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Contribution of phosphate intrinsic binding energy to the enzymatic rate acceleration for triosephosphate isomerase

Amyes, T.L.; O'Donoghue, A.C.; Richard, J.P.

Authors

T.L. Amyes

J.P. Richard



Abstract

We report that 80% of the enzymatic rate acceleration for the prototypical proton transfer from carbon catalyzed by triosephosphate isomerase can be directly attributed to the remote phosphodianion group of the substrate (R)-glyceraldehyde 3-phosphate, and that the intrinsic binding energy of this functional group in the transition state for enzyme-catalyzed enolization is 14 kcal/mol.

Citation

Amyes, T., O'Donoghue, A., & Richard, J. (2001). Contribution of phosphate intrinsic binding energy to the enzymatic rate acceleration for triosephosphate isomerase. Journal of the American Chemical Society, 123(45), 11325-11326. https://doi.org/10.1021/ja016754a

Journal Article Type Article
Publication Date Oct 1, 2001
Deposit Date May 3, 2007
Journal Journal of the American Chemical Society
Print ISSN 0002-7863
Electronic ISSN 1520-5126
Publisher American Chemical Society
Peer Reviewed Peer Reviewed
Volume 123
Issue 45
Pages 11325-11326
DOI https://doi.org/10.1021/ja016754a


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