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Literature summary extracted from

  • Vinogradov, A.D.; Kotlyar, A.B.; Burov, V.I.; Belikova, Y.O.
    Regulation of succinate dehydrogenase and tautomerization of oxaloacetate (1989), Adv. Enzyme Regul., 28, 271-280.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment 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 Comment 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 Comment 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 Comment 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 Comment 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] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
?
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 UniProt Comment 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 Comment Organism Textmining
1.3.5.1 heart
-
Bos taurus
-
5.3.2.2 heart
-
Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 D-malate + N,N,N',N'-tetramethyl 4-phenylenediamine
-
Bos taurus oxaloacetate + reduced N,N,N',N'-tetramethyl 4-phenylenediamine
-
r
1.3.5.1 additional information L- or D-malate oxidation 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 Bos taurus ?
-
?
1.3.5.1 succinate + ubiquinone
-
Bos taurus fumarate + ubiquinol
-
?
1.3.5.1 ubiquinone-1 + L-malate
-
Bos taurus ?
-
?
5.3.2.2 keto-Oxaloacetate r Bos taurus Enol-oxaloacetate
-
?
5.3.2.2 additional information OAT-2 catalyzes aconitase reaction after treatment with Fe2+ 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 Bos taurus ?
-
?

Subunits

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.2.2 40
-
enzyme form OAT-1: no inactivation Bos taurus
5.3.2.2 40
-
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 Comment 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