BRENDA - Enzyme Database

Isolation and properties of oxaloacetate keto-enol tautomerases from bovine heart mitochondria

Belikova, Y.O.; Burov, V.I.; Vinogradov, A.D.; Biochim. Biophys. Acta 936, 10-19 (1988)

Data extracted from this reference:

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
Commentary
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
Commentary
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
Commentary
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]
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
5.3.2.2
Bos taurus
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
5.3.2.2
enzyme form OAT-1 and enzyme form OAT-2
Bos taurus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
5.3.2.2
heart
-
Bos taurus
-
Storage Stability
EC Number
Storage Stability
Organism
5.3.2.2
0C, oxaloacetate tautomerase-1 is quite stable for several days
Bos taurus
5.3.2.2
0C, oxaloacetate tautomerase-2 gradually loses activity within several days
Bos taurus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.3.2.2
keto-Oxaloacetate
r
2879
Bos taurus
Enol-oxaloacetate
-
2879
Bos taurus
-
Subunits
EC Number
Subunits
Commentary
Organism
5.3.2.2
monomer
1 * 37000, enzyme form OAT-1, SDS-PAGE; 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
Commentary
Organism
Structure
5.3.2.2
26.7
-
enol-oxaloacetate
enzyme form OAT-2, 25C, pH 9.0
Bos taurus
5.3.2.2
45.7
-
enol-oxaloacetate
enzyme form OAT-1, 25C, pH 9.0
Bos taurus
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
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
Commentary
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
General Stability (protein specific)
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 (protein specific)
EC Number
Inhibitors
Commentary
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] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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 (protein specific)
EC Number
Localization
Commentary
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] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
5.3.2.2
enzyme form OAT-1 and enzyme form OAT-2
Bos taurus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
5.3.2.2
heart
-
Bos taurus
-
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
5.3.2.2
0C, oxaloacetate tautomerase-1 is quite stable for several days
Bos taurus
5.3.2.2
0C, oxaloacetate tautomerase-2 gradually loses activity within several days
Bos taurus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.3.2.2
keto-Oxaloacetate
r
2879
Bos taurus
Enol-oxaloacetate
-
2879
Bos taurus
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
5.3.2.2
monomer
1 * 37000, enzyme form OAT-1, SDS-PAGE; 1 * 80000, enzyme form OAT-2, SDS-PAGE
Bos taurus
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.3.2.2
26.7
-
enol-oxaloacetate
enzyme form OAT-2, 25C, pH 9.0
Bos taurus
5.3.2.2
45.7
-
enol-oxaloacetate
enzyme form OAT-1, 25C, pH 9.0
Bos taurus
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
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 (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
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