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Literature summary for 5.3.1.1 extracted from

  • Peimbert, M.; Dominguez-Ramirez, L.; Fernandez-Velasco, D.A.
    Hydrophobic repacking of the dimer interface of triosephosphate isomerase by in silico design and directed evolution (2008), Biochemistry, 47, 5556-5564.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K17A/Y46A/D48F/Q82A/D85S mutation of residues in the dimer interface of enzyme Saccharomyces cerevisiae
K17L/Y46F/D48F/Q82F/D85L mutation of residues in the dimer interface of enzyme. Decrease in catalytic efficiency by 4 orders of magnitude Saccharomyces cerevisiae
K17L/Y46F/D48Y/Q82A/D85A mutation of residues in the dimer interface of enzyme. Decrease in catalytic efficiency by 4 orders of magnitude Saccharomyces cerevisiae
K17P/Y46A/D48L/Q82T/D85A mutation of residues in the dimer interface of enzyme Saccharomyces cerevisiae
additional information mutation of five residues in the dimer interface of enzyme. Obtained proteins are soluble, dimeric, and compact. Proteins obtained from direct evolution experiments show wild-type-like catalytic activity, while their stability is decreased. In silico-designed proteins are very stable dimers that bind substrate with a wild-type-like Km value, albeit they exhibit a very low kcat Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.09
-
D-glyceraldehyde 3-phosphate mutant K17A/Y46A/D48F/Q82A/D85S , pH 7.4, 25°C Saccharomyces cerevisiae
1.2
-
D-glyceraldehyde 3-phosphate mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25°C Saccharomyces cerevisiae
1.26
-
D-glyceraldehyde 3-phosphate mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25°C Saccharomyces cerevisiae
1.4
-
D-glyceraldehyde 3-phosphate wild-type, pH 7.4, 25°C Saccharomyces cerevisiae
2.44
-
D-glyceraldehyde 3-phosphate mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25°C Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P00942
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.69
-
D-glyceraldehyde 3-phosphate mutant K17L/Y46F/D48F/Q82F/D85L, pH 7.4, 25°C Saccharomyces cerevisiae
1.04
-
D-glyceraldehyde 3-phosphate mutant K17L/Y46F/D48Y/Q82A/D85A, pH 7.4, 25°C Saccharomyces cerevisiae
4160
-
D-glyceraldehyde 3-phosphate mutant K17P/Y46A/D48L/Q82T/D85A, pH 7.4, 25°C Saccharomyces cerevisiae
6400
-
D-glyceraldehyde 3-phosphate wild-type, pH 7.4, 25°C Saccharomyces cerevisiae
7020
-
D-glyceraldehyde 3-phosphate mutant K17A/Y46A/D48F/Q82A/D85S , pH 7.4, 25°C Saccharomyces cerevisiae