cytochrome P450
Sign in to saveAlso known as cytochrome P-450, CYP, Cytochrome P-450 Enzyme System, Cyt_P450, IPR001128
superfamily of enzymes containing heme as a cofactor that function as monooxygenases
Key facts
- Symbol
- p450
- Pfam
- PF00067
- Interpro
- IPR001128
- Prosite
- PDOC00081
- Scop2
- 2cpp / SCOPe / SUPFAM
- Opm protein
- 2bdm
- Cdd
- cd00302
- Pdb
- IPR001128 PF00067 ( ECOD ; PDBsum )
- Alphafold
- IPR001128 PF00067
via Wikipedia infobox
Research
123,080 papers- Cytochrome P450 Structure, Function and Clinical Significance: A Review.Current drug targets · 2018
- Recent Structural Insights into Cytochrome P450 Function.Trends in pharmacological sciences · 2016
- Cytochrome P450: genotype to phenotype.Xenobiotica; the fate of foreign compounds in biological systems · 2020
- The effect of cytochrome P450 metabolism on drug response, interactions, and adverse effects.American family physician · 2007
- Cytochrome P450 research and The Journal of Biological Chemistry.The Journal of biological chemistry · 2019
via PubMed
~12 min read
Encyclopedic overview
Cytochromes P450 (P450s or CYPs) are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. However, they are not omnipresent; for example, they have not been found in Escherichia coli. In mammals, these enzymes oxidize steroids, fatty acids, xenobiotics, and participate in many biosyntheses. By hydroxylation, CYP450 enzymes convert xenobiotics into hydrophilic derivatives, which are more readily excreted.
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. Most P450s require a protein partner to deliver one or more electrons to reduce the iron (and eventually molecular oxygen).
Excerpted from Wikipedia’s “cytochrome P450” article, available under the CC BY-SA 4.0 licence.