ArticleBiochemistry2013
Identification of regions of rabbit muscle pyruvate kinase important for allosteric regulation by phenylalanine, detected by H/D exchange mass spectrometry.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- From structural insight to molecule: Integrative molecular simulations identify candidate pyruvate kinase activators.PloS one · 2026Article
- PYK-SubstitutionOME: an integrated database containing allosteric coupling, ligand affinity and mutational, structural, pathological, bioinformatic and computational information about pyruvate kinase isozymes.Database : the journal of biological databases and curation · 2023Article
- Ligand-specific changes in conformational flexibility mediate long-range allostery in the lac repressor.Nature communications · 2023Article
- Article
- H/D Exchange Characterization of Silent Coupling: Entropy-Enthalpy Compensation in Allostery.Biophysical journal · 2020Article
- Construction of a Fluorescent Screening System of Allosteric Modulators for the GABAACS central science · 2019Article
- Alternol eliminates excessive ATP production by disturbing Krebs cycle in prostate cancer.The Prostate · 2019Article
- RheoScale: A tool to aggregate and quantify experimentally determined substitution outcomes for multiple variants at individual protein positions.Human mutation · 2018Article
- An allostatic mechanism for M2 pyruvate kinase as an amino-acid sensor.The Biochemical journal · 2018Article
- Whole-protein alanine-scanning mutagenesis of allostery: A large percentage of a protein can contribute to mechanism.Human mutation · 2017Article
- Inhibition of expression of the circadian clock gene Period causes metabolic abnormalities including repression of glycometabolism in Bombyx mori cells.Scientific reports · 2017Article
- What Mutagenesis Can and Cannot Reveal About Allostery.Biophysical journal · 2016Review
- Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase.The Journal of biological chemistry · 2014Article
- ASD v2.0: updated content and novel features focusing on allosteric regulation.Nucleic acids research · 2014Article
- Glycolysis, tumor metabolism, cancer growth and dissemination. A new pH-based etiopathogenic perspective and therapeutic approach to an old cancer question.Oncoscience · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Mass spectrometry has been used to determine the number of exchangeable backbone amide protons and the associated rate constants that are altered when rabbit muscle pyruvate kinase (rM1-PYK) binds either the allosteric inhibitor (phenylalanine) or a nonallosteric analogue of the inhibitor. Alanine is used as the nonallosteric analogue because it binds competitively with phenylalanine but elicits a negligible allosteric inhibition, i.e., a negligible reduction in the affinity of rM1-PYK for the substrate, phosphoenolpyruvate. This experimental design is expected to distinguish changes in the protein caused by effector binding (i.e., those changes common upon the addition of alanine vs phenylalanine) from changes associated with allosteric regulation (i.e., those elicited by the addition of phenylalanine binding, but not alanine binding). High-quality peptic fragments covering 98% of the protein were identified. Changes in both the number of exchangeable protons per peptide and in the rate constant associated with exchange highlight regions of the protein with allosteric roles. The set of allosterically relevant peptides identified by this technique includes residues previously identified by mutagenesis to have roles in allosteric regulation by phenylalanine.
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