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Volumn 21, Issue 4, 2007, Pages 399-410

Clinical, structural and functional implications of mutations and polymorphisms in human NADPH P450 oxidoreductase

Author keywords

Antley Bixler syndrome; Cytochrome P450; Enzyme kinetics; P450 oxidoreductase; Polymorphisms; Sex steroids; Steroidogenesis

Indexed keywords

CYTOCHROME C; CYTOCHROME P450; CYTOCHROME P450 17; CYTOCHROME P450 17 A1; DNA; ENZYME VARIANT; MICROSOME ENZYME; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STEROID; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

EID: 34447532545     PISSN: 07673981     EISSN: 14728206     Source Type: Journal    
DOI: 10.1111/j.1472-8206.2007.00520.x     Document Type: Conference Paper
Times cited : (51)

References (78)
  • 1
    • 0024447464 scopus 로고
    • Isolation of a human cytochrome P-450 reductase cDNA clone and localization of the corresponding gene to chromosome 7q11.2
    • Shephard E.A., Phillips I.R., Santisteban I. et al. Isolation of a human cytochrome P-450 reductase cDNA clone and localization of the corresponding gene to chromosome 7q11.2. Ann. Hum. Genet. (1989) 53, 291 301.
    • (1989) Ann. Hum. Genet. , vol.53 , pp. 291-301
    • Shephard, E.A.1    Phillips, I.R.2    Santisteban, I.3
  • 2
    • 0024397098 scopus 로고
    • Human NADPH-P450 oxidoreductase: Complementary DNA cloning, sequence and vaccinia virus-mediated expression and localization of the CYPOR gene to chromosome 7
    • Yamano S., Aoyama T., McBride O.W., Hardwick J.P., Gelboin H.V., Gonzalez F.J. Human NADPH-P450 oxidoreductase: complementary DNA cloning, sequence and vaccinia virus-mediated expression and localization of the CYPOR gene to chromosome 7. Mol. Pharmacol. (1989) 36 83 88.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 83-88
    • Yamano, S.1    Aoyama, T.2    McBride, O.W.3    Hardwick, J.P.4    Gelboin, H.V.5    Gonzalez, F.J.6
  • 3
    • 34347219795 scopus 로고    scopus 로고
    • Apparent manifesting heterozygosity in p450 oxidoreductase deficiency and its effect on coexisting 21-hydroxylase deficiency
    • Scott R.R., Gomes L.G., Huang N., Van Vliet G., Miller W.L. Apparent manifesting heterozygosity in p450 oxidoreductase deficiency and its effect on coexisting 21-hydroxylase deficiency. J. Clin. Endocrinol. Metab. (2007) 92 2318 2322.
    • (2007) J. Clin. Endocrinol. Metab. , vol.92 , pp. 2318-2322
    • Scott, R.R.1    Gomes, L.G.2    Huang, N.3    Van Vliet, G.4    Miller, W.L.5
  • 4
    • 0000305842 scopus 로고
    • The reduction of cytochrome c by xanthine oxidase
    • Horecker B.L., Heppel L.A. The reduction of cytochrome c by xanthine oxidase. J. Biol. Chem. (1949) 178 683 690.
    • (1949) J. Biol. Chem. , vol.178 , pp. 683-690
    • Horecker, B.L.1    Heppel, L.A.2
  • 5
    • 0004563140 scopus 로고
    • Triphosphopyridine nucleotide-cytochrome c reductase in liver
    • Horecker B.L. Triphosphopyridine nucleotide-cytochrome c reductase in liver. J. Biol. Chem. (1950) 183 593 605.
    • (1950) J. Biol. Chem. , vol.183 , pp. 593-605
    • Horecker, B.L.1
  • 6
    • 73649173283 scopus 로고
    • Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver
    • Williams C.H. Jr., Kamin H. Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver. J. Biol. Chem. (1962) 237 587 595.
