刊名:International Journal of Biological Macromolecules
出版年:2010
出版时间:1 August 2010
年:2010
卷:47
期:2
页码:228-232
全文大小:294 K
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.