Cytochrome P450 reductase

Protein POR PDB 1amo

Cytochrome P450 Reductase

Cytochrome P450 reductase, also known as NADPH--cytochrome P450 reductase, is a membrane-bound enzyme involved in the electron transfer to cytochrome P450 enzymes. This essential enzyme plays a crucial role in the metabolism of various endogenous and exogenous compounds in organisms.

Structure

Cytochrome P450 reductase is a flavoprotein that contains both flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) as cofactors. The enzyme is anchored to the endoplasmic reticulum membrane and consists of multiple domains, including a flavodoxin-like domain, a FMN-binding domain, and a FAD-binding domain.

Function

The primary function of cytochrome P450 reductase is to transfer electrons from NADPH to cytochrome P450 enzymes, which are responsible for the oxidative metabolism of a wide range of substrates, including drugs, steroids, fatty acids, and environmental toxins. This electron transfer process is essential for the activation of cytochrome P450 enzymes and the subsequent biotransformation of their substrates.

Role in Drug Metabolism

Cytochrome P450 reductase plays a critical role in drug metabolism by facilitating the activation of cytochrome P450 enzymes, which are involved in the biotransformation of many pharmaceutical compounds. The activity of cytochrome P450 reductase can influence the efficacy and toxicity of drugs, making it an important target for drug development and personalized medicine.

Clinical Significance

Mutations in the gene encoding cytochrome P450 reductase have been associated with various disorders, including Antley-Bixler syndrome, a rare genetic condition characterized by craniosynostosis and skeletal abnormalities. Understanding the role of cytochrome P450 reductase in human health and disease is crucial for developing targeted therapies and diagnostic tools.

See also

• Cytochrome P450
• NADPH