ArticleACS chemical biology2013
Structural basis for enzyme I inhibition by α-ketoglutarate.
Article in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Structure-based Discovery of a Non-competitive FTO Inhibitor Bound to a Cryptic Site at the Domain Interface.Journal of molecular biology · 2026Article
- Inhibition of Chikungunya virus nsP2 protease in vitro by scorpion venom peptide pantinin-1.PloS one · 2026Article
- Increased Mevalonate Production Using Engineered Citrate Synthase and Phosphofructokinase Variants of Escherichia coli.Biotechnology and bioengineering · 2025Article
- Elucidation of the Mechanisms of Inter-domain Coupling in the Monomeric State of Enzyme I by High-pressure NMR.Journal of molecular biology · 2024Article
- Protein Conformational Dynamics Underlie Selective Recognition of Thermophilic over Mesophilic Enzyme I by a Substrate Analogue.Biomolecules · 2023Article
- Pyridoxal and α-Ketoglutarate Independently Improve Function of Saccharomyces cerevisiae Thi5 in the Metabolic Network of Salmonella enterica.Journal of bacteriology · 2022Article
- Structure elucidation of the elusive Enzyme I monomer reveals the molecular mechanisms linking oligomerization and enzymatic activity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Single Point Mutation Controls the Rate of Interconversion Between theFrontiers in molecular biosciences · 2021Article
- Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I.Journal of molecular biology · 2020Article
- N-terminal fusion of the N-terminal domain of bacterial enzyme I facilitates recombinant expression and purification of the human RNA demethylases FTO and Alkbh5.Protein expression and purification · 2020Article
- An allosteric pocket for inhibition of bacterial Enzyme I identified by NMR-based fragment screening.Journal of structural biology: X · 2020Article
- Regulatory mechanisms underlying coordination of amino acid and glucose catabolism in Escherichia coli.Nature communications · 2019Article
- The oligomerization state of bacterial enzyme I (EI) determines EI's allosteric stimulation or competitive inhibition by α-ketoglutarate.The Journal of biological chemistry · 2018Article
- Engineering glucose metabolism ofNPJ systems biology and applications · 2017Article
- Hybrid Approaches to Structural Characterization of Conformational Ensembles of Complex Macromolecular Systems Combining NMR Residual Dipolar Couplings and Solution X-ray Scattering.Chemical reviews · 2016Review
- The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite.Microbiology and molecular biology reviews : MMBR · 2015Review
- Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I.Nature communications · 2015Article
- Measurement of the temperature of the resting rotor in analytical ultracentrifugation.Analytical biochemistry · 2014Article
- Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Trends in biochemical sciences · 2013Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Creating new bacterial strains in which carbon and nitrogen metabolism are uncoupled is potentially very useful for optimizing yields of microbial produced chemicals from renewable carbon sources. However, the mechanisms that balance carbon and nitrogen consumption in bacteria are poorly understood. Recently, α-ketoglutarate (αKG), the carbon substrate for ammonia assimilation, has been observed to inhibit Escherichia coli enzyme I (EI), the first component of the bacterial phosphotransferase system (PTS), thereby providing a direct biochemical link between central carbon and nitrogen metabolism. Here we investigate the EI-αKG interaction by NMR and enzymatic assays. We show that αKG binds with a KD of ∼2.2 mM at the active site of EI, acting as a competitive inhibitor. In addition, we use molecular docking simulations to derive a structural model of the enzyme-inhibitor complex that is fully consistent with NMR and analytical ultracentrifugation data. We expect that the EI-αKG structure presented here will provide a starting point for structure-based design of EI mutants resistant to αKG.
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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.