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Literature summary extracted from

  • Chu, J.; Kimura, T.
    Studies on adrenal steroid hydroxylases. Molecular and catalytic properties of adrenodoxin reductase (a flavoprotein) (1973), J. Biol. Chem., 248, 2089-2094.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.6 0.00182
-
NADPH in sodium phosphate buffer, pH 7.5, temperature not specified in the publication Bos taurus
1.18.1.6 5.56
-
NADH in sodium phosphate buffer, pH 7.5, temperature not specified in the publication Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.1.6 54000
-
gel filtration Bos taurus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.6 Sephadex G-100 gel filtration and DEAE-cellulose column chromatography Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.18.1.6 adrenal gland
-
Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.6 oxidized adrenodoxin + NADH + H+ the enzyme has low affinity for NADH Bos taurus reduced adrenodoxin + NAD+
-
?
1.18.1.6 oxidized adrenodoxin + NADPH + H+ best substrate combination Bos taurus reduced adrenodoxin + NADP+
-
?

Subunits

EC Number Subunits Comment Organism
1.18.1.6 monomer 1 * 54000, SDS-PAGE Bos taurus

Synonyms

EC Number Synonyms Comment Organism
1.18.1.6 adrenodoxin reductase
-
Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.6 FAD the enzyme contains 1 mol FAD per mole enzyme Bos taurus