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P450s are, in general, the terminal oxidase enzymes in electron transfer chains, broadly categorized as P450-containing systems. The term "P450" is derived from the spectrophotometric peak at the wavelength of the absorption maximum of the enzyme (450 nm) when it is in the reduced state and complexed with carbon monoxide.
Effects on P450 isozyme activity are a major source of adverse drug interactions, since changes in P450 enzyme activity may affect the metabolism and clearance of various drugs. For example, if one drug inhibits the P450-mediated metabolism of another drug, the second drug may accumulate within the body to toxic levels.
"INHIBITORS, INDUCERS AND SUBSTRATES OF CYTOCHROME P450 ISOZYMES". "The Life Raft Group: Long List of Inhibitors and Inducers of CYP3A4 and CYP2D6". "DRUGBANK Online: Cytochrome P-450 Enzyme Inhibitors". "MEDICATIONS METABOLIZED BY CYTOCHROME P450 3A4" (PDF)
Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system. [1] [2] [3] [4]P450 enzymes usually function as a terminal oxidase in multicomponent electron-transfer chains, called P450-containing monooxygenase systems, although self-sufficient, non-monooxygenase P450s have been also described.
CYP2C9 is a crucial cytochrome P450 enzyme, which plays a significant role in the metabolism, by oxidation, of both xenobiotic and endogenous compounds. [7] CYP2C9 makes up about 18% of the cytochrome P450 protein in liver microsomes. The protein is mainly expressed in the liver, duodenum, and small intestine. [7]
Cholesterol side-chain cleavage enzyme is commonly referred to as P450scc, where "scc" is an abbreviation for side-chain cleavage. P450scc is a mitochondrial enzyme that catalyzes conversion of cholesterol to pregnenolone .
The cytochrome P450 (CYP) superfamily of membrane-bound (typically endoplasmic reticulum-bound) enzymes contain a heme cofactor and therefore are hemoproteins.The superfamily comprises more than 11,000 genes categorized into 1,000 families that are distributed broadly throughout bacteria, archaea, fungi, plants, animals, and even viruses.
Cytochrome P450 reductase (also known as NADPH:ferrihemoprotein oxidoreductase, NADPH:hemoprotein oxidoreductase, NADPH:P450 oxidoreductase, P450 reductase, POR, CPR, CYPOR) is a membrane-bound enzyme required for electron transfer from NADPH to cytochrome P450 [5] and other heme proteins including heme oxygenase in the endoplasmic reticulum [6] of the eukaryotic cell.