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In this regard, the structure has been compared to that of CYP102, which has already been employed extensively and shows the greatest similarity (Williams et al. 2000). The spatial arrangement of the major elements diverges from the other structures, with SRS-4 being the most conserved compared to CYP102. 3 AÊ root mean square (rms deviation) and the shape of the base of the active site is signi®cantly different, affecting the orientation and position of substrates as well as selectivity for different substrates.

1984). A systematic nomenclature system CYTOCHROME P450 35 was developed by Nebert (Nebert et al. 1987, 1989; Nelson et al. 1993) based upon the coding sequences. html.. For comparisons of older nomenclature to the current, see Nelson et al. (1993). The nomenclature system follows these basic rules: All P450s are members of the `superfamily' (some `functionally' related proteins such as fungal chloroperoxidase and the nitric oxide synthases are not included). The most de®ning region of the sequence is that surrounding the cysteine that serves as an axial thiolate ligand to the haem ion.

It should be pointed out that some microsomal P450s, because of particular processing patterns, are also delivered into the mitochondria (Addya et al. 1997; Neve and Ingelman-Sundberg 1999) and the plasma membrane (Loeper et al. 1998). In both cases there appears to be functional capability, although the details are not completely clear yet. The fraction of microsomal P450 targeted to the plasma membrane is very low but may be involved in the initiation of auto-immune responses 36 ENZYME SYSTEMS THAT METABOLISE DRUGS AND OTHER XENOBIOTICS involving P450s (Loeper et al.

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