Cytochrome P450 function and evolution   Email     Print   PDF

	Enlarge Image Cytochrome P450 Phylogenetic Tree. Maximum likelihood phylogenetic (evolutionary) tree of cytochrome P450 protein sequences. More than 1600 sequences in 16 species are included.

The cytochrome P450 (abbreviated CYP) enzymes catalyze oxidative transformation leading to activation or inactivation of many endogenous and exogenous chemicals, with consequences in normal physiology and disease processes.

Functional information is most abundant for mammalian CYPs, which be separated into two major groups: those with generally narrow substrate specificity that are involved primarily in synthesis, activation or inactivation of endogenous regulatory molecules (such as steroid, vitamin D, retinoids, and eicosanoids), and those involved most heavily in the metabolism of xenobiotics, but which may act as well in the metabolism of endogenous compounds. Thus, CYP enzymes can determine the persistence and action of endogenous regulatory molecules as well as many drugs and other toxicants and carcinogens.

We are interested in the evolution and function of non-mammalian cytochromes P450, in part to develop biomedical models of CYP function, but also to understand the functional evolution of this important enzyme superfamily.