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Use of inhibitors in elucidating the mechanism of an enzyme
Hence, much emphasis has been on the inhibition of these enzymes to develop potential cancer preventative and therapeutic agents [2,3,9,14].The potential anti-cancer strategies targeting P450 inhibition were postulated as: (i) preventing the conversion of environmental procarcinogens to active carcinogens; (ii) preventing the conversion of hormonal precursors to carcinogenic hormone derivatives; and (iii) preventing the metabolic inactivation of anti-cancer drugs .Like P450 1A1, this enzyme also metabolically activates procarcinogens to carcinogenic forms, resulting in mutagenesis and tumorigenesis .
Herein we will review multifarious inhibitors of cytochrome P450 family 1 enzymes, 1A1, 1A2, and 1B1.
Because of their high structural and functional similarity, cytochrome P450s 1A1, 1A2, and 1B1 are known to have overlapping substrates, inducers, and inhibitors.
P450 1A1 is one of the most important enzymes involved in tumorigenesis initiated by environmental pollutants .
A number of epidemiological studies have shown that genetic variants of human gene are significantly associated with the susceptibilities to lung and breast cancers [4,5,6].
Because of the significant role of P450 1A1 enzyme in human carcinogenesis, modulation of P450 1A1 activity has been considered as a potential target for cancer chemoprevention.
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P450 1A2 is one of the major cytochrome P450 enzymes in human liver (about 13%) responsible for the metabolism of a variety of arylamines and heterocyclic arylamines which include numerous therapeutic drugs such as phenacetin, lidocaine, tacrine, and theophylline [2,7].P450 families 1, 2, and 3 contribute most extensively to the biotransformation of xenobiotics into more polar metabolites that are readily excreted.In humans and most mammals, P450 family 1 comprises three well-studied monooxygenases, 1A1, 1A2, and 1B1.Thus, theoretical modeling can be extremely useful in the characterization of short-lived intermediates which either cannot be detected experimentally or have a lifetime that is too short to enable spectroscopic characterization.This paper gives an overview of the knowledge of the catalytic cycles of CDO and Tau D with particular emphasis on the processes obtained after dioxygen binding.Therefore, the development of selective inhibitors towards any of these enzymes is a great challenge.To date, thousands of compounds (including natural products, pharmaceuticals, and synthetic compounds) have been evaluated for their inhibitory activities toward P450 family 1 enzymes.In this review, we thoroughly discuss the selectivity of many representative P450 family 1 inhibitors reported in the past 20 years through a meta-analysis.Cytochrome P450 enzymes are a large ubiquitous superfamily of enzymes, playing a significant physiological role in the detoxification of xenobiotics, and the biosynthesis of many endogenous compounds.The latter is the oxidant that is able to abstract a hydrogen atom from a substrate and rebounds the hydroxyl group to form hydroxylated products.The theoretical (density functional theory (DFT)) studies show that the first step in this dioxygen activation process is the rate-determining step and that the reactions leading to products are highly exothermic as would be expected from an efficient catalytic cycle of an enzyme.