Affiliation: University of Kansas Medical Center
Harris R, Fenton A. A critical review of the role of M2PYK in the Warburg effect. Biochim Biophys Acta Rev Cancer. 2019;1871:225-239 pubmed publisher
..Additional in-depth studies of the Warburg effect and specifically of the possible regulatory role of M2PYK in the Warburg effect are needed. ..
Fenton A, Hutchinson M. The pH dependence of the allosteric response of human liver pyruvate kinase to fructose-1,6-bisphosphate, ATP, and alanine. Arch Biochem Biophys. 2009;484:16-23 pubmed publisher
..In addition, our results fail to support a general correlation between pH dependent changes in effector affinity and pH dependent changes in the corresponding allosteric response. ..
Fenton A. Identification of allosteric-activating drug leads for human liver pyruvate kinase. Methods Mol Biol. 2012;796:369-82 pubmed publisher
..Using hL-PYK, we demonstrate the potential of drug library screens to identify allosteric-activator drug leads. ..
Carlson G, Fenton A. What Mutagenesis Can and Cannot Reveal About Allostery. Biophys J. 2016;110:1912-23 pubmed publisher
..We conclude that different possible mechanisms (rotation-of-solid-domains, movement of secondary structure, side-chain repacking, changes in dynamics, etc.) will result in different findings in whole-protein mutagenesis studies. ..
Fenton A, Tang Q. An activating interaction between the unphosphorylated n-terminus of human liver pyruvate kinase and the main body of the protein is interrupted by phosphorylation. Biochemistry. 2009;48:3816-8 pubmed publisher
Fenton A, Johnson T, Holyoak T. The pyruvate kinase model system, a cautionary tale for the use of osmolyte perturbations to support conformational equilibria in allostery. Protein Sci. 2010;19:1796-800 pubmed publisher
..These findings highlight the need to verify that compounds used as osmolytes to perturb preexisting conformational equilibrium do not directly interact with the protein, a consideration not commonly addressed in the past. ..
Fenton A, Williams R, Trewhella J. Changes in small-angle X-ray scattering parameters observed upon binding of ligand to rabbit muscle pyruvate kinase are not correlated with allosteric transitions. Biochemistry. 2010;49:7202-9 pubmed publisher
..e., the small amino acids have minimal allosteric effects), PEP binding elicits different changes in the SAXS signature of the free enzyme versus the M(1)-PYK-small amino acid complexes...