    • (1962) J. Biol. Chem. , vol.237 , pp. 587-595
    • Williams Jr., C.H.1    Kamin, H.2
  • 7
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide-cytochrome c reductase: Isolation, characterization, and kinetic studies
    • Phillips A.H., Langdon R.G. Hepatic triphosphopyridine nucleotide-cytochrome c reductase: isolation, characterization, and kinetic studies. J. Biol. Chem. (1962) 237 2652 2660.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2652-2660
    • Phillips, A.H.1    Langdon, R.G.2
  • 8
    • 0014670327 scopus 로고
    • Resolution of the cytochrome P-450-containing ω-hydroxylation system of liver microsomes into three components
    • Lu A.Y., Junk K.W., Coon M.J. Resolution of the cytochrome P-450-containing ω-hydroxylation system of liver microsomes into three components. J. Biol. Chem. (1969) 244 3714 3721.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3714-3721
    • Lu, A.Y.1    Junk, K.W.2    Coon, M.J.3
  • 9
    • 0016641043 scopus 로고
    • Solubilization and partial characterization of rat liver squalene epoxidase
    • Ono T., Bloch K. Solubilization and partial characterization of rat liver squalene epoxidase. J. Biol. Chem. (1975) 250 1571 1579.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1571-1579
    • Ono, T.1    Bloch, K.2
  • 11
    • 0021093258 scopus 로고
    • Possible involvement of NADPH-cytochrome P450 reductase and cytochrome b5 on beta-ketostearoyl-CoA reduction in microsomal fatty acid chain elongation supported by NADPH
    • Nagao M., Ishibashi T., Okayasu T., Imai Y. Possible involvement of NADPH-cytochrome P450 reductase and cytochrome b5 on beta-ketostearoyl-CoA reduction in microsomal fatty acid chain elongation supported by NADPH. FEBS Lett. (1983) 155 11 14.
    • (1983) FEBS Lett. , vol.155 , pp. 11-14
    • Nagao, M.1    Ishibashi, T.2    Okayasu, T.3    Imai, Y.4
  • 12
    • 23744510839 scopus 로고    scopus 로고
    • Reduction of cytochrome b5 by NADPH-cytochrome P450 reductase
    • Guengerich F.P. Reduction of cytochrome b5 by NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. (2005) 440 204 211.
    • (2005) Arch. Biochem. Biophys. , vol.440 , pp. 204-211
    • Guengerich, F.P.1
  • 13
    • 0018801347 scopus 로고
    • Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase
    • Enoch H.G., Strittmatter P. Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase. J. Biol. Chem. (1979) 254 8976 8981.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8976-8981
    • Enoch, H.G.1    Strittmatter, P.2
  • 14
    • 0015501157 scopus 로고
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
    • Schacter B.A., Meyer U.A., Marver H.S. Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system. J. Biol. Chem. (1972) 247 3601 3607.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3601-3607
    • Schacter, B.A.1    Meyer, U.A.2    Marver, H.S.3
  • 15
    • 0015514943 scopus 로고
    • Hemoprotein catabolism during stimulation of microsomal lipid peroxidation
    • Schacter B.A., Meyer U.A., Marver H.S. Hemoprotein catabolism during stimulation of microsomal lipid peroxidation. Biochim. Biophys. Acta (1972) 279 221 227.
    • (1972) Biochim. Biophys. Acta , vol.279 , pp. 221-227
    • Schacter, B.A.1    Meyer, U.A.2    Marver, H.S.3
  • 16
    • 0034652106 scopus 로고    scopus 로고
    • Evidence for requirement of NADPH-cytochrome P450 oxidoreductase in the microsomal NADPH-sterol Delta7-reductase system
    • Nishino H., Ishibashi T. Evidence for requirement of NADPH-cytochrome P450 oxidoreductase in the microsomal NADPH-sterol Delta7-reductase system. Arch. Biochem. Biophys. (2000) 374 293 298.
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 293-298
    • Nishino, H.1    Ishibashi, T.2
  • 17
    • 0037155271 scopus 로고    scopus 로고
    • Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase
    • Shen A.L., O'Leary K.A., Kasper C.B. Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase. J. Biol. Chem. (2002) 277 6536 6541.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6536-6541
    • Shen, A.L.1    O'Leary, K.A.2    Kasper, C.B.3
  • 18
    • 0041468898 scopus 로고    scopus 로고
    • Identification of novel roles of the cytochrome P450 system in early embryogenesis: Effects on vasculogenesis and retinoic acid homeostasis
    • Otto D.M., Henderson C.J., Carrie D. et al. Identification of novel roles of the cytochrome P450 system in early embryogenesis: effects on vasculogenesis and retinoic acid homeostasis. Mol. Cell Biol. (2003) 23 6103 6116.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6103-6116
    • Otto, D.M.1    Henderson, C.J.2    Carrie, D.3
  • 19
    • 0038507099 scopus 로고    scopus 로고
    • Liver-specific deletion of the NADPH-cytochrome P450 reductase gene: Impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase
    • Gu J., Weng Y., Zhang Q.Y. et al. Liver-specific deletion of the NADPH-cytochrome P450 reductase gene: impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase. J. Biol. Chem. (2003) 278 25895 25901.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25895-25901
    • Gu, J.1    Weng, Y.2    Zhang, Q.Y.3
  • 20
    • 0037790603 scopus 로고    scopus 로고
    • Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase
    • Henderson C.J., Otto D.M., Carrie D. et al. Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase. J. Biol. Chem. (2003) 278 13480 13486.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13480-13486
    • Henderson, C.J.1    Otto, D.M.2    Carrie, D.3
  • 21
    • 19944426178 scopus 로고    scopus 로고
    • Transgenic mice with a hypomorphic NADPH-cytochrome P450 reductase gene: Effects on development, reproduction, and microsomal cytochrome P450
    • Wu L., Gu J., Cui H. et al. Transgenic mice with a hypomorphic NADPH-cytochrome P450 reductase gene: effects on development, reproduction, and microsomal cytochrome P450. J. Pharmacol. Exp. Ther. (2005) 312 35 43.
