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Literature summary for 5.3.1.1 extracted from

  • Zomosa-Signoret, V.; Aguirre-Lopez, B.; Hernandez-Alcantara, G.; Perez-Montfort, R.; Tuena de Gomez-Puyou, M.; Gomez-Puyou, A.
    Crosstalk between the subunits of the homodimeric enzyme triosephosphate isomerase (2007), Proteins Struct. Funct. Bioinform., 67, 75-83.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C15A dimer formation of mutant protein with intact Trypanosoma brucei monomer, maximal inhibition of catalysis by mutation is 60%. Dimer formation with catalytically inert Trypanosoma brucei mutant E168D causes a drop in activity by 50% Trypanosoma cruzi
E168D catalytically inert. Dimer formation with Trypanosoma cruzi dimer interface mutant C15Acauses a drop in activity by 50% Trypanosoma brucei
additional information hybrids of Trypanosoma cruzi enzyme carrying residues of the dimer interface from Trypanomsoma brucei and vice versa, and hybrids with one monomer in the enzyme dimer from Trypanosoma cruzi, and the second monomer from Trypanosoma brucei. Solvent exposure of the interfacial C15 depends predominantly on the characteristics of the adjoining monomer. Half of the activity of each monomer depends on the integrity of each of the two C15-loop3 portions of the interface Trypanosoma brucei
additional information hybrids of Trypanosoma cruzi enzyme carrying residues of the dimer interface from Trypanomsoma brucei and vice versa, and hybrids with one monomer in the enzyme dimer from Trypanosoma cruzi, and the second monomer from Trypanosoma brucei. Solvent exposure of the interfacial C15 depends predominantly on the characteristics of the adjoining monomer. Half of the activity of each monomer depends on the integrity of each of the two C15-loop3 portions of the interface Trypanosoma cruzi

Inhibitors

Inhibitors Comment Organism Structure
methylmethane thiosulfonate modification at C15 in the dimer interface, inducing abolition of catalysis and structural changes. Susceptibility of Trypanosoma cruzi enzyme to modification of C15 is nearly 100fold higher than susceptibility of C15 of Trypanosoma brucei Trypanosoma brucei
methylmethane thiosulfonate modification at C15 in the dimer interface, inducing abolition of catalysis and structural changes. Susceptibility of Trypanosoma cruzi enzyme to modification of C15 is nearly 100fold higher than susceptibility of C15 of Trypanosoma brucei Trypanosoma cruzi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.18
-
D-glyceraldehyde 3-phosphate mutant E168D, pH 7.4, 25°C Trypanosoma brucei
0.28
-
D-glyceraldehyde 3-phosphate in complex with mutant C15A of Trypanosoma cruzi enzyme, pH 7.4, 25°C Trypanosoma brucei
0.28
-
D-glyceraldehyde 3-phosphate mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25°C Trypanosoma cruzi
0.31
-
D-glyceraldehyde 3-phosphate in complex with monomer from Trypanosoma brucei, pH 7.4, 25°C Trypanosoma cruzi
0.31
-
D-glyceraldehyde 3-phosphate in complex with monomer from Trypanosoma cruzi, pH 7.4, 25°C Trypanosoma brucei
0.42
-
D-glyceraldehyde 3-phosphate mutant C15A, pH 7.4, 25°C Trypanosoma cruzi
0.45
-
D-glyceraldehyde 3-phosphate wild-type, pH 7.4, 25°C Trypanosoma cruzi
0.46
-
D-glyceraldehyde 3-phosphate wild-type, pH 7.4, 25°C Trypanosoma brucei
0.62
-
D-glyceraldehyde 3-phosphate in complex with mutant C15A of Trypanosoma cruzi enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C Trypanosoma brucei
0.62
-
D-glyceraldehyde 3-phosphate mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C Trypanosoma cruzi
0.69
-
D-glyceraldehyde 3-phosphate mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25°C Trypanosoma cruzi
0.69
-
D-glyceraldehyde 3-phosphate mutant E168D in complex with mutant C15A of Trypanosoma cruzi, pH 7.4, 25°C Trypanosoma brucei

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei
-
-
-
Trypanosoma cruzi
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate
-
Trypanosoma brucei dihydroxyacetone phosphate
-
?
D-glyceraldehyde 3-phosphate
-
Trypanosoma cruzi dihydroxyacetone phosphate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
11
-
D-glyceraldehyde 3-phosphate mutant E168D, pH 7.4, 25°C Trypanosoma brucei
750
-
D-glyceraldehyde 3-phosphate mutant C15A in complex with mutant E168D of Trypanosoma brucei, pH 7.4, 25°C Trypanosoma cruzi
750
-
D-glyceraldehyde 3-phosphate mutant E168D in complex with mutant C15A of Trypanosoma cruzi, pH 7.4, 25°C Trypanosoma brucei
833
-
D-glyceraldehyde 3-phosphate in complex with mutant C15A of Trypanosoma cruzi enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C Trypanosoma brucei
833
-
D-glyceraldehyde 3-phosphate mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, after modification by methylmethane thiosulfonate, pH 7.4, 25°C Trypanosoma cruzi
2170
-
D-glyceraldehyde 3-phosphate in complex with mutant C15A of Trypanosoma cruzi enzyme, pH 7.4, 25°C Trypanosoma brucei
2170
-
D-glyceraldehyde 3-phosphate mutant C15A in complex with intact monomer from Trypanosoma brucei enzyme, pH 7.4, 25°C Trypanosoma cruzi
2670
-
D-glyceraldehyde 3-phosphate mutant C15A, pH 7.4, 25°C Trypanosoma cruzi
4500
-
D-glyceraldehyde 3-phosphate wild-type, pH 7.4, 25°C Trypanosoma cruzi
5000
-
D-glyceraldehyde 3-phosphate in complex with monomer from Trypanosoma brucei, pH 7.4, 25°C Trypanosoma cruzi
5000
-
D-glyceraldehyde 3-phosphate in complex with monomer from Trypanosoma cruzi, pH 7.4, 25°C Trypanosoma brucei
5170
-
D-glyceraldehyde 3-phosphate wild-type, pH 7.4, 25°C Trypanosoma brucei