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Literature summary extracted from

  • Sagara, Y.; Wada, A.; Takata, Y.; Waterman, M.; Sekimizu, K.; Horiuchi, T.
    Direct expression of adrenodoxin reductase in Escherichia coli and the functional characterization (1993), Biol. Pharm. Bull., 16, 627-630.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.6 expressed in Escherichia coli JM109 cells Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.6 0.000016
-
 oxidized adrenodoxin recombinant enzyme, in 50 mM potassium phosphate (pH 7.4), temperature not specified in the publication Bos taurus
1.18.1.6 0.000017
-
 oxidized adrenodoxin native enzyme, in 50 mM potassium phosphate (pH 7.4), temperature not specified in the publication Bos taurus

Localization

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

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.6 adrenodoxin-Sepharose affinity column chromatography Bos taurus

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.6 oxidized adrenodoxin + NADPH + H+
-
 Bos taurus reduced adrenodoxin + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.18.1.6 AdR
-
 Bos taurus
1.18.1.6 adrenodoxin reductase
-
 Bos taurus
1.18.1.6 NADPH:adrenodoxin oxidoreductase
-
 Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.6 FAD contains 0.8 FAD per mol enzyme Bos taurus