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Literature summary for 4.2.3.3 extracted from

  • Saadat, D.; Harrison, D.H.T.
    Identification of catalytic bases in the active site of Escherichia coli methylglyoxal synthase: cloning, expression, and functional characterization of conserved aspartic acid residues (1998), Biochemistry, 37, 10074-10086.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
D101E reduced ratio of turnover-numer:Km-value by about 10000fold compared to the wild-type enzyme Escherichia coli
D101N reduced ratio of turnover-numer:Km-value by about 10000fold compared to the wild-type enzyme Escherichia coli
D71E reduced ratio of turnover-numer:Km-value by about 1000fold compared to the wild-type enzyme Escherichia coli
D71N reduced ratio of turnover-numer:Km-value by about 1000fold compared to the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-phosphoglycerate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
dihydroxyacetone phosphate wild-type enzyme Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
4 * 17000, SDS-PAGE Escherichia coli
67000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
wild-type enzyme and mutant enzymes D71E, D71N, D101E and D101N
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer 4 * 17000, SDS-PAGE Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
220
-
dihydroxyacetone phosphate wild-type enzyme Escherichia coli