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Literature summary extracted from

  • Belikova, Y.O.; Kotlyar, A.B.; Vinogradov, A.D.
    Identification of the high-molecular-mass mitochondrial oxaloacetate keto-enol tautomerase as inactive aconitase (1989), FEBS Lett., 246, 17-20.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.2.2 diphosphate
-
 Bos taurus
5.3.2.2 DL-isocitrate inhibits enzyme form OAT-2 Bos taurus
5.3.2.2 Fluorocitrate
-
 Bos taurus
5.3.2.2 NEM enzyme form OAT-2: irreversible loss of oxaloacetate keto-enol tautomerase activity and aconitase activity Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.2.2 220
-
 enol-oxaloacetate enzyme form OAT-2 Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.3.2.2 mitochondrial matrix
-
 Bos taurus 5759
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.2.2 Fe OAT-2 catalyzes aconitase reaction after treatment with Fe2+ under anaerobic conditions. 3Fe-4S to 4Fe-4S transformation is responsible for aconitase activation Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
5.3.2.2 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.3.2.2 heart
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.2.2 keto-Oxaloacetate
-
 Bos taurus Enol-oxaloacetate
-
 ?
5.3.2.2 additional information OAT-2 catalyzes aconitase reaction after treatment with Fe2+ under anaerobic conditions. 3Fe-4S to 4Fe-4S transformation is responsible for aconitase activation. The same catalytic site is involved in the oxaloacetate tautomerase and the aconitase reaction Bos taurus ?
-
 ?