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Literature summary for 1.18.1.6 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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
adrenal gland
-
Bos taurus
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
adrenodoxin reductase
-
Bos taurus

Cofactor

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