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The pyruvate kinase model system, a cautionary tale for the use of osmolyte perturbations to support conformational equilibria in allostery
Article first published online: 13 JUL 2010
DOI: 10.1002/pro.450
Copyright © 2010 The Protein Society
Additional Information
How to Cite
Fenton, A. W., Johnson, T. A. and Holyoak, T. (2010), The pyruvate kinase model system, a cautionary tale for the use of osmolyte perturbations to support conformational equilibria in allostery. Protein Science, 19: 1796–1800. doi: 10.1002/pro.450
Publication History
- Issue published online: 23 AUG 2010
- Article first published online: 13 JUL 2010
- Manuscript Accepted: 27 MAY 2010
- Manuscript Received: 13 APR 2010
Funded by
- NIH. Grant Number: DK78076
- National Center for Research Resources. Grant Number: P20 RR17708
References
- 1, , , , ( 2006) Differentiating a ligand's chemical requirements for allosteric interactions from those for protein binding. Phenylalanine inhibition of pyruvate kinase(,). Biochemistry 45: 5421–5429.
- 2( 2008) Allostery: an illustrated definition for the “second secret of life.” Trends Biochem Sci 33: 420–425.
- 3( 2008) Modulation of allostery of pyruvate kinase by shifting of an ensemble of microstates. Acta biochimica et biophysica Sinica 40: 663–669.Direct Link:
- 4, , ( 2003) Further evidence for the reliance of catalysis by rabbit muscle pyruvate kinase upon isomerization of the ternary complex between enzyme and products. Biophys Chem 104: 189–198.
- 5, ( 2002) Calorimetric demonstration of the potential of molecular crowding to emulate the effect of an allosteric activator on pyruvate kinase kinetics. Biochemistry 41: 6897–6901.
- 6( 2004) Quantitative analysis and interpretation of allosteric behavior. Methods Enzymol 380: 187–203.
- 7( 1972) Ligand binding and internal equilibria in proteins. Biochemistry 11: 864–878.

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