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Volumn 82, Issue , 2014, Pages 116-122

Heterologous expression and functional characterization of the NADPH-cytochrome P450 reductase from Capsicum annuum

Author keywords

Cytochrome P450; Doxorubicin; Heterologous expression; Plant NADPH cytochrome P450 reductase; Tetrazolium salts

Indexed keywords

CYTOCHROME B5; CYTOCHROME C; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

EID: 84902330198     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2014.05.010     Document Type: Article
Times cited : (20)

References (28)
  • 3
    • 0032865951 scopus 로고    scopus 로고
    • Reduction of a tetrazolium salt, CTC, by intact HepG2 human hepatoma cells: subcellular localisation of reducing systems
    • Bernas T., Dobrucki J. Reduction of a tetrazolium salt, CTC, by intact HepG2 human hepatoma cells: subcellular localisation of reducing systems. Biochim. Biophys. Acta 1999, 1451:73-81.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 73-81
    • Bernas, T.1    Dobrucki, J.2
  • 5
    • 58549119938 scopus 로고    scopus 로고
    • CDNA cloning and functional characterisation of CYP98A14 and NADPH:cytochrome P450 reductase from Coleus blumei involved in rosmarinic acid biosynthesis
    • Eberle D., Ullmann P., Werck-Reichhart D., Petersen M. cDNA cloning and functional characterisation of CYP98A14 and NADPH:cytochrome P450 reductase from Coleus blumei involved in rosmarinic acid biosynthesis. Plant Mol. Biol. 2009, 69:239-253.
    • (2009) Plant Mol. Biol. , vol.69 , pp. 239-253
    • Eberle, D.1    Ullmann, P.2    Werck-Reichhart, D.3    Petersen, M.4
  • 6
    • 0018354912 scopus 로고
    • Properties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes
    • French J.S., Coon M.J. Properties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes. Arch. Biochem. Biophys. 1979, 195:565-577.
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 565-577
    • French, J.S.1    Coon, M.J.2
  • 7
    • 0031822496 scopus 로고    scopus 로고
    • Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities
    • Hanna I.H., Teiber J.F., Kokones K.L., Hollenberg P.F. Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities. Arch. Biochem. Biophys. 1998, 350:324-332.
    • (1998) Arch. Biochem. Biophys. , vol.350 , pp. 324-332
    • Hanna, I.H.1    Teiber, J.F.2    Kokones, K.L.3    Hollenberg, P.F.4
  • 8
    • 0028786298 scopus 로고
    • Cinnamate 4-hydroxylase from Catharanthus roseus, and a strategy for the functional expression of plant cytochrome P450 proteins as translational fusions with P450 reductase in Escherichia coli
    • Hotze M., Schröder G., Schröder J. Cinnamate 4-hydroxylase from Catharanthus roseus, and a strategy for the functional expression of plant cytochrome P450 proteins as translational fusions with P450 reductase in Escherichia coli. FEBS Lett. 1995, 374:345-350.
    • (1995) FEBS Lett. , vol.374 , pp. 345-350
    • Hotze, M.1    Schröder, G.2    Schröder, J.3
  • 9
    • 0034089214 scopus 로고    scopus 로고
    • Bacterial expression and purification of the Arabidopsis NADPH-cytochrome P450 reductase ATR2
    • Hull A.K., Celenza J.L. Bacterial expression and purification of the Arabidopsis NADPH-cytochrome P450 reductase ATR2. Protein Expr. Purif. 2000, 18:310-315.
    • (2000) Protein Expr. Purif. , vol.18 , pp. 310-315
    • Hull, A.K.1    Celenza, J.L.2
  • 10
    • 73649131594 scopus 로고    scopus 로고
    • Plant NADPH-cytochrome P450 oxidoreductases
    • Jensen K., Møller B.L. Plant NADPH-cytochrome P450 oxidoreductases. Phytochem 2010, 71:132-141.
    • (2010) Phytochem , vol.71 , pp. 132-141
