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Literature summary for 4.2.3.3 extracted from

  • Mohammadi, M.; Zareian, S.; Khajeh, K.
    Conversion of non-allosteric methylglyoxal synthase into a homotropic allosteric enzyme by C-terminal deletion (2014), J. Mol. Catal. B, 107, 95-99.
No PubMed abstract available
Search for more literature for 4.2.3.3

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information mutant lacking ten amino acids from C-terminal tail shows homotropic cooperative behavior in presence of dihydroxyacetone phosphate and is not only more flexible but also less stable compared to wild-type Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.35
-
 dihydroxyacetone phosphate mutant lacking ten amino acids from C-terminal tail, Hill coefficient 1.3, pH 7.0, 60°C Escherichia coli
2.74
-
 dihydroxyacetone phosphate wild-type, Hill coefficient 1, pH 7.0, 60°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydroxyacetone phosphate
-
 Escherichia coli methylglyoxal + phosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1
-
 dihydroxyacetone phosphate mutant lacking ten amino acids from C-terminal tail, Hill coefficient 1.3, pH 7.0, 60°C Escherichia coli
23.1
-
 dihydroxyacetone phosphate wild-type, Hill coefficient 1, pH 7.0, 60°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.6
-
 dihydroxyacetone phosphate mutant lacking ten amino acids from C-terminal tail, Hill coefficient 1.3, pH 7.0, 60°C Escherichia coli
8.4
-
 dihydroxyacetone phosphate wild-type, Hill coefficient 1, pH 7.0, 60°C Escherichia coli