AK, formerly attributed to AMP, was suppressed at low magnesium concentrations and enhanced at high magnesium concentrations. This previously unreported magnesium dependence can be accounted for by a modified random bi-bi model in which Mg(2+) can bind to AK directly prior to AMP binding. A new kinetic model is proposed to replace the conventional random bi-bi mechanism with substrate inhibition and is able to describe the kinetic data over a physiologically relevant range of magnesium concentrations. According to this model, the magnesium-activated AK exhibits a 23- +/- 3-fold increase in its forward reaction rate compared with the unactivated form. The findings imply that Mg(2+) could be an important affecter in the energy signaling network in cells.
Indexed as
Identifiers
What OpenQuestion holds
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.