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Native Mass Spectrometry Gives Insight into the Allosteric Binding Mechanism of M2 Pyruvate Kinase to Fructose-1,6-Bisphosphate.

Biochemistry - 20 Mar 2018

Gavriilidou Agni F M, Holding Finn P, Mayer Daniel, Coyle Joseph E, Veprintsev Dmitry B, Zenobi Renato

Abstract excerpt

The various oligomeric states of the M2 isoform of pyruvate kinase (PKM2) were distinguished using native mass spectrometry. The effect of PKM2 concentration on its dimer-tetramer equilibrium was monitored, and a value for the dissociation constant ( Kd) of the two species was estimated to be 0.95 μM. Results of binding of fructose-1,6-bisphosphate (FBP) to PKM2 are shown and provide insight into the allosteric...

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PMID: 29499117
DOI: 10.1021/acs.biochem.7b01270

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