POR reduces CYP450:Fe3+ to CYP450:Fe2+

Stable Identifier
R-HSA-76494
Type
Reaction
Species
Homo sapiens
Compartment
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NADPH-cytochrome P450 reductase (POR) (Shephard et al. 1992) and cytochrome-b5 and NADH-b5 reductase play important roles in cytochrome P450-mediated drug metabolism (Gan et al. 2009). POR can transfer electrons to many naturally occurring electron acceptors, including cytochrome P450 enzymes where it transfers the electrons from NADPH into the P450 catalytic cycle (Elmore & Porter 2002). The P450 catalytic cycle describes the transitional mechanistic steps by which P450s bind a substrate, act upon it and finally release the product, returning P450s to their initial state (see mini-review Guengerich 2007).

Literature References
PubMed ID Title Journal Year
18838505 Role of NADPH-cytochrome P450 reductase and cytochrome-b5/NADH-b5 reductase in variability of CYP3A activity in human liver microsomes

Gan, L, von Moltke, LL, Trepanier, LA, Harmatz, JS, Greenblatt, DJ, Court, MH

Drug Metab. Dispos. 2009
17936929 Mechanisms of cytochrome P450 substrate oxidation: MiniReview

Guengerich, FP

J. Biochem. Mol. Toxicol. 2007
12381719 Modification of the nucleotide cofactor-binding site of cytochrome P-450 reductase to enhance turnover with NADH in Vivo

Elmore, CL, Porter, TD

J. Biol. Chem. 2002
1550342 Quantification of cytochrome P450 reductase gene expression in human tissues

Shephard, EA, Palmer, CN, Segall, HJ, Phillips, IR

Arch. Biochem. Biophys. 1992
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
NADPH-hemoprotein reductase activity of POR [endoplasmic reticulum membrane]
Physical Entity
Activity
Authored
Reviewed
Created