Regular ArticleBaculovirus Expression and Purification of Human and Rat Cytochrome P450 2E1☆
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2018, Encyclopedia of Interfacial Chemistry: Surface Science and ElectrochemistryStructural and functional effects of cytochrome b<inf>5</inf> interactions with human cytochrome P450 enzymes
2017, Journal of Biological ChemistryCitation Excerpt :Comparisons of the mutational effects are clearer when evaluating chlorzoxaone 6-hydroxylation. Consistent with previous literature reports (28, 29), the effect of wild-type b5 on 2E1 chlorzoxazone 6-hydroxylation was pronounced, with both an increased kcat and decreased Km (Fig. 3D). Specifically, experiments herein revealed an ∼1.7-fold increase in kcat and a 2-fold decrease in Km, yielding an ∼3.5-fold increase in kcat/Km.
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2010, Journal of Biomedical ResearchStructures of human cytochrome P-450 2E1: Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates
2008, Journal of Biological ChemistryCitation Excerpt :Multiple roles have been proposed for cytochrome b5 in P-450-mediated metabolism, including delivering to P-450 the second electron required for catalysis and/or stabilization of P-450 in support of catalysis. Cytochrome b5 addition strongly stimulates CYP2E1 metabolism, ∼12-fold for p-nitrophenol (63), 25-fold for acetaminophen (64), 67-fold for 7-ethoxycoumarin (65), and 270-fold for aniline (66). Although for many P-450 proteins stimulation of metabolism can be observed upon the addition of either cytochrome b5 or apo cytochrome b5 (lacking the heme and therefore unable to do electron transfer), apo cytochrome b5 cannot replace holo cytochrome b5 in CYP2E1 catalysis, suggesting a role in electron transfer (65).
CYP2E1 substrate inhibition: Mechanistic interpretation through an effector site for monocyclic compounds
2008, Journal of Biological ChemistryCitation Excerpt :Despite the evidence for substrate inhibition, the observed data were not fit to a particular kinetic mechanism. Subsequent steady-state studies by others have been typically limited to a maximal concentration of 100 μm pNP and relied on a simple Michaelis-Menten scheme to analyze data (23-25). For the rabbit CYP2E1 system, kcat and Km were reported to be 30 min-1 and 38 μm, respectively (23).
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This work was supported by National Institutes of Health Research Grants ES02728 (S.D.N.), GM32165 (S.D.N.), and GM48349 (K.E.T.).
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To whom correspondence should be addressed at Department of Medicinal Chemistry, School of Pharmacy, Box 357610, University of Washington, Seattle, WA 98195. Fax: (206) 685-3252.