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Cytochrome P450 reductase domains

Figure 3 Schematic representation of nitric oxide synthase isoforms and cytochrome P450 reductase. Haem, heme PDZ, PDZ domain (GLGF repeats) CaM, calmodulin FMN, flavin mononucleotide FAD, flavin adenine dinucleotide (adapted from Hobbs et al., 1999). Figure 3 Schematic representation of nitric oxide synthase isoforms and cytochrome P450 reductase. Haem, heme PDZ, PDZ domain (GLGF repeats) CaM, calmodulin FMN, flavin mononucleotide FAD, flavin adenine dinucleotide (adapted from Hobbs et al., 1999).
Figure 7 The crystal structure of NADPH-cytochrome P450 reductase (CPR). The FAD and FMN domains are linked by a hinge domain... Figure 7 The crystal structure of NADPH-cytochrome P450 reductase (CPR). The FAD and FMN domains are linked by a hinge domain...
Hodgson, A.V and H.W. Strobel (1996). Characterization of the FAD binding domain of cytochrome P450 reductase. Arch. Biochem. Biophys. 325, 99-106. [Pg.139]

Gutierrez, A., L.Y. Lian, C.R. Wolf, N.S. Scrutton, and G.C.K. Roberts (2001). Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains. Biochemistry 40, 1964-1975. [Pg.142]

Knight, K. and N.S. Scrutton (2002). Stopped-flow kinetic studies of electron transfer in the reductase domain of neuronal nitric oxide synthase Reevaluation of the kinetic mechanism reveals new enzyme intermediates and variation with cytochrome P450 reductase. Biochem. J. 367,19-30. [Pg.142]

Figure 13.2. A proposal for a simplified classification of CYPs with reference to either use of a ferredoxin or alternative electron transport mechanism. Class la— typical bacterial system supported by ferredoxin and ferredoxin reductase, for example, CYPlOl Class Ib—Rhodococcus sp. CYP fusion protein containing a ferredoxin domain Class Ic—Methylococcus capsulatus CYPS 1-ferredoxin fusion . Class 11a— typical eukaryotic CYP/NADPH-cytochrome P450 reductase system Class lib—a fusion protein of a CYP and flavoprotein reductase, for example, P450gM 3 Class IIc—P450 j containing separate flavodoxin and flavodoxin reductase partners . Class fll—standalone functional CYPs, for example, P450jj. ... Figure 13.2. A proposal for a simplified classification of CYPs with reference to either use of a ferredoxin or alternative electron transport mechanism. Class la— typical bacterial system supported by ferredoxin and ferredoxin reductase, for example, CYPlOl Class Ib—Rhodococcus sp. CYP fusion protein containing a ferredoxin domain Class Ic—Methylococcus capsulatus CYPS 1-ferredoxin fusion . Class 11a— typical eukaryotic CYP/NADPH-cytochrome P450 reductase system Class lib—a fusion protein of a CYP and flavoprotein reductase, for example, P450gM 3 Class IIc—P450 j containing separate flavodoxin and flavodoxin reductase partners . Class fll—standalone functional CYPs, for example, P450jj. ...
Black, S.D. and M.J. Coon (1982). Structural features of liver microsomal NADPH-cytochrome P450 reductase hydrophobic domain, hydrophilic domain and connecting region. J. Biol. Chem. 257, 5929-5938. [Pg.616]

Huang WC, Ellis J, Moody PC, Raven EL, Roberts GC (2013) Redox-linked domain movements in the eatalytie eycle of cytochrome P450 reductase. Structure 21 1581 1589... [Pg.62]

Narayanasami R, Horowitz PM, Masters BS (1995) Flavin-binding and protein structural integrity studies on NADPH-cytochrome P450 reductase are consistent with the presence of distinct domain. Arch Biochem Biophys 316 267-274... [Pg.62]

Zhao Q, Modi S, Smith G, Paine M, McDonagh PD, Wolf CR, Tew D, Lian LY, Roberts GC, Driessen HP (1999) Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. Protein Sci 8 298-306... [Pg.63]

Ellis J, Gutierrez A, Barsukov IL, Huang WC, Gross-mann JG, Roberts GC (2009) Domain motion in cytochrome P450 reductase conformational equilibria revealed by NMR and small-angle x-ray scattering. J Biol Chem 284 36628-36637... [Pg.63]

Vincent B, Morellet N, Fatemi F, Aigrain L, Truan G, Guittet E, Lescop E (2012) The closed and compact domain organization of the 70-kDa human cytochrome P450 reductase in its oxidized state as revealed by NMR. J Mol Biol 420 296-309... [Pg.63]

Jenldns CM, Waterman MR (1999) Flavodoxin as a model for the P450-interacting domain of NADPH cytochrome P450 reductase. Drug Metab Rev 31 195-203... [Pg.66]

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See also in sourсe #XX -- [ Pg.117 , Pg.118 , Pg.122 , Pg.124 , Pg.125 , Pg.129 , Pg.131 ]



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