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

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