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Literature summary for 1.6.2.4 extracted from

  • Ivanov, A.S.; Gnedenko, O.V.; Molnar, A.A.; Archakov, A.I.; Podust, L.M.
    FMN binding site of yeast NADPH-cytochrome P450 reductase exposed at the surface is highly specific (2010), ACS Chem. Biol., 5, 767-776.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.6.2.4

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferricytochrome P450 + NADPH Saccharomyces cerevisiae
-
 2 ferrocytochrome P450 + NADP+ + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome P450 + NADPH
-
 Saccharomyces cerevisiae 2 ferrocytochrome P450 + NADP+ + H+
-
 ?

Synonyms

Synonyms Comment Organism
CPR
-
 Saccharomyces cerevisiae
NADPH-cytochrome P450 reductase
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Saccharomyces cerevisiae
FMN binding affinity for FMN is in the submicromolar range, 30times higher than that for FAD Saccharomyces cerevisiae
NADPH
-
 Saccharomyces cerevisiae