BRENDA - Enzyme Database

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
EC Number
Activating Compound
Commentary
Organism
Structure
5.3.2.2
Acid-labile sulfur
enzyme form OAT-2 contains 2 atoms of acid-labile sulfur
Bos taurus
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.3.5.1
malonate
-
Bos taurus
1.3.5.1
N-ethylmaleimide
-
Bos taurus
1.3.5.1
oxaloacetate
-
Bos taurus
5.3.2.2
diphosphate
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
5.3.2.2
Fluorocitrate
inhibition of OAT-2, tautomerase reaction and aconitase reaction
Bos taurus
5.3.2.2
Maleate
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
5.3.2.2
NEM
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
5.3.2.2
oxalate
enzyme form OAT-1 is inhibited, enzyme form OAT-2 not
Bos taurus
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.3.5.1
0.1
-
succinate
-
Bos taurus
1.3.5.1
1.5
-
D-malate
-
Bos taurus
1.3.5.1
2.2
-
L-malate
-
Bos taurus
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
5.3.2.2
220
-
enol-oxaloacetate
enzyme form OAT-2
Bos taurus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.3.5.1
mitochondrion
-
Bos taurus
5739
-
5.3.2.2
mitochondrial matrix
-
Bos taurus
5759
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
5.3.2.2
Fe
enzyme form OAT-2 contains 2 atoms of non-heme Fe per mol
Bos taurus
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
5.3.2.2
37000
-
enzyme form OAT-1
Bos taurus
5.3.2.2
80000
-
enzyme form OAT-2
Bos taurus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.3.5.1
additional information
Bos taurus
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
?
-
-
-
1.3.5.1
succinate + ubiquinone
Bos taurus
-
fumarate + ubiquinol
-
Bos taurus
?
5.3.2.2
additional information
Bos taurus
significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.3.5.1
Bos taurus
-
succinate dehydrogenase
-
5.3.2.2
Bos taurus
-
enzyme forms OAT-1 and OAT-2
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.3.5.1
heart
-
Bos taurus
-
5.3.2.2
heart
-
Bos taurus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.3.5.1
additional information
L- or D-malate oxidation
2877
Bos taurus
?
-
-
-
-
1.3.5.1
additional information
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
2877
Bos taurus
?
-
-
-
-
1.3.5.1
succinate + ubiquinone
-
2877
Bos taurus
fumarate + ubiquinol
-
2877
Bos taurus
?
1.3.5.1
ubiquinone-1 + L-malate
-
2877
Bos taurus
?
-
-
-
-
5.3.2.2
keto-Oxaloacetate
r
2877
Bos taurus
Enol-oxaloacetate
-
2877
Bos taurus
-
5.3.2.2
additional information
OAT-2 catalyzes aconitase reaction after treatment with Fe2+
2877
Bos taurus
?
-
-
-
-
5.3.2.2
additional information
significant role of enzymatic oxaloacetate tautomerization in the control of the succinate dehydrogenase activity in the mitochondrial matrix
2877
Bos taurus
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
5.3.2.2
monomer
1 * 37000, enzyme form OAT-1; 1 * 80000, enzyme form OAT-2
Bos taurus
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
5.3.2.2
40
-
enzyme form OAT-1: no inactivation; enzyme form OAT-2: t1/2: about 15 min
Bos taurus
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.3.5.1
0.142
-
L-malate
-
Bos taurus
1.3.5.1
0.283
-
D-malate
-
Bos taurus
1.3.5.1
28.3
-
succinate
-
Bos taurus
5.3.2.2
3.58
-
keto-oxaloacetate
enzyme form OAT-1, 25°C, pH 9.0
Bos taurus
5.3.2.2
26.7
-
enol-oxaloacetate
enzyme form OAT-2, 25°C, pH 9.0
Bos taurus
5.3.2.2
45
-
enol-oxaloacetate
enzyme form OAT-1, 25°C, pH 9.0
Bos taurus
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
5.3.2.2
Acid-labile sulfur
enzyme form OAT-2 contains 2 atoms of acid-labile sulfur
Bos taurus
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.3.5.1
malonate
-
Bos taurus
1.3.5.1
N-ethylmaleimide
-
Bos taurus
1.3.5.1
oxaloacetate
-
Bos taurus
5.3.2.2
diphosphate
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
5.3.2.2
Fluorocitrate
inhibition of OAT-2, tautomerase reaction and aconitase reaction
Bos taurus
5.3.2.2
Maleate
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
5.3.2.2
NEM
enzyme form OAT-2 is inhibited, enzyme form OAT-1 not
Bos taurus
5.3.2.2
oxalate
enzyme form OAT-1 is inhibited, enzyme form OAT-2 not
Bos taurus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.3.5.1
0.1
-
succinate
-
Bos taurus
1.3.5.1
1.5
-
D-malate
-
Bos taurus
1.3.5.1
2.2
-
L-malate
-
Bos taurus
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
5.3.2.2
220
-
enol-oxaloacetate
enzyme form OAT-2
Bos taurus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.3.5.1
mitochondrion
-
Bos taurus
5739
-
5.3.2.2
mitochondrial matrix
-
Bos taurus
5759
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
5.3.2.2
Fe
enzyme form OAT-2 contains 2 atoms of non-heme Fe per mol
Bos taurus
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
Bos taurus
5.3.2.2
80000
-
enzyme form OAT-2
Bos taurus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.3.5.1
additional information
Bos taurus
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
?
-
-
-
1.3.5.1
succinate + ubiquinone
Bos taurus
-
fumarate + ubiquinol
-
Bos taurus
?
5.3.2.2
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)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.3.5.1
heart
-
Bos taurus
-
5.3.2.2
heart
-
Bos taurus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.3.5.1
additional information
L- or D-malate oxidation
2877
Bos taurus
?
-
-
-
-
1.3.5.1
additional information
succinate dehydrogenase is a component of the respiratory chain and operates as a compulsory member of the Krebs cycle in mammals
2877
Bos taurus
?
-
-
-
-
1.3.5.1
succinate + ubiquinone
-
2877
Bos taurus
fumarate + ubiquinol
-
2877
Bos taurus
?
1.3.5.1
ubiquinone-1 + L-malate
-
2877
Bos taurus
?
-
-
-
-
5.3.2.2
keto-Oxaloacetate
r
2877
Bos taurus
Enol-oxaloacetate
-
2877
Bos taurus
-
5.3.2.2
additional information
OAT-2 catalyzes aconitase reaction after treatment with Fe2+
2877
Bos taurus
?
-
-
-
-
5.3.2.2
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)
EC Number
Subunits
Commentary
Organism
5.3.2.2
monomer
1 * 37000, enzyme form OAT-1; 1 * 80000, enzyme form OAT-2
Bos taurus
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
5.3.2.2
40
-
enzyme form OAT-1: no inactivation; enzyme form OAT-2: t1/2: about 15 min
Bos taurus
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.3.5.1
0.142
-
L-malate
-
Bos taurus
1.3.5.1
0.283
-
D-malate
-
Bos taurus
1.3.5.1
28.3
-
succinate
-
Bos taurus
5.3.2.2
3.58
-
keto-oxaloacetate
enzyme form OAT-1, 25°C, pH 9.0
Bos taurus
5.3.2.2
26.7
-
enol-oxaloacetate
enzyme form OAT-2, 25°C, pH 9.0
Bos taurus
5.3.2.2
45
-
enol-oxaloacetate
enzyme form OAT-1, 25°C, pH 9.0
Bos taurus