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Literature summary for 5.3.1.1 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
Search for more literature for 5.3.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Inhibitors

Inhibitors Comment Organism Structure
2-Phosphoglycolate
-
 Trypanosoma brucei
AsO43-
-
 Trypanosoma brucei

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei P04789
-
-

Reaction

Reaction Comment Organism Reaction ID
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
a

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Ki Value [mM]

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