BRENDA - Enzyme Database

Identification of the high-molecular-mass mitochondrial oxaloacetate keto-enol tautomerase as inactive aconitase

Belikova, Y.O.; Kotlyar, A.B.; Vinogradov, A.D.; FEBS Lett. 246, 17-20 (1989)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary
Organism
Structure
5.3.2.2
220
-
enol-oxaloacetate
enzyme form OAT-2
Bos taurus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
5.3.2.2
mitochondrial matrix
-
Bos taurus
5759
-
Metals/Ions
EC Number
Metals/Ions
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
5.3.2.2
Bos taurus
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
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
5.3.2.2
keto-Oxaloacetate
-
2878
Bos taurus
Enol-oxaloacetate
-
2878
Bos taurus
-
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
2878
Bos taurus
?
-
-
-
-
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
5.3.2.2
220
-
enol-oxaloacetate
enzyme form OAT-2
Bos taurus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
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
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
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
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
5.3.2.2
keto-Oxaloacetate
-
2878
Bos taurus
Enol-oxaloacetate
-
2878
Bos taurus
-
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
2878
Bos taurus
?
-
-
-
-