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

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

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
• Public URL: https://durham-repository.worktribe.com/output/1574525