Regular ArticleExpression of Cytochrome P450 2A6 in Escherichia coli: Purification, Spectral and Catalytic Characterization, and Preparation of Polyclonal Antibodies☆
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Structural and functional effects of cytochrome b<inf>5</inf> interactions with human cytochrome P450 enzymes
2017, Journal of Biological ChemistryCitation Excerpt :The influence of b5 on the major drug-metabolizing P450 enzyme CYP3A4 has been widely documented, with numerous CYP3A4-mediated reactions showing stimulation in the presence of both holo- and apo-b5 (21). CYP2A6 coumarin 7-hydroxylation has also been reported to be stimulated 1.5–2.5-fold by b5 (19, 22–24). CYP2D6 is a clinically significant P450 enzyme because of its ability to metabolize a wide array of pharmaceuticals and its high degree of polymorphism (25), but its metabolite production is reportedly less influenced by b5, at least with in vitro experiments (19, 20, 26, 27).
Inhibition effects of Vernonia cinerea active compounds against cytochrome P450 2A6 and human monoamine oxidases, possible targets for reduction of tobacco dependence
2015, Drug Metabolism and PharmacokineticsMechanism-based inactivation of cytochrome P450 2A6 and 2A13 by Rhinacanthus nasutus constituents
2014, Drug Metabolism and PharmacokineticsInhibition and inactivation of cytochrome P450 2A6 and cytochrome P450 2A13 by menthofuran, β-nicotyrine and menthol
2012, Chemico-Biological InteractionsCytochrome P450 is present in both ferrous and ferric forms in the resting state within intact Escherichia coli and hepatocytes
2011, Journal of Biological ChemistryCitation Excerpt :Livers were obtained from male Sprague-Dawley rats (Central Animal Breeding Facility of the University of Queensland) under procedures approved by University of Queensland ethics committees, and microsomes were prepared as described previously (18). CYP1A2, CYP2A6, CYP2A13, CYP2C9, CYP2C19, CYP3A4, CYP176A1 (P450cin), and CYP101A1 were expressed in E. coli according to the general procedures outlined previously (19–24). Bacterial chaperones were coexpressed using the pGro7 plasmid to augment P450 yields (22, 25, 26).
Drug metabolism by CYP2C8.3 is determined by substrate dependent interactions with cytochrome P450 reductase and cytochrome b5
2011, Biochemical PharmacologyCitation Excerpt :Interestingly, both amino acid mutations (R139K and K399R) in the corresponding CYP2C8.3 protein are located on the proximal site of the heme in the binding region of cytochrome b5 and CPR [16] and may suggest an involvement of the redox-partners in the variable activity of CYP2C8. The activation of CYP enzymes by cytochrome b5 is well established [17] for CYP3A4 [18], CYP2B4 and variants [19], CYP2A6 [20], CYP2C9 [21] and CYP2C19 [22]. Further, cytochrome b5 is also reported to decrease reaction uncoupling [23] and increase kcat.
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Supported by the Internal Grant Agency of Czech Ministry of Health, Grant IGA 3505-3 (1996-98), and the Grant Agency of Czech Republic, Grant 303/96/0373 (1996).
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