Free-energy profile for the reaction catalyzed by triosephosphate isomerase

Abstract
The experimental results on the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate catalyzed by triosephosphate isomerase are collected and analyzed according to a theory previously presented in this series. The rate constants and fractionation factors so derived allow the construction of the Gibbs free-energy profile for this enzyme-catalyzed reaction.