BRENDA - Enzyme Database show
show all sequences of 5.3.2.2

Regulation of succinate dehydrogenase and tautomerization of oxaloacetate

Vinogradov, A.D.; Kotlyar, A.B.; Burov, V.I.; Belikova, Y.O.; Adv. Enzyme Regul. 28, 271-280 (1989)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Acid-labile sulfur
enzyme form OAT-2 contains 2 atoms of acid-labile sulfur
Bos taurus
Inhibitors
Inhibitors
Commentary
Organism
Structure
diphosphate
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
Fluorocitrate
inhibition of OAT-2, tautomerase reaction and aconitase reaction
Bos taurus
Maleate
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
NEM
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
oxalate
enzyme form OAT-1 is inhibited, enzyme form OAT-2 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
220
-
enol-oxaloacetate
enzyme form OAT-2
Bos taurus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrial matrix
-
Bos taurus
5759
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe
enzyme form OAT-2 contains 2 atoms of non-heme Fe per mol
Bos taurus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37000
-
enzyme form OAT-1
Bos taurus
80000
-
enzyme form OAT-2
Bos taurus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bos taurus
significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
enzyme forms OAT-1 and OAT-2
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
heart
-
Bos taurus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
keto-Oxaloacetate
r
2877
Bos taurus
Enol-oxaloacetate
-
2877
Bos taurus
-
additional information
OAT-2 catalyzes aconitase reaction after treatment with Fe2+
2877
Bos taurus
?
-
-
-
-
additional information
significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
2877
Bos taurus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 37000, enzyme form OAT-1; 1 * 80000, enzyme form OAT-2
Bos taurus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
enzyme form OAT-1: no inactivation; enzyme form OAT-2: t1/2: about 15 min
Bos taurus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.58
-
keto-oxaloacetate
enzyme form OAT-1, 25°C, pH 9.0
Bos taurus
26.7
-
enol-oxaloacetate
enzyme form OAT-2, 25°C, pH 9.0
Bos taurus
45
-
enol-oxaloacetate
enzyme form OAT-1, 25°C, pH 9.0
Bos taurus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Acid-labile sulfur
enzyme form OAT-2 contains 2 atoms of acid-labile sulfur
Bos taurus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
diphosphate
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
Fluorocitrate
inhibition of OAT-2, tautomerase reaction and aconitase reaction
Bos taurus
Maleate
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
NEM
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
oxalate
enzyme form OAT-1 is inhibited, enzyme form OAT-2 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
220
-
enol-oxaloacetate
enzyme form OAT-2
Bos taurus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrial matrix
-
Bos taurus
5759
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe
enzyme form OAT-2 contains 2 atoms of non-heme Fe per mol
Bos taurus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37000
-
enzyme form OAT-1
Bos taurus
80000
-
enzyme form OAT-2
Bos taurus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bos taurus
significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
heart
-
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
2877
Bos taurus
Enol-oxaloacetate
-
2877
Bos taurus
-
additional information
OAT-2 catalyzes aconitase reaction after treatment with Fe2+
2877
Bos taurus
?
-
-
-
-
additional information
significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
2877
Bos taurus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 37000, enzyme form OAT-1; 1 * 80000, enzyme form OAT-2
Bos taurus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
-
enzyme form OAT-1: no inactivation; enzyme form OAT-2: t1/2: about 15 min
Bos taurus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.58
-
keto-oxaloacetate
enzyme form OAT-1, 25°C, pH 9.0
Bos taurus
26.7
-
enol-oxaloacetate
enzyme form OAT-2, 25°C, pH 9.0
Bos taurus
45
-
enol-oxaloacetate
enzyme form OAT-1, 25°C, pH 9.0
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
2
-
2
-
-
2
-
-
1
-
-
2
-
2
1
1
-
-
-
2
2
2
-
-
-
-
-
-
-
-
-
-
-
1
-
7
-
2
2
-
2
-
-
-
-
1
-
2
-
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
-
-
-
-
-
-
-
-
9
-
-
-
-
5
-
-
-
-
-
8
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
8
-
-
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
-
-
-
-
-
-
-