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 35-43
    • Wu, L.1    Gu, J.2    Cui, H.3
  • 22
    • 0022590907 scopus 로고
    • Congenital adrenal hyperplasia
    • Miller W.L. Congenital adrenal hyperplasia. N. Engl. J. Med. (1986) 314 1321 1322.
    • (1986) N. Engl. J. Med. , vol.314 , pp. 1321-1322
    • Miller, W.L.1
  • 23
    • 10744224515 scopus 로고    scopus 로고
    • Mutant P450 oxidoreductase causes disordered steroidogenesis with and without Antley-Bixler syndrome
    • Flück C.E., Tajima T., Pandey A.V. et al. Mutant P450 oxidoreductase causes disordered steroidogenesis with and without Antley-Bixler syndrome. Nat. Genet. (2004) 36 228 230.
    • (2004) Nat. Genet. , vol.36 , pp. 228-230
    • Flück, C.E.1    Tajima, T.2    Pandey, A.V.3
  • 24
    • 11244288204 scopus 로고    scopus 로고
    • P450 oxidoreductase deficiency: A new disorder of steroidogenesis affecting all microsomal P450 enzymes
    • Pandey A.V., Flück C.E., Huang N., Tajima T., Fujieda K., Miller W.L. P450 oxidoreductase deficiency: A new disorder of steroidogenesis affecting all microsomal P450 enzymes. Endocrinol. Res. (2004) 30 881 888.
    • (2004) Endocrinol. Res. , vol.30 , pp. 881-888
    • Pandey, A.V.1    Flück, C.E.2    Huang, N.3    Tajima, T.4    Fujieda, K.5    Miller, W.L.6
  • 26
    • 3042613405 scopus 로고    scopus 로고
    • Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase and human androgen synthesis: Analytical study
    • Arlt W., Walker E.A., Draper N. et al. Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase and human androgen synthesis: analytical study. Lancet (2004) 363 2128 2135.
    • (2004) Lancet , vol.363 , pp. 2128-2135
    • Arlt, W.1    Walker, E.A.2    Draper, N.3
  • 27
    • 20244367932 scopus 로고    scopus 로고
    • Diversity and function of mutations in p450 oxidoreductase in patients with Antley-Bixler syndrome and disordered steroidogenesis
    • Huang N., Pandey A.V., Agrawal V. Diversity and function of mutations in p450 oxidoreductase in patients with Antley-Bixler syndrome and disordered steroidogenesis. Am. J. Hum. Genet. (2005) 76 729 749.
    • (2005) Am. J. Hum. Genet. , vol.76 , pp. 729-749
    • Huang, N.1    Pandey, A.V.2    Agrawal, V.3
  • 28
    • 3342918965 scopus 로고    scopus 로고
    • Compound heterozygous mutations of cytochrome P450 oxidoreductase gene (POR) in two patients with Antley-Bixler syndrome
    • Adachi M., Tachibana K., Asakura Y., Yamamoto T., Hanaki K., Oka A. Compound heterozygous mutations of cytochrome P450 oxidoreductase gene (POR) in two patients with Antley-Bixler syndrome. Am. J. Med. Genet. (2004) 128A 333 339.
    • (2004) Am. J. Med. Genet. , vol.128 , pp. 333-339
    • Adachi, M.1    Tachibana, K.2    Asakura, Y.3    Yamamoto, T.4    Hanaki, K.5    Oka, A.6
  • 29
    • 19944429961 scopus 로고    scopus 로고
    • Cytochrome P450 oxidoreductase gene mutations and Antley-Bixler syndrome with abnormal genitalia and/or impaired steroidogenesis: Molecular and clinical studies in 10 patients
    • Fukami M., Horikawa R., Nagai T. et al. Cytochrome P450 oxidoreductase gene mutations and Antley-Bixler syndrome with abnormal genitalia and/or impaired steroidogenesis: molecular and clinical studies in 10 patients. J. Clin. Endocrinol. Metab. (2005) 90 414 426.