    • Jensen, K.1    Møller, B.L.2
  • 11
    • 37349017983 scopus 로고    scopus 로고
    • Heterologous expression and characterization of wild-type human cytochrome P450 1A2 without conventional N-terminal modification in Escherichia coli
    • Kim D.H., Kim K.H., Isin E.M., Guengerich F.P., Chae H.Z., Ahn T., Yun C.H. Heterologous expression and characterization of wild-type human cytochrome P450 1A2 without conventional N-terminal modification in Escherichia coli. Protein Expr. Purif. 2008, 57:188-200.
    • (2008) Protein Expr. Purif. , vol.57 , pp. 188-200
    • Kim, D.H.1    Kim, K.H.2    Isin, E.M.3    Guengerich, F.P.4    Chae, H.Z.5    Ahn, T.6    Yun, C.H.7
  • 12
    • 58149197763 scopus 로고    scopus 로고
    • Continuous spectrofluorometric and spectrophotometric assays for NADPH-cytochrome P450 reductase activity using 5-cyano-2,3-ditolyl tetrazolium chloride
    • Kim D.H., Yim S.K., Kim K.H., Ahn T., Yun C.H. Continuous spectrofluorometric and spectrophotometric assays for NADPH-cytochrome P450 reductase activity using 5-cyano-2,3-ditolyl tetrazolium chloride. Biotechnol. Lett. 2009, 31:271-275.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 271-275
    • Kim, D.H.1    Yim, S.K.2    Kim, K.H.3    Ahn, T.4    Yun, C.H.5
  • 13
    • 33646267951 scopus 로고    scopus 로고
    • Kinetic deuterium isotope effects for 7-alkoxycoumarin O-dealkylation reactions catalysed by human cytochromes P450 and in liver microsomes. Rate-limiting C-H bond breaking in cytochrome P450 1A2 substrate oxidation
    • Kim K.H., Isin E.M., Yun C.H., Kim D.H., Guengerich F.P. Kinetic deuterium isotope effects for 7-alkoxycoumarin O-dealkylation reactions catalysed by human cytochromes P450 and in liver microsomes. Rate-limiting C-H bond breaking in cytochrome P450 1A2 substrate oxidation. FEBS J. 2006, 273:2223-2231.
    • (2006) FEBS J. , vol.273 , pp. 2223-2231
    • Kim, K.H.1    Isin, E.M.2    Yun, C.H.3    Kim, D.H.4    Guengerich, F.P.5
  • 16
    • 84861900283 scopus 로고    scopus 로고
    • Impacts of diversification of cytochrome P450 on plant metabolism
    • Mizutani M. Impacts of diversification of cytochrome P450 on plant metabolism. Biol. Pharm. Bull. 2012, 35:824-832.
    • (2012) Biol. Pharm. Bull. , vol.35 , pp. 824-832
    • Mizutani, M.1
  • 17
    • 0031594283 scopus 로고    scopus 로고
    • Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Gene structure, heterologous expression in insect cells, and differential regulation
    • Mizutani M., Ohta D. Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Gene structure, heterologous expression in insect cells, and differential regulation. Plant Physiol. 1998, 116:357-367.
    • (1998) Plant Physiol. , vol.116 , pp. 357-367
    • Mizutani, M.1    Ohta, D.2
  • 18
    • 0141813521 scopus 로고    scopus 로고
    • Distinct mechanisms of site-specific oxidative DNA damage by doxorubicin in the presence of copper(II) and NADPH-cytochrome P450 reductase
    • Mizutani H., Oikawa S., Hiraku Y., Murata M., Kojima M., Kawanishi S. Distinct mechanisms of site-specific oxidative DNA damage by doxorubicin in the presence of copper(II) and NADPH-cytochrome P450 reductase. Cancer Sci. 2003, 94:686-691.
    • (2003) Cancer Sci. , vol.94 , pp. 686-691
    • Mizutani, H.1    Oikawa, S.2    Hiraku, Y.3    Murata, M.4    Kojima, M.5    Kawanishi, S.6
  • 19
    • 77950941685 scopus 로고    scopus 로고
    • Engineering bacterial cytochrome P450 (P450) BM3 into a prototype with human P450 enzyme activity using indigo formation
    • Park S.H., Kim D.H., Kim D., Kim D.H., Jung H.C., Pan J.G., Ahn T., Kim D., Yun C.H. Engineering bacterial cytochrome P450 (P450) BM3 into a prototype with human P450 enzyme activity using indigo formation. Drug. Metab. Dispos. 2010, 38:732-739.
    • (2010) Drug. Metab. Dispos. , vol.38 , pp. 732-739
    • Park, S.H.1    Kim, D.H.2    Kim, D.3    Kim, D.H.4    Jung, H.C.5    Pan, J.G.6    Ahn, T.7    Kim, D.8    Yun, C.H.9
  • 20
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST©) for groupwise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl M.W., Horgan G.W., Dempfle L. Relative expression software tool (REST©) for groupwise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res. 2002, 30:E36.
    • (2002) Nucleic Acids Res. , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 21
    • 84874308835 scopus 로고    scopus 로고
    • NADPH-cytochrome P450 reductase: molecular cloning and functional characterization of two paralogs from Withania somnifera (L.) dunal
    • Rana S., Lattoo S.K., Dhar N., Razdan S., Bhat W.W., Dhar R.S., Vishwakarma R. NADPH-cytochrome P450 reductase: molecular cloning and functional characterization of two paralogs from Withania somnifera (L.) dunal. PLoS One 2013, 8:e57068.
    • (2013) PLoS One , vol.8
    • Rana, S.1    Lattoo, S.K.2    Dhar, N.3    Razdan, S.4    Bhat, W.W.5    Dhar, R.S.6    Vishwakarma, R.7
  • 22
    • 0036918780 scopus 로고    scopus 로고
    • Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar
    • Ro D.K., Ehlting J., Douglas C.J. Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar. Plant Physiol. 2002, 130:1837-1851.
    • (2002) Plant Physiol. , vol.130 , pp. 1837-1851
    • Ro, D.K.1    Ehlting, J.2    Douglas, C.J.3
  • 23
    • 70449227895 scopus 로고
    • Oxidation of reduced diphosphopyridine nucleotide
    • Schellenberg K.A., Hellerman L. Oxidation of reduced diphosphopyridine nucleotide. J.Biol. Chem. 1958, 231:547-556.
    • (1958) J.Biol. Chem. , vol.231 , pp. 547-556
    • Schellenberg, K.A.1    Hellerman, L.2
  • 24
    • 0022574425 scopus 로고
    • Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction
    • Shimada T., Misono K.S., Guengerich F.P. Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction. J.Biol. Chem. 1986, 261:909-921.
    • (1986) J.Biol. Chem. , vol.261 , pp. 909-921
    • Shimada, T.1    Misono, K.S.2    Guengerich, F.P.3
  • 25
    • 0020851704 scopus 로고
    • Microsomal NADH cytochrome b5 reductase of bovine brain: purification and properties
    • Tamura M., Yubisui T., Takeshita M. Microsomal NADH cytochrome b5 reductase of bovine brain: purification and properties. J.Biochem. 1983, 94:1547-1555.
    • (1983) J.Biochem. , vol.94 , pp. 1547-1555
    • Tamura, M.1    Yubisui, T.2    Takeshita, M.3
  • 26
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 27
    • 0019876543 scopus 로고
    • Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase
    • Vermilion J.L., Ballou D.P., Massey V., Coon M.J. Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase. J.Biol. Chem. 1981, 256:266-277.
    • (1981) J.Biol. Chem. , vol.256 , pp. 266-277
    • Vermilion, J.L.1    Ballou, D.P.2    Massey, V.3    Coon, M.J.4
  • 28
    • 25444487217 scopus 로고    scopus 로고
    • Acontinuous spectrophotometric assay for NADPH-cytochrome P450 reductase activity using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
    • Yim S.K., Yun C.H., Ahn T., Jung H.C., Pan J.G. Acontinuous spectrophotometric assay for NADPH-cytochrome P450 reductase activity using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide. J.Biochem. Mol. Biol. 2005, 38:366-369.
    • (2005) J.Biochem. Mol. Biol. , vol.38 , pp. 366-369
    • Yim, S.K.1    Yun, C.H.2    Ahn, T.3    Jung, H.C.4    Pan, J.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.