Regular ArticleCompetitive Interactions between Cytochromes P450 2A6 and 2E1 for NADPH-Cytochrome P450 Oxidoreductase in the Microsomal Membranes Produced by a Baculovirus Expression System☆,☆☆
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2017, Journal of Biological ChemistryInteractions among cytochromes P450 in microsomal membranes: Oligomerization of cytochromes P4503A4,3A5, and 2E1 and its functional consequences
2015, Journal of Biological ChemistryCitation Excerpt :“control” SupersomesTM containing rat recombinant NADPH-cytochrome P450 reductase manufactured by Corning Life Sciences (catalog no. 456514). Competition of different P450 species for a limited amount of CPR, which has been observed by numerous investigators (1–6), constitutes an important element in the inter-P450 cross-talk. However, the integrative connections in microsomal monooxygenase go far beyond that and involve functional effects of physical interactions of multiple P450 molecules that result in oligomerization (7–17).
A novel type of allosteric regulation: Functional cooperativity in monomeric proteins
2012, Archives of Biochemistry and BiophysicsCitation Excerpt :The importance of cytochrome P450 oligomerization for their cooperative and allosteric functional properties is briefly discussed further in this review. In addition, the interaction of the P450 heme enzyme with its redox partners can be also modulated by the presence of substrates, effectors, and by interactions with other cytochrome P450 molecules [56,60,62–65]. The commonly accepted catalytic cycle shown in the Scheme 1, includes all important intermediates of P450 catalysis.
Formation of P450 • P450 complexes and their effect on P450 function
2012, Pharmacology and TherapeuticsCitation Excerpt :Kinetic analysis of the rates of metabolism by reconstituted systems varying the relative amounts of the purified enzymes was shown to be consistent with simple competition for CPR. The interaction of CYP2A6 and CYP2E1 was also reported in a study that used microsomes from Baculovirus expression systems engineered to express CPR and one or both of the P450s (Tan et al., 1997). Thus, this study examined P450–P450 interactions in natural membranes, and the results were not influenced by potential artifacts resulting from incorporation of proteins into lipid-reconstituted systems.
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Supported by NIH Grant ES03938 and NIEHS Center Grant ES05022.
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R. N. LoeppkyC. J. Michejda, Eds.
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Conducted in partial fulfillment of a requirement for a Ph.D. in the Graduate Program of Biochemistry and Molecular Biology, Rutgers University.
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To whom correspondence should be addressed.