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , pp. 414-426
    • Fukami, M.1    Horikawa, R.2    Nagai, T.3
  • 30
    • 33644862230 scopus 로고    scopus 로고
    • POR R457H is a global founder mutation causing Antley-Bixler syndrome with autosomal recessive trait
    • Adachi M., Asakura Y., Matsuo M., Yamamoto T., Hanaki K., Arlt W. POR R457H is a global founder mutation causing Antley-Bixler syndrome with autosomal recessive trait. Am. J. Med. Genet. A (2006) 140 633 635.
    • (2006) Am. J. Med. Genet. a , vol.140 , pp. 633-635
    • Adachi, M.1    Asakura, Y.2    Matsuo, M.3    Yamamoto, T.4    Hanaki, K.5    Arlt, W.6
  • 31
    • 33745790703 scopus 로고    scopus 로고
    • Urine steroid hormone profile analysis in cytochrome P450 oxidoreductase deficiency: Implication for the backdoor pathway to dihydrotestosterone
    • Homma K., Hasegawa T., Nagai T. et al. Urine steroid hormone profile analysis in cytochrome P450 oxidoreductase deficiency: implication for the backdoor pathway to dihydrotestosterone. J. Clin. Endocrinol. Metab. (2006) 91 2643 2649.
    • (2006) J. Clin. Endocrinol. Metab. , vol.91 , pp. 2643-2649
    • Homma, K.1    Hasegawa, T.2    Nagai, T.3
  • 32
    • 33646691530 scopus 로고    scopus 로고
    • Cytochrome P450 oxidoreductase deficiency in three patients initially regarded as having 21-hydroxylase deficiency and/or aromatase deficiency: Diagnostic value of urine steroid hormone analysis
    • Fukami M., Hasegawa T., Horikawa R. et al. Cytochrome P450 oxidoreductase deficiency in three patients initially regarded as having 21-hydroxylase deficiency and/or aromatase deficiency: diagnostic value of urine steroid hormone analysis. Pediatr. Res. (2006) 59 276 280.
    • (2006) Pediatr. Res. , vol.59 , pp. 276-280
    • Fukami, M.1    Hasegawa, T.2    Horikawa, R.3
  • 33
    • 34248582836 scopus 로고    scopus 로고
    • A variant in the cytochrome p450 oxidoreductase gene is associated with breast cancer risk in African Americans
    • Haiman C.A., Setiawan V.W., Xia L.Y. et al. A variant in the cytochrome p450 oxidoreductase gene is associated with breast cancer risk in African Americans. Cancer Res. (2007) 67 3565 3568.
    • (2007) Cancer Res. , vol.67 , pp. 3565-3568
    • Haiman, C.A.1    Setiawan, V.W.2    Xia, L.Y.3
  • 34
    • 0022374725 scopus 로고
    • Male pseudohermaphroditism due to multiple defects in steroid-biosynthetic microsomal mixed-function oxidases. a new variant of congenital adrenal hyperplasia
    • Peterson R.E., Imperato-McGinley J., Gautier T., Shackleton C.H.L. Male pseudohermaphroditism due to multiple defects in steroid-biosynthetic microsomal mixed-function oxidases. A new variant of congenital adrenal hyperplasia. N. Engl. J. Med. (1985) 313 1182 1191.
    • (1985) N. Engl. J. Med. , vol.313 , pp. 1182-1191
    • Peterson, R.E.1    Imperato-Mcginley, J.2    Gautier, T.3    Shackleton, C.H.L.4
  • 35
    • 4344591415 scopus 로고    scopus 로고
    • Prenatal diagnosis of P450 oxidoreductase deficiency (ORD): A disorder causing low pregnancy estriol, maternal and fetal virilization, and the Antley-Bixler syndrome phenotype
    • Shackleton C., Marcos J., Arlt W., Hauffa B.P. Prenatal diagnosis of P450 oxidoreductase deficiency (ORD): a disorder causing low pregnancy estriol, maternal and fetal virilization, and the Antley-Bixler syndrome phenotype. Am. J. Med. Genet. (2004) 129A 105 112.
    • (2004) Am. J. Med. Genet. , vol.129 , pp. 105-112
    • Shackleton, C.1    Marcos, J.2    Arlt, W.3    Hauffa, B.P.4
  • 36
    • 0034059969 scopus 로고    scopus 로고
    • Evidence for digenic inheritance in some cases of Antley-Bixler syndrome?
