Cytochrome P450 | |||||||||
---|---|---|---|---|---|---|---|---|---|
Cytochrome 750 Oxidase (CYP2C9)
|
|||||||||
Identifiers | |||||||||
Symbol | p450 | ||||||||
Pfam | PF00067 | ||||||||
InterPro | IPR0011 | ||||||||
PROSITE | PDOC00081 | ||||||||
SCOP | 2cpp | ||||||||
SUPERFAMILY | 2cpp | ||||||||
OPM superfamily | 41 | ||||||||
OPM protein | 2bdm | ||||||||
|
Available protein structures: | |
---|---|
Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Cytochromes P450 (CYPs) are proteins of the superfamily containing heme as a cofactor and, therefore, are hemoproteins. CYPs use a variety of small and large molecules as substrates in enzymatic reactions. They 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.
CYP enzymes have been identified in all kingdoms of life: animals, plants, fungi, protists, bacteria, archaea, and even in viruses. However, they are not omnipresent; for example, they have not been found in Escherichia coli. More than 200,000 distinct CYP proteins are known.
Most CYPs require a protein partner to deliver one or more electrons to reduce the iron (and eventually molecular oxygen). Based on the nature of the electron transfer proteins, CYPs can be classified into several groups: