| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1987406 | International Journal of Biological Macromolecules | 2010 | 5 Pages |
Abstract
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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Authors
Yan Ou, Wenbing Tao, Yun Zhang, Guangrong Wu, Shaoning Yu,