Regular ArticleThe Kinetic and Spectral Characterization of the E. coli-Expressed Mammalian CYP4A7: Cytochrome b5 Effects Vary with Substrate
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Novel insights into oxidation of fatty acids and fatty alcohols by cytochrome P450 monooxygenase CYP4B1
2020, Archives of Biochemistry and BiophysicsCitation Excerpt :Nevertheless, the substrate binding site is at least big enough to accept the furan compounds IPO 13 and PK 14 [11] as well as the even bulkier 2-aminoanthracene [48] as substrates. External factors such as the addition of cytochrome b5 can influence fatty acid hydroxylation activity as well: Loughran et al. [49] reported that the turnover of C12 4 by CYP4A7 increased from 28 to 130 min−1 through the addition of cytochrome b5; based on their data the authors suggested that cytochrome b5 in this particular case did not serve as an electron donor for CYP4A7, but rather took a conformational role in such that it docks at the proximal surface of the heme pocket to open the substrate channel for greater access to substrates of varying flexibility, bulk, and chain length [49]. Regarding the role of cytochrome b5 in CYP4B1 fatty acid hydroxylation, we observed that under the given experimental conditions, addition of cytochrome b5 led to an increase of C12 4 conversion from 24 to 45% within 30 min.
Role of cytochrome b5 in the modulation of the enzymatic activities of cytochrome P450 17α-hydroxylase/17,20-lyase (P450 17A1)
2017, Journal of Steroid Biochemistry and Molecular BiologyChallenges in assignment of allosteric effects in cytochrome P450-catalyzed substrate oxidations to structural dynamics in the hemoprotein architecture
2017, Journal of Inorganic BiochemistryCitation Excerpt :In this regard, POR triggered opening of water channels in P450s and strengthened substrate binding [41,42]. Similarly cytochrome b5 (b5) and its heme-depleted variant (apo-b5) may act as allosteric regulators in a P450 isoform-dependent manner, forcing the monooxygenases into an optimized geometry such as to permit facile POR complexation, greater access of substrates with increased binding affinity and collision frequency with the active oxygen species [43–47]. Though the effector role of b5 has been occasionally challenged [48], reexamination dismissed heme transfer from P450s to regenerate holo-b5 as a prerequisite for catalytic stimulation [49].
NAD(P)H Cytochrome b<inf>5</inf> oxidoreductase deficiency in Leishmania major results in impaired linoleate synthesis followed by increased oxidative stress and cell death
2012, Journal of Biological ChemistryCitation Excerpt :The cb5 domain participates in a variety of metabolic conversions including the desaturation and elongation of FAs (13, 14), cholesterol biosynthesis (15), and cytochrome P450-mediated mono-oxygenation (16). Specific examples of these various electron acceptors are Δ9-, Δ6-, and Δ5-acyl CoA desaturases (17), FA elongation enzyme (13), alkyl acylglycero-3-phosphoryl ethanolamine desaturase (18), phospholipid desaturase (19), Δ7-sterol Δ9-desaturase (15), N-hydroxylamine reductase (19), 4-methylsterol oxidase (20), prostaglandin synthase reductase (21), and cytochrome P450 4A7 (22). In addition, cb5 domain is found in other unrelated proteins such as nitrate reductase (23), sulfite oxidases (24, 25), and lactate dehydrogenase (26).
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