Literature summary for 5.3.1.1 extracted from

Reyes-Lopez, C.A.; Gonzalez-Mondragon, E.; Benitez-Cardoza, C.G.; Chanez-Cardenas, M.E.; Cabrera, N.; Perez-Montfort, R.; Hernandez-Arana, A.
The conserved salt bridge linking two C-terminal beta /alpha units in homodimeric triosephosphate isomerase determines the folding rate of the monomer (2008), Proteins Struct. Funct. Bioinform., 72, 972-979.

Protein Variants

Protein Variants	Comment	Organism
D225Q	mutation causes minor drops in Km and kcat value without changes catalytic efficiency. Temperature-induced unfolding-refolding of both wild-type and mutant D225Q samples display hysteresis cycles, indicative of processes far from equilibrium. The rate constant for unfolding is about three-fold larger in the mutant than in wild-type. Upon mutation, the rate-limiting step changes from a second-order at submicromolar concentrations to a first-order reaction. Renaturation occurs through a uni-bimolecular mechanism in which refolding of the monomer most likely begins at the C-terminal half of its polypeptide chain	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.91	-	D-glyceraldehyde 3-phosphate	mutant D225Q, pH 7.4, 25°C	Saccharomyces cerevisiae
1.13	-	D-glyceraldehyde 3-phosphate	wild-type, pH 7.4, 25°C	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
temperature-induced unfolding-refolding of both wild-type and mutant D225Q samples display hysteresis cycles, indicative of processes far from equilibrium. The rate constant for unfolding is about three-fold larger in the mutant than in wild-type. Upon mutation, the rate-limiting step changes from a second-order at submicromolar concentrations to a first-order reaction. Renaturation occurs through a uni-bimolecular mechanism in which refolding of the monomer most likely begins at the C-terminal half of its polypeptide chain	Saccharomyces cerevisiae

Renatured (Comment)

Organism

temperature-induced unfolding-refolding of both wild-type and mutant D225Q samples display hysteresis cycles, indicative of processes far from equilibrium. The rate constant for unfolding is about three-fold larger in the mutant than in wild-type. Upon mutation, the rate-limiting step changes from a second-order at submicromolar concentrations to a first-order reaction. Renaturation occurs through a uni-bimolecular mechanism in which refolding of the monomer most likely begins at the C-terminal half of its polypeptide chain

Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glyceraldehyde 3-phosphate	-	Saccharomyces cerevisiae	dihydroxyacetone phosphate	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
4600	-	D-glyceraldehyde 3-phosphate	mutant D225Q, pH 7.4, 25°C	Saccharomyces cerevisiae
6900	-	D-glyceraldehyde 3-phosphate	wild-type, pH 7.4, 25°C	Saccharomyces cerevisiae