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Literature summary extracted from

  • Salamanca-Pinzon, S.; Guengerich, F.
    A tricistronic human adrenodoxin reductase-adrenodoxin-cytochrome P450 27A1 vector system for substrate hydroxylation in Escherichia coli (2011), Protein Expr. Purif., 79, 231-236.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.6 coexpressed with P450 27A1 and adrenodoxin in Escherichia coli DH5alpha cells Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.1.6 52000
-
 x * 52000, SDS-PAGE Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.6 Homo sapiens
-
-
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.18.1.6 ? x * 52000, SDS-PAGE Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.18.1.6 AdR
-
 Homo sapiens
1.18.1.6 adrenodoxin reductase
-
 Homo sapiens
1.18.1.6 NADPH-adrenodoxin reductase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.6 FAD
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.18.1.6 metabolism the enzyme is the first component in the mitochondrial P450 electron transfer systems. Coexpressed P450, adrenodoxin, and adrenodoxin reductase interact catalytically and allow Escherichia coli to oxidize both cholesterol and vitamin D3 Homo sapiens