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

Amyes, T. L. and O'Donoghue, A. M. C. and Richard, J. P. (2001) 'Contribution of phosphate intrinsic binding energy to the enzymatic rate acceleration for triosephosphate isomerase.', Journal of the American Chemical Society., 123 (45). pp. 11325-11326.

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.

Item Type:Article
Additional Information:
Full text:Full text not available from this repository.
Publisher Web site:http://dx.doi.org/10.1021/ja016754a
Record Created:03 May 2007
Last Modified:08 Apr 2009 16:30

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