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Updated: Jun 19, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase
Andrea Varga1, Judit Szabó, Beáta Flachner
1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, PO Box 7, H-1518 Budapest, Hungary.
Abstract:
The energetic changes accompanying domain closure of 3-phosphoglycerate kinase, a typical hinge-bending enzyme, were assessed. Calorimetric titrations of the enzyme with each substrate, both in the absence and presence of the other one, provide information not only about the energetics of substrate binding, but of the associated conformational changes, including domain closure. Our results suggest that conformational rearrangements in the hinge generated by binding of both substrates provide the main driving force for domain closure overcoming the slightly unfavourable contact interactions between the domains.
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