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Literature summary extracted from

  • Casteleijn, M.G.; Alahuhta, M.; Groebel, K.; El-Sayed, I.; Augustyns, K.; Lambeir, A.M.; Neubauer, P.; Wierenga, R.K.
    Functional role of the conserved active site proline of triosephosphate isomerase (2006), Biochemistry, 45, 15483-15494.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.1 mutant P168A, with and without 2-phosphoglycolate. Phosphate moiety of 2-phosphoglycolate is bound similarly as in wild-type, but interactions of the carboxylic acid moiety with the side chain of catalytic Glu167 differ Trypanosoma brucei

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.1 P168A mutation beside catalytic residue Glu167. Mutant turnover number is 50fold reduced, Km value is 2fold reduced Trypanosoma brucei

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.1 2-Phosphoglycolate
-
Trypanosoma brucei
5.3.1.1 AsO43-
-
Trypanosoma brucei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.1 0.16
-
D-glyceraldehyde 3-phosphate mutant P168A, 25°C, pH 7.6 Trypanosoma brucei
5.3.1.1 0.26
-
D-glyceraldehyde 3-phosphate wild-type, 25°C, pH 7.6 Trypanosoma brucei
5.3.1.1 0.5
-
dihydroxyacetone phosphate mutant P168A, 25°C, pH 7.6 Trypanosoma brucei
5.3.1.1 0.9
-
dihydroxyacetone phosphate wild-type, 25°C, pH 7.6 Trypanosoma brucei

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.1 Trypanosoma brucei P04789
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.3.1.1 D-Glyceraldehyde 3-phosphate = glycerone phosphate upon binding of ligand, the side chain of Glu167 flips from the inactive swung-out to the active swung-in conformation. A concerted movement of loop 6 and loop 7 from unliganded-open to liganded-closed is facilitated by the interactions of the phosphate moiety with loop 7. Rotation of the Gly211-Gly212 peptide plane of 90° is involved in this concerted movement Trypanosoma brucei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.1 D-glyceraldehyde 3-phosphate
-
Trypanosoma brucei dihydroxyacetone phosphate
-
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Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.1 19
-
dihydroxyacetone phosphate mutant P168A, 25°C, pH 7.6 Trypanosoma brucei
5.3.1.1 60
-
D-glyceraldehyde 3-phosphate mutant P168A, 25°C, pH 7.6 Trypanosoma brucei
5.3.1.1 645
-
dihydroxyacetone phosphate wild-type, 25°C, pH 7.6 Trypanosoma brucei
5.3.1.1 3570
-
D-glyceraldehyde 3-phosphate wild-type, 25°C, pH 7.6 Trypanosoma brucei

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.3.1.1 0.05
-
2-Phosphoglycolate wild-type, 25°C, pH 7.6 Trypanosoma brucei
5.3.1.1 0.3
-
2-Phosphoglycolate mutant P168A, 25°C, pH 7.6 Trypanosoma brucei
5.3.1.1 4.9
-
AsO43- wild-type, 25°C, pH 7.6 Trypanosoma brucei
5.3.1.1 5.8
-
AsO43- mutant P168A, 25°C, pH 7.6 Trypanosoma brucei