    • Reardon W., Smith A., Honour J.W. et al. Evidence for digenic inheritance in some cases of Antley-Bixler syndrome? J. Med. Genet. (2000) 37 26 32.
    • (2000) J. Med. Genet. , vol.37 , pp. 26-32
    • Reardon, W.1    Smith, A.2    Honour, J.W.3
  • 37
    • 0037408258 scopus 로고    scopus 로고
    • Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes
    • Backes W.L., Kelley R.W. Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes. Pharmacol. Ther. (2003) 98 221 233.
    • (2003) Pharmacol. Ther. , vol.98 , pp. 221-233
    • Backes, W.L.1    Kelley, R.W.2
  • 38
    • 0038650809 scopus 로고    scopus 로고
    • Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues
    • Gutierrez A., Munro A.W., Grunau A., Wolf C.R., Scrutton N.S., Roberts G.C. Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues. Eur. J. Biochem. (2003) 270 2612 2621.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2612-2621
    • Gutierrez, A.1    Munro, A.W.2    Grunau, A.3    Wolf, C.R.4    Scrutton, N.S.5    Roberts, G.C.6
  • 39
    • 0015795938 scopus 로고
    • Some properties of hepatic reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase
    • Iyanagi T., Mason H.S. Some properties of hepatic reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase. Biochemistry (1973) 12 2297 2308.
    • (1973) Biochemistry , vol.12 , pp. 2297-2308
    • Iyanagi, T.1    Mason, H.S.2
  • 40
    • 0035916295 scopus 로고    scopus 로고
    • Determination of the redox properties of human NADPH-cytochrome P450 reductase
    • Munro A.W., Noble M.A., Rabledo L., Daff S.N., Chapman S.K. Determination of the redox properties of human NADPH-cytochrome P450 reductase. Biochemistry (2001) 40 1956 1963.
    • (2001) Biochemistry , vol.40 , pp. 1956-1963
    • Munro, A.W.1    Noble, M.A.2    Rabledo, L.3    Daff, S.N.4    Chapman, S.K.5
  • 41
    • 0035800760 scopus 로고    scopus 로고
    • NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer
    • Hubbard P.A., Shen A.L., Paschke R., Kasper C.B., Kim J.J. NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer. J. Biol. Chem. (2001) 276 29163 29170.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29163-29170
    • Hubbard, P.A.1    Shen, A.L.2    Paschke, R.3    Kasper, C.B.4    Kim, J.J.5
  • 42
    • 0030873316 scopus 로고    scopus 로고
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
    • Wang M., Roberts D.L., Paschke R., Shea T.M., Masters B.S.S., Kim J.J. Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Proc. Natl Acad. Sci. USA (1997) 94 8411 8416.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8411-8416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.S.S.5    Kim, J.J.6
  • 43
    • 0038152781 scopus 로고    scopus 로고
    • Chimeric enzymes of cytochrome P450 oxidoreductase and neuronal nitric-oxide synthase reductase domain reveal structural and functional differences
    • Roman L.J., McLain J., Masters B.S.S. Chimeric enzymes of cytochrome P450 oxidoreductase and neuronal nitric-oxide synthase reductase domain reveal structural and functional differences. J. Biol. Chem. (2003) 278 25700 25707.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25700-25707
    • Roman, L.J.1    McLain, J.2    Masters, B.S.S.3
  • 44
    • 0032539512 scopus 로고    scopus 로고
    • Glu-320 and Asp-323 are determinants of the CYP4A1 hydroxylation regiospecificity and resistance to inactivation by 1-aminobenzotriazole
    • Dierks E.A., Davis S.C., Ortiz de Montellano P.R. Glu-320 and Asp-323 are determinants of the CYP4A1 hydroxylation regiospecificity and resistance to inactivation by 1-aminobenzotriazole. Biochemistry (1998) 37 1839 1847.
    • (1998) Biochemistry , vol.37 , pp. 1839-1847
    • Dierks, E.A.1    Davis, S.C.2    Ortiz De Montellano, P.R.3
  • 46
    • 0029776005 scopus 로고    scopus 로고
    • Yeast expression of animal and plant P450s in optimized redox environments
    • Pompon D., Louerat B., Bronine A., Urban P. Yeast expression of animal and plant P450s in optimized redox environments. Methods Enzymol. (1996) 272 51 64.
