Cytochrome P450 2A6 overexpression 293T lysate (whole cell)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

CYP2A6 also known as cytochrome P450 2A6 is an enzyme with a mass of approximately 56 kDa. It is a member of the cytochrome P450 superfamily and is expressed mainly in the liver with some expression in the respiratory tract. CYP2A6 is involved in the oxidation of several drugs and foreign chemicals. It functions by catalyzing the hydroxylation of various substrates which aids in their metabolism and clearance from the body. Despite its primary presence in hepatic tissue its expression can occur in other extrahepatic tissues as well.

Biological function summary

CYP2A6 plays a significant role in phase I metabolism as part of the cytochrome P450 enzyme complex. This enzyme contributes to the metabolic activation and detoxification of many xenobiotic substances including nicotine and coumarin. Through its enzymatic action CYP2A6 influences the pharmacokinetics of several drugs impacting their absorption distribution metabolism and excretion. It also contributes to the interindividual variability seen in the metabolism of drugs affecting both therapeutic outcomes and toxicity risks.

Pathways

CYP2A6 plays an essential role in drug metabolism and the detoxification pathway. It is heavily involved in the metabolism of nicotine by converting it to cotinine therefore playing a prominent role in nicotine addiction and dependence. CYP2A6 is also associated with the synthesis of steroid hormones. Through these pathways it interacts with other cytochrome P450 enzymes like CYP2A7 as well as enzymes involved in the drug metabolism processes.

CYP2A6 is linked with several conditions primarily due to its role in drug metabolism. Altered activity of CYP2A6 can affect the risk of nicotine addiction impacting individuals' susceptibility to tobacco dependence. Furthermore variations in CYP2A6 activity are associated with susceptibility to certain cancers due to changes in the activation of procarcinogens. The enzyme's involvement in liver cancer emphasizes the importance of understanding its interaction with other CYP enzymes notably CYP2A6/7. This understanding suggests potential pathways for therapeutic targeting in diseases linked to metabolic dysfunction.