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Literature summary for 1.6.2.4 extracted from

  • Munro, A.W.; Noble, M.A.; Robledo, L.; Daff, S.N.; Chapman, S.K.
    Determination of the redox properties of human NADPH-cytochrome P450 reductase (2003), Biochemistry, 40, 1956-1963.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
two different domains separately expressed in Escherichia coli BL21(DE3) Homo sapiens

General Stability

General Stability Organism
FAD-domains tends to form aggregates and precipitates upon storage at -20°C Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferricytochrome P450 + NADPH Homo sapiens involved in drug metabolism 2 ferrocytochrome P450 + NADP+ + H+
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Storage Stability

Storage Stability Organism
-20°C, 50 mM Tris/HCl, pH 7.25, 1 mM EDTA, 50% glycerol, enzyme stored for less than 1 month prior to use Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome P450 + NADPH involved in drug metabolism Homo sapiens 2 ferrocytochrome P450 + NADP+ + H+
-
?

Synonyms

Synonyms Comment Organism
NADPH-cytochrome P450 reductase
-
Homo sapiens
NADPH-ferrihemoprotein reductase
-
Homo sapiens
NADPH:ferrihemoprotein oxidoreductase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD together with FMN Homo sapiens
FMN together with FAD Homo sapiens
NADPH
-
Homo sapiens