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Literature summary for 5.3.1.1 extracted from

  • Alvarez, M.; Zeelen, J.P.; Mainfroid, V.; Rentier-Delrue, F.; Martial, J.A.; Wyns, L.; Wierenga, R.K.; Maes, D.
    Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus (1998), J. Biol. Chem., 273, 2199-2206.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Moritella marina

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of the vTIM-sulfate complex and the vTIM-2-phosphoglycolate complex, at 2.7 A resolution Moritella marina
hanging drop vapor diffusion method. Crystal structure of the enzyme-sulfate complex and the enzyme-2-phosphoglycolate complex at a 2.7 A resolution Moritella marina

Protein Variants

Protein Variants Comment Organism
A238S mutant enzyme A238S has a higher thermal stability than the wild-type enzyme. The turnover number of the mutant enzyme is somewhat lower than that observed for the wild-type enzyme, the Km-value for D-glyceraldehyde 2-phosphate is somewhat higher Moritella marina
A238S catalytic efficiency of the mutant enzyme is somewhat reduced, and its stability is considerably increased. The half-life at 25°C is 27 min compared to 10 min for the wild-type enzyme Moritella marina

Inhibitors

Inhibitors Comment Organism Structure
2-Phosphoglycolate
-
Escherichia coli
2-Phosphoglycolate
-
Moritella marina

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.03
-
D-glyceraldehyde 3-phosphate pH 7.6, wild-type enzyme Escherichia coli
1.9
-
D-glyceraldehyde 3-phosphate wild-type enzyme Moritella marina
1.9
-
D-glyceraldehyde 3-phosphate pH 7.6, wild-type enzyme Moritella marina
4.8
-
D-glyceraldehyde 3-phosphate mutant A238S Moritella marina
4.8
-
D-glyceraldehyde 3-phosphate pH 7.6, mutant enzyme A238S Moritella marina

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Moritella marina
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzyme A238S Moritella marina

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glyceraldehyde 3-phosphate
-
Escherichia coli Glycerone phosphate
-
?
D-Glyceraldehyde 3-phosphate
-
Moritella marina Glycerone phosphate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10
-
half-life of wild-type enzyme: 58 min Moritella marina
25
-
wild-type enzyme, half-life: 10 min Moritella marina
25
-
mutant A238S, half-life: 27 min Moritella marina
25
-
half-life of wild-type enzyme: 10 min, half-life of mutant enzyme A238S: 27 min Moritella marina

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4667
-
D-glyceraldehyde 3-phosphate pH 7.6, mutant enzyme A238S Moritella marina
4670
-
D-glyceraldehyde 3-phosphate mutant A238S Moritella marina
4670
-
D-glyceraldehyde 3-phosphate pH 7.6, mutant enzyme A238S Moritella marina
7000
-
D-glyceraldehyde 3-phosphate wild type enzyme Moritella marina
7000
-
D-glyceraldehyde 3-phosphate pH 7.6, wild-type enzyme Moritella marina
9000
-
D-glyceraldehyde 3-phosphate pH 7.6, wild-type enzyme Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6
-
2-Phosphoglycolate
-
Escherichia coli
89
-
2-Phosphoglycolate pH 7.6, wild-type enzyme Moritella marina
101
-
2-Phosphoglycolate pH 7.6, mutant enzyme A238S Moritella marina