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

Yan Ou; Wenbing Tao; Yun Zhang; Guangrong Wu; Shaoning Yu

doi:10.1016/j.ijbiomac.2010.04.017

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

Int J Biol Macromol. 2010 Aug 1;47(2):228-32. doi: 10.1016/j.ijbiomac.2010.04.017. Epub 2010 May 8.

Authors

Yan Ou¹, Wenbing Tao, Yun Zhang, Guangrong Wu, Shaoning Yu

Affiliation

¹ Department of Chemistry, Fudan University, Shanghai 200433, China.

PMID: 20435056
DOI: 10.1016/j.ijbiomac.2010.04.017

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 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Cations / pharmacology
Circular Dichroism
Enzyme Activation / drug effects
Enzyme Inhibitors / pharmacology
Models, Molecular
Muscles / enzymology*
Protein Conformation / drug effects
Protein Denaturation / drug effects
Pyruvate Kinase / antagonists & inhibitors
Pyruvate Kinase / chemistry*
Pyruvate Kinase / metabolism*
Rabbits
Solvents / chemistry
Spectrometry, Fluorescence
Temperature
Tryptophan

Substances

Cations
Enzyme Inhibitors
Solvents
Tryptophan
Pyruvate Kinase