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Literature summary for 5.3.1.1 extracted from

  • Chu, C.H.; Lai, Y.J.; Huang, H.; Sun, Y.J.
    Kinetic and structural properties of triosephosphate isomerase from Helicobacter pylori (2008), Proteins, 71, 396-406.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Helicobacter pylori

Crystallization (Commentary)

Crystallization (Comment) Organism
determination by molecular replacement, at 2.3 A resolution and in the closed state. Phosphate acts as a competitive inhibitor and occupies the binding pocket. Binding pocket has a very stable conformation even without a substrate Helicobacter pylori

Protein Variants

Protein Variants Comment Organism
D213A Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type Helicobacter pylori
D213Q Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type Helicobacter pylori
K183A Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type Helicobacter pylori
K183S Residue putatively involved in a highly conserved salt bridge lacking in Helicobacter pylori enzyme. Kinetics and isomerization activity similar to wild-type Helicobacter pylori

Inhibitors

Inhibitors Comment Organism Structure
phosphate competitive, occupies the substrate binding pocket Helicobacter pylori

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.49
-
D-glyceraldehyde 3-phosphate mutant D213A, pH 7.5, 25°C Helicobacter pylori
3.27
-
D-glyceraldehyde 3-phosphate mutant D213Q, pH 7.5, 25°C Helicobacter pylori
3.46
-
D-glyceraldehyde 3-phosphate wild-type, pH 7.5, 25°C Helicobacter pylori
3.56
-
D-glyceraldehyde 3-phosphate mutant K183S, pH 7.5, 25°C Helicobacter pylori
9.09
-
D-glyceraldehyde 3-phosphate mutant K183A, pH 7.5, 25°C Helicobacter pylori

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28108
-
2 * 28108, mass spectrometry Helicobacter pylori
56000
-
gel filtration Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori P56076
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Helicobacter pylori

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 28108, mass spectrometry Helicobacter pylori

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1470
-
D-glyceraldehyde 3-phosphate wild-type, pH 7.5, 25°C Helicobacter pylori
1570
-
D-glyceraldehyde 3-phosphate mutant D213A, pH 7.5, 25°C Helicobacter pylori
1830
-
D-glyceraldehyde 3-phosphate mutant D213Q, pH 7.5, 25°C Helicobacter pylori
2000
-
D-glyceraldehyde 3-phosphate mutant K183S, pH 7.5, 25°C Helicobacter pylori
2330
-
D-glyceraldehyde 3-phosphate mutant K183A, pH 7.5, 25°C Helicobacter pylori