Cytochrome P450
Class of enzymes / From Wikipedia, the free encyclopedia
Dear Wikiwand AI, let's keep it short by simply answering these key questions:
Can you list the top facts and stats about Cytochrome P450?
Summarize this article for a 10 year old
Cytochromes P450 (P450s or CYPs) are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases.[1][2][3] In mammals, these enzymes oxidize steroids, fatty acids, xenobiotics, and participate in many biosyntheses.[2] CYP450 enzymes convert xenobiotics into hydrophilic derivatives, which are more readily excreted. In almost all of the transformations that they catalyze, P450's affect hydroxylation.
Cytochrome P450 | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | p450 | ||||||||
Pfam | PF00067 | ||||||||
InterPro | IPR001128 | ||||||||
PROSITE | PDOC00081 | ||||||||
SCOP2 | 2cpp / SCOPe / SUPFAM | ||||||||
OPM superfamily | 39 | ||||||||
OPM protein | 2bdm | ||||||||
CDD | cd00302 | ||||||||
Membranome | 265 | ||||||||
|
P450 enzymes have been identified in all kingdoms of life: animals, plants, fungi, protists, bacteria, and archaea, as well as in viruses.[4] However, they are not omnipresent; for example, they have not been found in Escherichia coli.[3][5] As of 2018[update], more than 300,000 distinct CYP proteins are known.[6][7]
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).