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show all sequences of 5.3.2.2

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
General Stability
Organism
oxaloacetate tautomerase-1 resists freezing and thawing when dissolved in potassium phosphate buffer, pH 7.8
Bos taurus
Inhibitors
Inhibitors
Commentary
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
Commentary
Organism
Structure
0.045
-
enol-oxaloacetate
enzyme form OAT-1
Bos taurus
0.068
-
keto-oxaloacetate
enzyme form OAT-1
Bos taurus
Localization
Localization
Commentary
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]
Commentary
Organism
37000
-
enzyme form OAT-1, gel filtration
Bos taurus
80000
-
enzyme form OAT-2, gel filtration
Bos taurus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
-
-
Purification (Commentary)
Commentary
Organism
enzyme form OAT-1 and enzyme form OAT-2
Bos taurus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
heart
-
Bos taurus
-
Storage Stability
Storage Stability
Organism
0C, oxaloacetate tautomerase-1 is quite stable for several days
Bos taurus
0C, oxaloacetate tautomerase-2 gradually loses activity within several days
Bos taurus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
keto-Oxaloacetate
r
2879
Bos taurus
Enol-oxaloacetate
-
2879
Bos taurus
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 37000, enzyme form OAT-1, SDS-PAGE; 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
Commentary
Organism
Structure
26.7
-
enol-oxaloacetate
enzyme form OAT-2, 25C, pH 9.0
Bos taurus
45.7
-
enol-oxaloacetate
enzyme form OAT-1, 25C, pH 9.0
Bos taurus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
10
oxaloacetate tautomerase-1
Bos taurus
9
-
oxaloacetate tautomerase-2
Bos taurus
pH Range
pH Minimum
pH Maximum
Commentary
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
General Stability (protein specific)
General Stability
Organism
oxaloacetate tautomerase-1 resists freezing and thawing when dissolved in potassium phosphate buffer, pH 7.8
Bos taurus
Inhibitors (protein specific)
Inhibitors
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.045
-
enol-oxaloacetate
enzyme form OAT-1
Bos taurus
0.068
-
keto-oxaloacetate
enzyme form OAT-1
Bos taurus
Localization (protein specific)
Localization
Commentary
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] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37000
-
enzyme form OAT-1, gel filtration
Bos taurus
80000
-
enzyme form OAT-2, gel filtration
Bos taurus
Purification (Commentary) (protein specific)
Commentary
Organism
enzyme form OAT-1 and enzyme form OAT-2
Bos taurus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
heart
-
Bos taurus
-
Storage Stability (protein specific)
Storage Stability
Organism
0C, oxaloacetate tautomerase-1 is quite stable for several days
Bos taurus
0C, oxaloacetate tautomerase-2 gradually loses activity within several days
Bos taurus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
keto-Oxaloacetate
r
2879
Bos taurus
Enol-oxaloacetate
-
2879
Bos taurus
-
Subunits (protein specific)
Subunits
Commentary
Organism
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)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
26.7
-
enol-oxaloacetate
enzyme form OAT-2, 25C, pH 9.0
Bos taurus
45.7
-
enol-oxaloacetate
enzyme form OAT-1, 25C, pH 9.0
Bos taurus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
10
oxaloacetate tautomerase-1
Bos taurus
9
-
oxaloacetate tautomerase-2
Bos taurus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
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
Other publictions for EC 5.3.2.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
2877
Vinogradov
Regulation of succinate dehydr ...
Bos taurus
Adv. Enzyme Regul.
28
271-280
1989
1
-
-
-
-
-
5
3
1
1
2
1
-
1
-
-
-
-
-
1
-
-
3
1
-
-
1
3
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
5
-
3
1
1
2
1
-
-
-
-
-
1
-
-
3
1
-
-
1
3
-
-
-
-
-
-
-
-
-
-
2878
Belikova
Identification of the high-mol ...
Bos taurus
FEBS Lett.
246
17-20
1989
-
-
-
-
-
-
4
1
2
1
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
1
2
1
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2879
Belikova
Isolation and properties of ox ...
Bos taurus
Biochim. Biophys. Acta
936
10-19
1988
-
-
-
-
-
1
7
2
1
-
2
-
-
2
-
-
1
-
-
1
-
2
1
1
-
-
-
2
2
2
-
-
-
-
-
-
-
-
-
-
-
1
-
7
-
2
1
-
2
-
-
-
-
1
-
1
-
2
1
1
-
-
-
2
2
2
-
-
-
-
-
-
-
-
2880
Belikova
Oxidation of malate by mitocho ...
Bos taurus
Biochim. Biophys. Acta
936
1-9
1988
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2876
Johnson
Stereochemistry and function o ...
Sus scrofa
J. Biol. Chem.
261
4535-4541
1986
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
1
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2875
Wesenberg
Localization of oxalacetate ke ...
Rattus norvegicus, Sus scrofa
Can. J. Biochem.
54
233-237
1976
-
-
-
-
-
-
-
-
6
-
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2874
Annett
Oxalacetate keto-enol tautomer ...
Sus scrofa
J. Biol. Chem.
244
2059-2067
1969
-
-
-
-
-
-
17
-
-
-
-
-
-
1
-
-
1
-
-
1
1
-
1
-
-
-
1
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
17
-
-
-
-
-
-
-
-
-
1
-
1
1
-
1
-
-
-
1
-
-
-
4
-
-
-
-
-
-
-