    • (1996) Methods Enzymol. , vol.272 , pp. 51-64
    • Pompon, D.1    Louerat, B.2    Bronine, A.3    Urban, P.4
  • 47
    • 0027742081 scopus 로고
    • Xenobiotic metabolism in humanized yeast: Engineered yeast cells producing human NADPH-cytochrome P-450 reductase, cytochrome b5, epoxide hydrolase and P-450s
    • Urban P., Truan G., Gautier J.C., Pompon D. Xenobiotic metabolism in humanized yeast: engineered yeast cells producing human NADPH-cytochrome P-450 reductase, cytochrome b5, epoxide hydrolase and P-450s. Biochem. Soc. Trans. (1993) 21 1028 1034.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 1028-1034
    • Urban, P.1    Truan, G.2    Gautier, J.C.3    Pompon, D.4
  • 48
    • 0037474198 scopus 로고    scopus 로고
    • Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17
    • Pandey A.V., Mellon S.H., Miller W.L. Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17. J. Biol. Chem. (2003) 278 2837 2844.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2837-2844
    • Pandey, A.V.1    Mellon, S.H.2    Miller, W.L.3
  • 49
    • 17144426051 scopus 로고    scopus 로고
    • Regulation of 17,20 lyase activity by cytochrome b5 and by serine phosphorylation of P450c17
    • Pandey A.V., Miller W.L. Regulation of 17,20 lyase activity by cytochrome b5 and by serine phosphorylation of P450c17. J. Biol. Chem. (2005) 280 13265 13271.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13265-13271
    • Pandey, A.V.1    Miller, W.L.2
  • 50
    • 0032488666 scopus 로고    scopus 로고
    • Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer
    • Auchus R.J., Lee T.C., Miller W.L. Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer. J. Biol. Chem. (1998) 273 3158 3165.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 51
    • 0028786656 scopus 로고
    • Serine phosphorylation of human P450c17 increases 17,20-lyase activity: Implications for adrenarche and the polycystic ovary syndrome
    • Zhang L.H., Rodriguez H., Ohno S., Miller W.L. Serine phosphorylation of human P450c17 increases 17,20-lyase activity: implications for adrenarche and the polycystic ovary syndrome. Proc. Natl Acad. Sci. USA (1995) 92 10619 10623.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10619-10623
    • Zhang, L.H.1    Rodriguez, H.2    Ohno, S.3    Miller, W.L.4
  • 52
    • 0022997597 scopus 로고
    • Role of electron transport in the regulation of the lyase activity of C21 side-chain cleavage P-450 from porcine adrenal and testicular microsomes
    • Yanagibashi K., Hall P.F. Role of electron transport in the regulation of the lyase activity of C21 side-chain cleavage P-450 from porcine adrenal and testicular microsomes. J. Biol. Chem. (1986) 261 8429 8433.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8429-8433
    • Yanagibashi, K.1    Hall, P.F.2
  • 53
    • 33845936862 scopus 로고    scopus 로고
    • Genetic variation of human cytochrome p450 reductase as a potential biomarker for mitomycin C-induced cytotoxicity
    • Wang S.L., Han J.F., He X.Y., Wang X.R., Hong J.Y. Genetic variation of human cytochrome p450 reductase as a potential biomarker for mitomycin C-induced cytotoxicity. Drug Metab. Dispos. (2007) 35 176 179.
    • (2007) Drug Metab. Dispos. , vol.35 , pp. 176-179
    • Wang, S.L.1    Han, J.F.2    He, X.Y.3    Wang, X.R.4    Hong, J.Y.5
  • 54
    • 0030458025 scopus 로고    scopus 로고
    • Interactions of cytochrome P450 2B4 with NADPH-cytochrome P450 reductase studied by fluorescent probe
    • Davydov D.R., Knyushko T.V., Kanaeva I.P. et al. Interactions of cytochrome P450 2B4 with NADPH-cytochrome P450 reductase studied by fluorescent probe. Biochimie (1996) 78 734 743.
    • (1996) Biochimie , vol.78 , pp. 734-743
    • Davydov, D.R.1    Knyushko, T.V.2    Kanaeva, I.P.3
  • 55
    • 0030781147 scopus 로고    scopus 로고
    • Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: Rapid reduction in the absence of substrate and variations among cytochrome P450 systems
    • Guengerich F.P., Johnson W.W. Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems. Biochemistry (1997) 36 14741 14750.
    • (1997) Biochemistry , vol.36 , pp. 14741-14750
    • Guengerich, F.P.1    Johnson, W.W.2
  • 56
    • 0023972392 scopus 로고
    • Role of electrostatic interactions in the reaction of NADPH-cytochrome P-450 reductase with cytochromes P-450
    • Nadler S.G., Strobel H.W. Role of electrostatic interactions in the reaction of NADPH-cytochrome P-450 reductase with cytochromes P-450. Arch. Biochem. Biophys. (1988) 261 418 429.
