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.
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.
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|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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