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Literature summary for 1.6.2.4 extracted from

  • Gutierrez, A.; Grunau, A.; Paine, M.; Munro, A.W.; Wolf, C.R.; Roberts, G.C.; Scrutton, N.S.
    Electron transfer in human cytochrome P450 reductase (2003), Biochem. Soc. Trans., 31, 497-501.
    View publication on PubMed
Search for more literature for 1.6.2.4

Activating Compound

Activating Compound Comment Organism Structure
2',5'-ADP increases internal electron transfer in dithionite reduced enzyme Homo sapiens

Protein Variants

Protein Variants Comment Organism
W676H rate of FAD-reduction is modestly affected, enzyme is reduced only to the two-electron level in rapid mixing experiments Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Homo sapiens 5783
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome c + NADH 3-fold lower activity than with NADPH Homo sapiens 2 ferrocytochrome c + NAD+ + H+
-
 ?
2 ferricytochrome c + NADPH
-
 Homo sapiens 2 ferrocytochrome c + NADP+ + H+
-
 ?
2 ferricytochrome P450 + NADPH
-
 Homo sapiens 2 ferrocytochrome P450 + NADP+ + H+
-
 ?
ferricytochrome c + dithionite
-
 Homo sapiens ferrocytochrome c + ?
-
 ?

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, two binding sites Homo sapiens
FMN together with FAD Homo sapiens
NADPH
-
 Homo sapiens