    • (1988) Arch. Biochem. Biophys. , vol.261 , pp. 418-429
    • Nadler, S.G.1    Strobel, H.W.2
  • 57
    • 0028805425 scopus 로고
    • Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c
    • Shen A.L., Kasper C.B. Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c. J. Biol. Chem. (1995) 270 27475 27480.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27475-27480
    • Shen, A.L.1    Kasper, C.B.2
  • 58
    • 0025939628 scopus 로고
    • Identification and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450
    • Nadler S.G., Strobel H.W. Identification and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450. Arch. Biochem. Biophys. (1991) 290 277 284.
    • (1991) Arch. Biochem. Biophys. , vol.290 , pp. 277-284
    • Nadler, S.G.1    Strobel, H.W.2
  • 59
    • 0027216444 scopus 로고
    • Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase
    • Shen S., Strobel H.W. Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. (1993) 304 257 265.
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 257-265
    • Shen, S.1    Strobel, H.W.2
  • 60
    • 0026589172 scopus 로고
    • The role of cytochrome P450 lysine residues in the interaction between cytochrome P450IA1 and NADPH-cytochrome P450 reductase
    • Shen S., Strobel H.W. The role of cytochrome P450 lysine residues in the interaction between cytochrome P450IA1 and NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. (1992) 294 83 90.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 83-90
    • Shen, S.1    Strobel, H.W.2
  • 61
    • 0025755694 scopus 로고
    • Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase
    • Shimizu T., Tateishi T., Hatano M., Fujii-Kuriyama Y. Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase. J. Biol. Chem. (1991) 266 3372 3375.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3372-3375
    • Shimizu, T.1    Tateishi, T.2    Hatano, M.3    Fujii-Kuriyama, Y.4
  • 62
    • 0023028914 scopus 로고
    • Localization of cytochrome c-binding domain on NADPH-cytochrome P-450 reductase
    • Nisimoto Y. Localization of cytochrome c-binding domain on NADPH-cytochrome P-450 reductase. J. Biol. Chem. (1986) 261 14232 14239.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14232-14239
    • Nisimoto, Y.1
  • 63
    • 0030249221 scopus 로고    scopus 로고
    • The interaction of NADPH-P450 reductase with P450: An electrochemical study of the role of the flavin mononucleotide-binding domain
    • Estabrook R.W., Shet M.S., Fisher C.W., Jenkins C.M., Waterman M.R. The interaction of NADPH-P450 reductase with P450: an electrochemical study of the role of the flavin mononucleotide-binding domain. Arch. Biochem. Biophys. (1996) 333 308 315.
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 308-315
    • Estabrook, R.W.1    Shet, M.S.2    Fisher, C.W.3    Jenkins, C.M.4    Waterman, M.R.5
  • 64
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: A comparative analysis of three crystal structures
    • Hasemann C.A., Kurumbail R.G., Boddupalli S.S., Peterson J.A., Deisenhofer J. Structure and function of cytochromes P450: a comparative analysis of three crystal structures. Structure (1995) 3 41 62.
    • (1995) Structure , vol.3 , pp. 41-62
    • Hasemann, C.A.1    Kurumbail, R.G.2    Boddupalli, S.S.3    Peterson, J.A.4    Deisenhofer, J.5
  • 65
    • 0029738284 scopus 로고    scopus 로고
    • Construction of plasmids and expression in Escherichia coli of enzymatically active fusion proteins containing the heme-domain of a P450 linked to NADPH-P450 reductase
    • Fisher C.W., Shet M.S., Estabrook R.W. Construction of plasmids and expression in Escherichia coli of enzymatically active fusion proteins containing the heme-domain of a P450 linked to NADPH-P450 reductase. Methods Enzymol. (1996) 272 15 25.
    • (1996) Methods Enzymol. , vol.272 , pp. 15-25
    • Fisher, C.W.1    Shet, M.S.2    Estabrook, R.W.3
  • 66
    • 0034733026 scopus 로고    scopus 로고
    • Association of cytochromes P450 with their reductases: Opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system
    • Davydov D.R., Kariakin A.A., PetushKova N.A., Peterson J.A. Association of cytochromes P450 with their reductases: opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system. Biochemistry (2000) 39 6489 6497.
    • (2000) Biochemistry , vol.39 , pp. 6489-6497
    • Davydov, D.R.1    Kariakin, A.A.2    Petushkova, N.A.3    Peterson, J.A.4
  • 67
    • 0024441228 scopus 로고
    • Cytochrome P-450: Cytochrome P-450 reductase interactions
    • Strobel H.W., Nadler S.G., Nelson D.R. Cytochrome P-450: cytochrome P-450 reductase interactions. Drug Metab. Rev. (1989) 20 519 533.
