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Literature summary for 4.2.3.3 extracted from

  • Hopper, D.J.; Cooper, R.A.
    The purification and properties of Escherichia coli methylglyoxal synthase (1972), Biochem. J., 128, 321-329.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
dihydroxyacetone phosphate or bovine serum albumin stabilizes Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
3-phosphoglycerate
-
Escherichia coli
arsenate
-
Escherichia coli
diphosphate
-
Escherichia coli
phosphate
-
Escherichia coli
phosphoenolpyruvate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.47
-
dihydroxyacetone phosphate
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
67000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dihydroxyacetone phosphate Escherichia coli the enzyme plays an important role in the catabolism of the triose phosphates ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
K 12 strain CA244
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydroxyacetone phosphate
-
Escherichia coli methylglyoxal + phosphate
-
?
dihydroxyacetone phosphate the enzyme plays an important role in the catabolism of the triose phosphates Escherichia coli ?
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
1 min, complete inactivation Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Escherichia coli