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 Mg 2+ and K + lead to a more exposed active site of PK while interactions with PE...

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Bibliographic Details
Published in:International journal of biological macromolecules 2010-08, Vol.47 (2), p.228-232
Main Authors: Ou, Yan, Tao, Wenbing, Zhang, Yun, Wu, Guangrong, Yu, Shaoning
Format: Article
Language:English
Subjects:
Acrylamide quenching
Animals
Cations - pharmacology
Circular Dichroism
Conformational change
Enzyme Activation - drug effects
Enzyme Inhibitors - pharmacology
Fluorescence
Models, Molecular
Muscles - enzymology
Protein Conformation - drug effects
Protein Denaturation - drug effects
Pyruvate kinase
Pyruvate Kinase - antagonists & inhibitors
Pyruvate Kinase - chemistry
Pyruvate Kinase - metabolism
Rabbits
Solvents - chemistry
Spectrometry, Fluorescence
Temperature
Tryptophan
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Summary: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 Mg 2+ and K + lead to a more exposed active site of PK while interactions with PEP and ADP decrease solvent accessibility of the active site.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2010.04.017