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Literature summary 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

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.2.2 0.045
-
 enol-oxaloacetate enzyme form OAT-1 Bos taurus
5.3.2.2 0.068
-
 keto-oxaloacetate enzyme form OAT-1 Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.3.2.2 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.2.2 37000
-
 enzyme form OAT-1, gel filtration Bos taurus
5.3.2.2 80000
-
 enzyme form OAT-2, gel filtration Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
5.3.2.2 Bos taurus
-
-
-

Purification (Commentary)

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.3.2.2 heart
-
 Bos taurus
-

Storage Stability

EC Number Storage Stability Organism
5.3.2.2 0°C, oxaloacetate tautomerase-1 is quite stable for several days Bos taurus
5.3.2.2 0°C, oxaloacetate tautomerase-2 gradually loses activity within several days Bos taurus

Substrates and Products (Substrate)

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

Subunits

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.2.2 26.7
-
 enol-oxaloacetate enzyme form OAT-2, 25°C, pH 9.0 Bos taurus
5.3.2.2 45.7
-
 enol-oxaloacetate enzyme form OAT-1, 25°C, pH 9.0 Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.2.2 8.5 10 oxaloacetate tautomerase-1 Bos taurus
5.3.2.2 9
-
 oxaloacetate tautomerase-2 Bos taurus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.3.2.2 7 10 pH 7.0: about 50% of maximal activity, pH 8.5-10.0: maximal activity, oxaloacetate tautomerase-1 Bos taurus
5.3.2.2 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