    • (1989) Drug Metab. Rev. , vol.20 , pp. 519-533
    • Strobel, H.W.1    Nadler, S.G.2    Nelson, D.R.3
  • 68
    • 0024516824 scopus 로고
    • CDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases
    • Hanukoglu I., Gutfinger T. cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases. Eur. J. Biochem. (1989) 180 479 484.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 479-484
    • Hanukoglu, I.1    Gutfinger, T.2
  • 69
    • 0026023225 scopus 로고
    • Atomic structure of ferredoxin-NADP+ reductase: Prototype for a structurally novel flavoenzyme family
    • Karplus P.A., Daniels M.J., Herriott J.R. Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family. Science (1991) 251 60 66.
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 70
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • Bredt D.S., Hwang P.M., Glatt C.E., Lowenstein C., Reed R.R., Snyder S.H. Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature (1991) 351 714 718.
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5    Snyder, S.H.6
  • 71
    • 0024518203 scopus 로고
    • Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis
    • Shen A.L., Porter T.D., Wilson T.E., Kasper C.B. Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis. J. Biol. Chem. (1989) 264 7584 7589.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7584-7589
    • Shen, A.L.1    Porter, T.D.2    Wilson, T.E.3    Kasper, C.B.4
  • 72
    • 0034731525 scopus 로고    scopus 로고
    • Differential contributions of NADPH-cytochrome P450 oxidoreductase FAD binding site residues to flavin binding and catalysis
    • Shen A.L., Kasper C.B. Differential contributions of NADPH-cytochrome P450 oxidoreductase FAD binding site residues to flavin binding and catalysis. J. Biol. Chem. (2000) 275 41087 41091.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41087-41091
    • Shen, A.L.1    Kasper, C.B.2
  • 73
    • 0029759441 scopus 로고    scopus 로고
    • Role of Ser457 of NADPH-cytochrome P450 oxidoreductase in catalysis and control of FAD oxidation-reduction potential
    • Shen A.L., Kasper C.B. Role of Ser457 of NADPH-cytochrome P450 oxidoreductase in catalysis and control of FAD oxidation-reduction potential. Biochemistry (1996) 35 9451 9459.
    • (1996) Biochemistry , vol.35 , pp. 9451-9459
    • Shen, A.L.1    Kasper, C.B.2
  • 74
    • 0033605237 scopus 로고    scopus 로고
    • Mechanistic studies on the reductive half-reaction of NADPH-cytochrome P450 oxidoreductase
    • Shen A.L., Sem D.S., Kasper C.B. Mechanistic studies on the reductive half-reaction of NADPH-cytochrome P450 oxidoreductase. J. Biol. Chem. (1999) 274 5391 5398.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5391-5398
    • Shen, A.L.1    Sem, D.S.2    Kasper, C.B.3
  • 75
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton N.S., Berry A., Perham R.N. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature (1990) 343 38 43.
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 76
    • 0024420756 scopus 로고
    • Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: Complete sequence of human enzyme and NADPH-binding sites
    • Haniu M., McManus M.E., Birkett D.J., Lee T.D., Shively J.E. Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites. Biochemistry (1989) 28 8639 8645.
    • (1989) Biochemistry , vol.28 , pp. 8639-8645
    • Haniu, M.1    McManus, M.E.2    Birkett, D.J.3    Lee, T.D.4    Shively, J.E.5
  • 77
    • 0025885546 scopus 로고
    • NADPH-cytochrome P-450 oxidoreductase. the role of cysteine 566 in catalysis and cofactor binding
    • Shen A.L., Christensen M.J., Kasper C.B. NADPH-cytochrome P-450 oxidoreductase. The role of cysteine 566 in catalysis and cofactor binding. J. Biol. Chem. (1991) 266 19976 19980.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19976-19980
    • Shen, A.L.1    Christensen, M.J.2    Kasper, C.B.3
  • 78
    • 0021739143 scopus 로고
    • Structural analysis of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes. Sequences of proteolytic fragments, cysteine-containing peptides, and a NADPH-protected cysteine peptide
    • Haniu M., Iyanagi T., Legesse K., Shively J.E. Structural analysis of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes. Sequences of proteolytic fragments, cysteine-containing peptides, and a NADPH-protected cysteine peptide. J. Biol. Chem. (1984) 259 13703 13711.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13703-13711
    • Haniu, M.1    Iyanagi, T.2    Legesse, K.3    Shively, J.E.4


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