Divalent cations in human liver pyruvate kinase exemplify the combined effects of complex-equilibrium and allosteric regulation.

ABSTRACT: There is growing recognition that the functional outcome of binding of an allosteric regulator to a protein/enzyme is influenced by the presence of other ligands. Here, this complexity is exemplified in the allosteric regulation of human liver pyruvate kinase (hLPYK) that is influenced by the presence of a range of divalent cation types and concentrations. For this system, fructose-1,6-bisphosphate (activator) and alanine (inhibitor) both influence the protein's affinity for the substrate, phosphoenolpyruvate (PEP). Mg²⁺, Mn²⁺, Ni²⁺, and Co²⁺ were the primary divalent cations evaluated, although Zn²⁺, Cd²⁺, V²⁺, Pb²⁺, Fe²⁺, and Cu²⁺also supported activity. Allosteric coupling betwe

SUBMITTER: Martin TA 

PROVIDER: S-EPMC10310847 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature