Literature summary for 5.3.1.1 extracted from

Samanta, M.; Banerjee, M.; Murthy, M.R.; Balaram, H.; Balaram, P.
Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stability (2011), FEBS J., 278, 1932-1943.

Search for more literature for 5.3.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli AA200 cells	Plasmodium falciparum

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant enzyme C126S in complex with PGA, hanging drop vapor diffusion method, using 20% (w/v) poly(ethylene glycol), 1 M HEPES buffer (pH 7.5), and 10 mM lithium sulfate, at 23°C. Unliganded mutant enzymes C126S and C126A, hanging drop vapor diffusion method, using 24% (w/v) poly(ethylene glycol), 1 M HEPES buffer (pH 7.0), and 10 mM lithium sulfate	Plasmodium falciparum

Protein Variants

Protein Variants	Comment	Organism
C126A	the mutant shows an approximately 5.8fold drop in kcat compared to the wild type enzyme	Plasmodium falciparum
C126M	the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme	Plasmodium falciparum
C126S	the mutant shows an approximately 5.8fold drop in kcat compared to the wild type enzyme	Plasmodium falciparum
C126T	the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme	Plasmodium falciparum
C126V	the mutant shows an approximately 10fold drop in catalytic activity compared to the wild type enzyme	Plasmodium falciparum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.35	-	D-glyceraldehyde 3-phosphate	wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
1	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
1.2	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
1.4	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
1.5	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
1.5	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	Q07412	-	-

Purification (Commentary)

Purification (Comment)	Organism
ammonium sulfate precipitation, Q-Sepharose column chromatography, and Sephacryl-200 gel filtration	Plasmodium falciparum

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
TIM	-	Plasmodium falciparum
Triosephosphate isomerase	-	Plasmodium falciparum

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
25	50	for the wild type enzyme, there is an increase in activity over the temperature range 25-40°C, with a leveling off between 40°C and 50°C	Plasmodium falciparum

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
160	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
190	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
330	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
750	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
770	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
4300	-	D-glyceraldehyde 3-phosphate	wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
120	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126M, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
160	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126V, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
280	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126T, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
520	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126A, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
540	-	D-glyceraldehyde 3-phosphate	mutant enzyme C126S, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum
12000	-	D-glyceraldehyde 3-phosphate	wild type enzyme, in 100 mM triethanolamine-HCl (pH 7.6), at 23°C	Plasmodium falciparum

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Release 2023.1 (January 2023)