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Literature summary for 5.3.1.1 extracted from

  • Banerjee, M.; Balaram, H.; Balaram, P.
    Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations (2009), FEBS J., 276, 4169-4183.
    View publication on PubMed

Application

Application Comment Organism
additional information the glycolytic enzyme triosephosphate isomerase occupies a central position in the development of structural and mechanistic enzymology Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
W11F/W168F/Y74W site-directed mutagenesis, template is the available crystal structure of the enzyme from Giardia lamblia, which contains a Trp residue at position 47. The mutant dissociates at low protein concentrations, and exhibits considerably reduced stability in the presence of denaturants, urea and guanidinium chloride, and it shows approximately 20fold reduction in kcat at low protein concetrations compared to the wild-type enzyme, but the mutant mutant shows an enhancement of activity of 21.9fold at higher concentration range Plasmodium falciparum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27000
-
2 * 27000, gel filtration and SDS-PAGE, the active site of triosephosphate isomerase lies very close to the subunit interface, a network of key interactions spans the interacting subunits Plasmodium falciparum
54000
-
gel filtration Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q07412
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information importance of conserved residues in the vicinity of the active site that serve to position the functional K12 residue. A network of key interactions spans the interacting subunits Plasmodium falciparum ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 27000, gel filtration and SDS-PAGE, the active site of triosephosphate isomerase lies very close to the subunit interface, a network of key interactions spans the interacting subunits Plasmodium falciparum

Synonyms

Synonyms Comment Organism
TIM
-
Plasmodium falciparum
Triosephosphate isomerase
-
Plasmodium falciparum