The conformational change of rabbit muscle pyruvate kinase induced by activating cations and its substrates

Catalysis by rabbit muscle pyruvate kinase involves domain movements and conformational changes induced by activating cations and its substrates. Fluorescence acrylamide quenching analyses reveal that interactions with Mg2+ and K+ lead to a more exposed active site of PK while interactions with PEP and ADP decrease solvent accessibility of the active site.