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Literature summary for 1.18.1.6 extracted from

  • Fujii, S.; Nonaka, Y.; Okamoto, M.; Miura, R.
    On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase as studied by (1991), J. Biochem., 109, 144-149.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2',5'-ADP 2',5'-ADP inhibits the NADPH-ferricyanide reductase activity of the enzyme competitively Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Bos taurus 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
x * 54000, SDS-PAGE Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
adrenal cortex
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADPH the enzyme also has NADPH-ferricyanide activity Bos taurus 2 ferrocyanide + NADP+ + H+
-
?

Subunits

Subunits Comment Organism
? x * 54000, SDS-PAGE Bos taurus

Synonyms

Synonyms Comment Organism
AdR
-
Bos taurus
adrenodoxin reductase
-
Bos taurus
NADPH-adrenodoxin reductase
-
Bos taurus
NADPH:adrenal ferredoxin oxidoreductase
-
Bos taurus

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme contains one molecule of FAD noncovalently bound to a subunit Bos taurus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.28
-
2',5'-ADP at 25°C in 50 mM potassium phosphate, pH 7.4 Bos taurus