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. 1980 Jun;77(6):3374–3378. doi: 10.1073/pnas.77.6.3374

Conformational changes during enzyme catalysis: role of water in the transition state.

R B Loftfield, E A Eigner, A Pastuszyn, T N Lövgren, H Jakubowski
PMCID: PMC349618  PMID: 6932025

Abstract

The entropy of activation for the synthesis of Ile-tRNA is high and positive. The only likely source of a high delta S is the loss of structured water as the enzyme . substrate complex moves toward the transition state. This requires a change in the orientation or nature of water-organizing residues in the interface between the enzyme . substrate complex and the water. Such changes, which may be some distance from the "active site," are coupled to the active site in such a way that the increased entropy and decreased free energy of the water--enzyme interface is available at the "active site" to reduce the free energy of activation. The effects of Hofmeister anions on KmS and KcatS are consistent with the entropy data.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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