Literature DB >> 999838

Free-energy profile of the reaction catalyzed by triosephosphate isomerase.

W J Albery, J R Knowles.   

Abstract

The experimental results on the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate catalyzed by triosephosphate isomerase that are presented in the previous five papers are here collected and analyzed according to the theory presented in the first paper (Albery, W.J., Knowles, J.R. (1976), Biochemistry 15, the first of eight papers in a series in this issue). The rate constants and fractionation factors so derived allow the construction of theGibbs free-energy profile for this enzyme-catalyzed reaction.

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Year:  1976        PMID： 999838     DOI： 10.1021/bi00670a031

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


  53 in total

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9.  Stereospecific Formation of E- and Z-Disubstituted Double Bonds by Dehydratase Domains from Modules 1 and 2 of the Fostriecin Polyketide Synthase.

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