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Literature summary for 4.2.3.3 extracted from

  • Tsai, P.K.; Gracy, R.W.
    Isolation and characterization of crystalline methylglyoxal synthetase from Proteus vulgaris (1976), J. Biol. Chem., 251, 364-367.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Proteus vulgaris

Inhibitors

Inhibitors Comment Organism Structure
phosphate
-
 Proteus vulgaris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.19
-
 dihydroxyacetone phosphate enzyme form II Proteus vulgaris
0.23
-
 dihydroxyacetone phosphate enzyme form I Proteus vulgaris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
 2 * 66000, SDS-PAGE Proteus vulgaris
135000
-
 gel filtration Proteus vulgaris

Organism

Organism UniProt Comment Textmining
Proteus vulgaris
-
 two enzyme forms, may be post-translational modifications or conformational changes
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
9.43
-
-
 Proteus vulgaris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydroxyacetone phosphate strictly specific for Proteus vulgaris methylglyoxal + phosphate
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 66000, SDS-PAGE Proteus vulgaris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
-
 Proteus vulgaris

pH Range

pH Minimum pH Maximum Comment Organism
5.6 8.3 50% of maximal activity at pH 5.6 and at pH 8.3 Proteus vulgaris