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Cytochrome P450's [1,2,3,E1] are a group of enzymes involved in the oxidative metabolism of a high number of natural compounds (such as steroids, fatty acids, prostaglandins, leukotrienes, etc) as well as drugs, carcinogens and mutagens. Based on sequence similarities, P450's have been classified into about forty different families [4,5]. P450's are proteins of 400 to 530 amino acids; the only exception is Bacillus BM-3 (CYP102) which is a protein of 1048 residues that contains a N-terminal P450 domain followed by a reductase domain. P450's are heme proteins. A conserved cysteine residue in the C-terminal part of P450's is involved in binding the heme iron in the fifth coordination site. From a region around this residue, we developed a ten residue signature specific to P450's.

The term 'cytochrome' P450, while commonly used, is incorrect as P450 are not electron-transfer proteins; the appropriate name is P450 'heme- thiolate proteins'.

Degtyarenko K.N.

December 2004 / Pattern and text revised.

PROSITE method (with tools and information) covered by this documentation:

CYTOCHROME_P450, PS00086; Cytochrome P450 cysteine heme-iron ligand signature  (PATTERN)

Consensus pattern: [FW]-[SGNH]-x-[GD]-{F}-[RKHPT]-{P}-C-[LIVMFAP]-[GAD] C is the heme iron ligand Sequences known to belong to this class detected by the pattern: ALL, except for P450 IIB10 from mouse, which has Lys in the first position of the pattern Other sequence(s) detected in Swiss-Prot: 9.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00086 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00086 • Scan Swiss-Prot/TrEMBL entries against PS00086 • view ligand binding statistics

Matching PDB structures: 1AKD 1BU7 1BVY 1C8J ... [ALL]

1	Authors	Nebert D.W., Gonzalez F.J.
	Title	P450 genes: structure, evolution, and regulation.
	Source	Annu. Rev. Biochem. 56:945-993(1987).
	PubMed ID	3304150
	DOI	10.1146/annurev.bi.56.070187.004501

2	Authors	Coon M.J., Ding X.X., Pernecky S.J., Vaz A.D.
	Title	Cytochrome P450: progress and predictions.
	Source	FASEB J. 6:669-673(1992).
	PubMed ID	1537454

3	Authors	Guengerich F.P.
	Title	Reactions and significance of cytochrome P-450 enzymes.
	Source	J. Biol. Chem. 266:10019-10022(1991).
	PubMed ID	2037557

4	Authors	Nelson D.R., Kamataki T., Waxman D.J., Guengerich F.P., Estabrook R.W., Feyereisen R., Gonzalez F.J., Coon M.J., Gunsalus I.C., Gotoh O.
	Title	The P450 superfamily: update on new sequences, gene mapping, accession numbers, early trivial names of enzymes, and nomenclature.
	Source	DNA Cell Biol. 12:1-51(1993).
	PubMed ID	7678494

5	Authors	Degtyarenko K.N., Archakov A.I.
	Title	Molecular evolution of P450 superfamily and P450-containing monooxygenase systems.
	Source	FEBS Lett. 332:1-8(1993).
	PubMed ID	8405421

E1
Source	http://www.icgeb.trieste.it/p450/

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