BRENDA - Enzyme Database

Interactions of oxaloacetate with Escherichia coli fumarate reductase

Ackrell, B.A.C.; Cochran, B.; Cecchini, G.; Arch. Biochem. Biophys. 268, 26-34 (1989)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.3.5.1
cell membranes transformed with plasmid which codes for all four subunits of the fumarate reductase complex
Escherichia coli
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.3.5.1
malonate
-
Escherichia coli
1.3.5.1
N-ethylmaleimide
-
Escherichia coli
1.3.5.1
oxaloacetate
reactivation by reduction of enzyme with succinate; reactivation with anions
Escherichia coli
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.3.5.1
Escherichia coli
-
fumarate reductase
-
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.3.5.1
FAD
-
Escherichia coli
1.3.5.1
additional information
the enzyme contains iron-sulfur centers
Escherichia coli
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.3.5.1
cell membranes transformed with plasmid which codes for all four subunits of the fumarate reductase complex
Escherichia coli
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.3.5.1
FAD
-
Escherichia coli
1.3.5.1
additional information
the enzyme contains iron-sulfur centers
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.3.5.1
malonate
-
Escherichia coli
1.3.5.1
N-ethylmaleimide
-
Escherichia coli
1.3.5.1
oxaloacetate
reactivation by reduction of enzyme with succinate; reactivation with anions
Escherichia coli