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Literature summary for 5.3.2.2 extracted from

  • Belikova, Y.O.; Burov, V.I.; Vinogradov, A.D.
    Isolation and properties of oxaloacetate keto-enol tautomerases from bovine heart mitochondria (1988), Biochim. Biophys. Acta, 936, 10-19.
    View publication on PubMed

General Stability

General Stability Organism
oxaloacetate tautomerase-1 resists freezing and thawing when dissolved in potassium phosphate buffer, pH 7.8 Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
diphosphate enzyme form OAT-2 is inhibited, enzyme form OAT-1 not Bos taurus
Maleate
-
Bos taurus
malonate enzyme form OAT-2 is inhibited, enzyme form OAT-1 not Bos taurus
oxalate
-
Bos taurus
Oxaloacetic acid diethylester enzyme form OAT-1 is inhibited, enzyme form OAT-2 not Bos taurus
phenylpyruvate enzyme form OAT-2 is inhibited, enzyme form OAT-1 not Bos taurus
phosphoenolpyruvate enzyme form OAT-2 is inhibited, enzyme form OAT-1 not Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.045
-
enol-oxaloacetate enzyme form OAT-1 Bos taurus
0.068
-
keto-oxaloacetate enzyme form OAT-1 Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial matrix about 30% of the tautomerase activity in the matrix are represented by oxaloacetate tautomerase-1 and about 70% by oxaloacetate tautomerase-2 Bos taurus 5759
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
enzyme form OAT-1, gel filtration Bos taurus
80000
-
enzyme form OAT-2, gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
enzyme form OAT-1 and enzyme form OAT-2 Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-

Storage Stability

Storage Stability Organism
0°C, oxaloacetate tautomerase-1 is quite stable for several days Bos taurus
0°C, oxaloacetate tautomerase-2 gradually loses activity within several days Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
keto-Oxaloacetate r Bos taurus Enol-oxaloacetate
-
?

Subunits

Subunits Comment Organism
monomer 1 * 37000, enzyme form OAT-1, SDS-PAGE Bos taurus
monomer 1 * 80000, enzyme form OAT-2, SDS-PAGE Bos taurus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
26.7
-
enol-oxaloacetate enzyme form OAT-2, 25°C, pH 9.0 Bos taurus
45.7
-
enol-oxaloacetate enzyme form OAT-1, 25°C, pH 9.0 Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 10 oxaloacetate tautomerase-1 Bos taurus
9
-
oxaloacetate tautomerase-2 Bos taurus

pH Range

pH Minimum pH Maximum Comment Organism
7 10 pH 7.0: about 50% of maximal activity, pH 8.5-10.0: maximal activity, oxaloacetate tautomerase-1 Bos taurus
7.7 9.5 pH 7.7: about 20% of maximal activity, pH 9.5: about 40% of maximal activity, oxaloacetate tautomerase-2 Bos taurus