The conformational change of rabbit muscle pyruvate kinase induced by activating cations and its substrates
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,General Medicine,Biochemistry,Structural Biology
Reference19 articles.
1. Ligand-Induced Domain Movement in Pyruvate Kinase: Structure of the Enzyme from Rabbit Muscle with Mg2+, K+, andl-Phospholactate at 2.7 Å Resolution
2. The structure of cat muscle pyruvate kinase.
3. Structure of Rabbit Muscle Pyruvate Kinase Complexed with Mn2+, K+, and Pyruvate
4. Reversible solvent denaturation of rabbit muscle pyruvate kinase
5. Domain interaction in rabbit muscle pyruvate kinase. I. Effects of ligands on protein denaturation induced by guanidine hydrochloride.
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1. An overview of structure, function, and regulation of pyruvate kinases;Protein Science;2019-08-12
2. Changes in Enzyme Structural Dynamics Studied by Hydrogen Exchange-Mass Spectrometry: Ligand Binding Effects or Catalytically Relevant Motions?;Analytical Chemistry;2017-11-30
3. Monitoring thermal and chemical unfolding of Brugia malayi calreticulin using fluorescence and Circular Dichroism spectroscopy;International Journal of Biological Macromolecules;2017-09
4. Effects of activating cations and inhibitor on the allosteric regulation of rabbit muscle pyruvate kinase;International Journal of Biological Macromolecules;2013-09
5. Chemical and enzymatic characterization of recombinant rabbit muscle pyruvate kinase;Biological Chemistry;2013-05-01
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