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Literature summary 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)

EC Number Cloned (Comment) Organism
5.3.1.1
-
 Helicobacter pylori

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.1 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

EC Number Protein Variants Comment Organism
5.3.1.1 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
5.3.1.1 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
5.3.1.1 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
5.3.1.1 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.1 2.49
-
 D-glyceraldehyde 3-phosphate mutant D213A, pH 7.5, 25°C Helicobacter pylori
5.3.1.1 3.27
-
 D-glyceraldehyde 3-phosphate mutant D213Q, pH 7.5, 25°C Helicobacter pylori
5.3.1.1 3.46
-
 D-glyceraldehyde 3-phosphate wild-type, pH 7.5, 25°C Helicobacter pylori
5.3.1.1 3.56
-
 D-glyceraldehyde 3-phosphate mutant K183S, pH 7.5, 25°C Helicobacter pylori
5.3.1.1 9.09
-
 D-glyceraldehyde 3-phosphate mutant K183A, pH 7.5, 25°C Helicobacter pylori

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.1 28108
-
 2 * 28108, mass spectrometry Helicobacter pylori
5.3.1.1 56000
-
 gel filtration Helicobacter pylori

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.1 Helicobacter pylori P56076
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.1 recombinant enzyme Helicobacter pylori

Substrates and Products (Substrate)

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

Subunits

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.1 1470
-
 D-glyceraldehyde 3-phosphate wild-type, pH 7.5, 25°C Helicobacter pylori
5.3.1.1 1570
-
 D-glyceraldehyde 3-phosphate mutant D213A, pH 7.5, 25°C Helicobacter pylori
5.3.1.1 1830
-
 D-glyceraldehyde 3-phosphate mutant D213Q, pH 7.5, 25°C Helicobacter pylori
5.3.1.1 2000
-
 D-glyceraldehyde 3-phosphate mutant K183S, pH 7.5, 25°C Helicobacter pylori
5.3.1.1 2330
-
 D-glyceraldehyde 3-phosphate mutant K183A, pH 7.5, 25°C Helicobacter pylori