Cytochrome nomenclature

Nelson DR. 1998. Cytochrome P450 nomenclature. Methods Mol Biol 107 15-24. 

Human Cytochrome P450 CYP) Allele Nomenclature Committee home page. Available at www.imm.ki.se/CYPalleles/cyp2d6.htm. 

Extensive analysis of the EPR and redox behavior of this unusual copper protein led to the hypothesis that the protein might contain a Cu(A) site similar to that in cytochrome oxidase (Riester et ai, 1989) and that the unusual seven-line EPR is due to the Cu(A)-type site. An alternative interpretation of this EPR is based on electron spin-echo spectroscopy as well, and that is that the seven-line EPR is due to a half-met Cu—Cu pair and to unusual type I sites (Jin et ai, 1989). Three sets of spin-echo peaks can be attributed to nitrogens on imidazole ligands to a CuA-type site and to another imidazole on the half-met site. The electron spin-echo spectra of cytochrome oxidase are similar, although there is not enough copper in cytochrome oxidase for a half-met site. Conceivably, the property of delocalization of the paramagnetic electron could be effected by the proposed bridging between Cub and heme as (nomenclature summarized by Capaldi, 1990), which are proposed to be 3-4 A apart. 

Ingelman-Sundberg, M., A.K. Daly, M. Oscarson, and D.W. Nebert, Human cytochrome P450 (CYP) genes recommendations for the nomenclature of alleles. Pharmacogenetics, 2000.10(1) 91-3. 

The cytochrome P450 system is the principal enzyme system for the metabolism of lipophilic xenobiotics. It is a heme-containing, membrane-bound, multi-enzyme system which is present in many tissues in vivo but is present at the highest level in liver. A coenzyme, cytochrome P450 NADPH oxidoreductase (OR), is essential for P450 catalytic function and cytochrome bs may stimulate catalytic activities of some enzymes. In human liver, it is estimated that there are 15-20 different xenobiotic-metabolizing cytochrome P450 forms. A standard nomenclature, based on relatedness of the amino acid sequences, has been developed (Nelson et al., 1993). The most recent... 

The CYPs, the carbon monoxide-binding pigments of microsomes, are heme proteins of the b cytochrome type. Originally described as a single protein, there are now known to be more than 2000 CYPs widely distributed throughout animals, plants, and microorganisms. A system of nomenclature utilizing the prefix CYP has been devised... 

Most Phase I oxidations are performed by cytochrome P-450. "Cytochrome," derived from Greek, literally means "colored substance in the cell." The color is derived from the properties of the outer electrons of the transition element iron. "P-450" denotes a reddish pigment with the unusual property of having its major optical absorption peak (Soret maximum) at about 450 nm, when it has been reduced and combined with carbon monoxide.330 Although the name "P-450" was intended to be temporary (until more was known about the substance), the terminology has persisted for 18 yr because of the increasing complexity of this enzyme system and because of the lack of agreement on new nomenclature. 

Figure 9.1. Nomenclature of cytochromes P450. Members of the same family share >40% amino acid homology, and members of the same subfamily share >55% amino acid homology.

Source Nelson, D. R., et al. Comparison of cytochrome P450 genes from the mouse and human genomes including nomenclature recommendations for genes, pseudogenes, and alternative-splice variants. Pharmacogenetics 14, 1-18, 2004. 

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