Distinguishing the Interactions in the Fructose 1,6-Bisphosphate Binding Site of Human Liver Pyruvate Kinase That Contribute to Allostery
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, Kansas 66160, United States
2. Clinical Laboratory Sciences, The University of Kansas Medical Center, Kansas City, Kansas 66160, United States
Funder
National Institutes of Health
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi501426w
Reference27 articles.
1. Differentiating a Ligand's Chemical Requirements for Allosteric Interactions from Those for Protein Binding. Phenylalanine Inhibition of Pyruvate Kinase,
2. Effector Analogues Detect Varied Allosteric Roles for Conserved Protein−Effector Interactions in Pyruvate Kinase Isozymes
3. Glutamic Dehydrogenase
4. Allosteric nucleotide specificity of phosphorylase kinase: correlation of binding, conformational transitions, and activation. Utilization of lin-benzo-ADP to measure the binding of other nucleoside diphosphates, including the phosphorothioates of ADP.
5. Use of Binding Enthalpy To Drive an Allosteric Transition
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