Abstract: Cytochrome P450s comprise a superfamily of heme-thiolate proteins named for thespectral absorbance peak of their carbon-monoxide-bound species at 450 nm. Having been foundin every class of organism, including Archaea, the P450 superfamily is believed to haveoriginated from an ancestral gene that existed over 3 billion years ago. Repeated geneduplications have subsequently given rise to one of the largest of multigene families. Theseenzymes are notable both for the diversity of reactions that they catalyze and the range ofchemically dissimilar substrates upon which they act. Cytochrome P450s support the oxidative,peroxidative and reductive metabolism of such endogenous and xenobiotic substrates asenvironmental pollutants, agrochemicals, plant allelochemicals, steroids, prostaglandins and fatty acids. In humans,cytochrome P450s are best know for their central role in phase I drug metabolism where they are of critical importance totwo of the most significant problems in clinical pharmacology: drug interactions and interindividual variability in drugmetabolism. Recent advances in our understanding of cytochrome P450-mediated drug metabolism have been acceleratedas a result of an increasing emphasis on functional genomic approaches to P450 research. While human cytochrome P450databases have swelled with a flood of new human sequence variants, the functional characterization of the correspondinggene products has not kept pace. In response researchers have begun to apply the tools of proteomics as well ashomology-based and ab initio modeling to salient questions of cytochrome P450 structure/function. This review examinesthe latest advances in our understanding of human cytochrome P450s
The Cytochrome P450 Superfamily: Biochemistry, Evolution and Drug Metabolism in Humans (PDF Download Available). Available from: https://www.researchgate.net/publication/11089661_The_Cytochrome_P450_Superfamily_Biochemistry_Evolution_and_Drug_Metabolism_in_Humans [accessed May 7, 2016].