It has been suggested that this article should be split into multiple articles. (discuss) (March 2024)
Cytochrome P450
Structure of lanosterol 14α-demethylase (CYP51)
Identifiers
Symbol
p450
Pfam
PF00067
InterPro
IPR001128
PROSITE
PDOC00081
SCOP2
2cpp / SCOPe / SUPFAM
OPM superfamily
39
OPM protein
2bdm
CDD
cd00302
Membranome
265
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
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.
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).
^ abDanielson PB (December 2002). "The cytochrome P450 superfamily: biochemistry, evolution and drug metabolism in humans". Current Drug Metabolism. 3 (6): 561–597. doi:10.2174/1389200023337054. PMID 12369887.
^Lamb DC, Lei L, Warrilow AG, Lepesheva GI, Mullins JG, Waterman MR, Kelly SL (August 2009). "The first virally encoded cytochrome p450". Journal of Virology. 83 (16): 8266–8269. doi:10.1128/JVI.00289-09. PMC 2715754. PMID 19515774.
^Sigel A, Sigel H, Sigel RK (2007). The Ubiquitous Roles of Cytochrome P450 Proteins: Metal Ions in Life Sciences. New York: Wiley. ISBN 978-0-470-01672-5.
^Nelson DR (January 2018). "Cytochrome P450 diversity in the tree of life". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1866 (1): 141–154. doi:10.1016/j.bbapap.2017.05.003. PMC 5681887. PMID 28502748.
^Nelson DR (October 2009). "The cytochrome p450 homepage". Human Genomics. 4 (1). University of Tennessee: 59–65. doi:10.1186/1479-7364-4-1-59. PMC 3500189. PMID 19951895.
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