Literature summary for 5.3.1.1 extracted from

Rozovsky, S.; McDermott, A.E.
Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase (2007), Proc. Natl. Acad. Sci. USA, 104, 2080-2085.

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Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
D-Glyceraldehyde 3-phosphate = glycerone phosphate	in situ magnetic resonance probes of the enzyme-bound substrates to test the question of whether the equilibrium concentrations are perturbed by the enzyme. In the exergonic conversion of glycerinaldehyde 3-phosphate to dihydroxyacetone phosphate the high discrimination against solvent isotope uptake is consistent with chemistry protected by a water-tight active-site loop, therefore introducing asymmetry into the reversible reaction	Saccharomyces cerevisiae	a

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Release 2023.1 (January 2023)