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Volumn 190, Issue , 2012, Pages 16-23

Differential expression and functional characterization of the NADPH cytochrome P450 reductase genes from Nothapodytes foetida

Author keywords

Camptothecin; Cytochrome P450; NADPH cytochrome P450 reductase; Nothapodytes foetida

Indexed keywords

CAMPTOTHECIN; COMPLEMENTARY DNA; CYTOCHROME P450; GERANIOL 10 HYDROXYLASE; GERANIOL 10-HYDROXYLASE; MESSENGER RNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; VEGETABLE PROTEIN;

EID: 84859785881     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2012.03.007     Document Type: Article
Times cited : (22)

References (40)
  • 1
    • 0014670327 scopus 로고
    • Resolution of the cytochrome P-450-containing (ω-hydroxylation system of liver microsomes into three components
    • Lu A.Y.H., 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.H.1    Junk, K.W.2    Coon, M.J.3
  • 4
    • 0019877474 scopus 로고
    • Evidence for a new physiological role of hepatic NADPH:ferricytochrome (P-450) oxidoreductase. Direct electron input to the microsomal fatty acid chain elongation system
    • Ilan Z., Ilan R., Cinti D.L. Evidence for a new physiological role of hepatic NADPH:ferricytochrome (P-450) oxidoreductase. Direct electron input to the microsomal fatty acid chain elongation system. J. Biol. Chem. 1981, 256:10066-10072.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10066-10072
    • Ilan, Z.1    Ilan, R.2    Cinti, D.L.3
  • 7
    • 0030852872 scopus 로고    scopus 로고
    • Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5
    • Urban P., Mignotte C., Kazmaier M., Delorme F., Pompon D. Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5. J. Biol. Chem. 1997, 272:19176-19186.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19176-19186
    • Urban, P.1    Mignotte, C.2    Kazmaier, M.3    Delorme, F.4    Pompon, D.5
  • 8
    • 0031594283 scopus 로고    scopus 로고
    • Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana
    • Mizutani M., Ohta D. Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Plant Physiol. 1998, 116:357-367.
    • (1998) Plant Physiol. , vol.116 , pp. 357-367
    • Mizutani, M.1    Ohta, D.2
  • 10
    • 0031464795 scopus 로고    scopus 로고
    • Differentially regulated NADPH:cytochrome P450 oxidoreductases in parsley
    • Koopmann E., Hahlbrock K. Differentially regulated NADPH:cytochrome P450 oxidoreductases in parsley. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:14954-14959.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14954-14959
    • Koopmann, E.1    Hahlbrock, K.2
  • 11
    • 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
  • 12
    • 71849099944 scopus 로고    scopus 로고
    • Characterization of two NADPH:cytochrome P450 reductases from cotton (Gossypium hirsutum)
    • Yang C.Q., Lu S., Mao Y.B., Wang L.J., Chen X.Y. Characterization of two NADPH:cytochrome P450 reductases from cotton (Gossypium hirsutum). Phytochemistry 2010, 71:27-35.
    • (2010) Phytochemistry , vol.71 , pp. 27-35
    • Yang, C.Q.1    Lu, S.2    Mao, Y.B.3    Wang, L.J.4    Chen, X.Y.5
  • 13
    • 64349116223 scopus 로고    scopus 로고
    • Purification, cDNA cloning and functional expression of NADPH-cytochrome P450 reductase from Centaurium erythraea cell cultures
    • Schwarz H., Liu B., Peters S., Barillas W., Beerhues L. Purification, cDNA cloning and functional expression of NADPH-cytochrome P450 reductase from Centaurium erythraea cell cultures. Plant Biol. 2009, 11:300-306.
    • (2009) Plant Biol. , vol.11 , pp. 300-306
    • Schwarz, H.1    Liu, B.2    Peters, S.3    Barillas, W.4    Beerhues, L.5
  • 14
    • 37049108698 scopus 로고
    • Strictosidine (Isovincoside): the key intermediate in the biosynthesis of monoterpenoid indole alkaloids
    • Stöckigt J., Zenk M.H. Strictosidine (Isovincoside): the key intermediate in the biosynthesis of monoterpenoid indole alkaloids. JCS Chem. Commun. 1977, 646-648.
    • (1977) JCS Chem. Commun. , pp. 646-648
    • Stöckigt, J.1    Zenk, M.H.2
  • 15
    • 0013012666 scopus 로고    scopus 로고
    • Strictosidine-the biosynthetic key to monoterpenoid indole alkaloids
    • Elsevier Science Ltd, Kidlington, Oxford, UK, S.D. Barton, K. Nakanishi, O. Meth-Cohn (Eds.)
    • Stöckigt J., Ruppert M. Strictosidine-the biosynthetic key to monoterpenoid indole alkaloids. Comprehensive Natural Products Chemistry, Ed 1 Vol. 4 1999, 109-138. Elsevier Science Ltd, Kidlington, Oxford, UK. S.D. Barton, K. Nakanishi, O. Meth-Cohn (Eds.).
    • (1999) Comprehensive Natural Products Chemistry, Ed 1 Vol. 4 , pp. 109-138
    • Stöckigt, J.1    Ruppert, M.2
  • 17
    • 0037657891 scopus 로고    scopus 로고
    • Camptothecin biosynthetic genes in hairy roots of Ophiorrhiza pumila: cloning, characterization and differential expression in tissues and by stress compounds
    • Yamazaki Y., Sudo H., Yamazaki M., Aimi N., Saito K. Camptothecin biosynthetic genes in hairy roots of Ophiorrhiza pumila: cloning, characterization and differential expression in tissues and by stress compounds. Plant Cell Physiol. 2003, 44:395-403.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 395-403
    • Yamazaki, Y.1    Sudo, H.2    Yamazaki, M.3    Aimi, N.4    Saito, K.5
  • 19
    • 0034490132 scopus 로고    scopus 로고
    • Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P450 CYP72A1 as secologanin synthase
    • Irmler S., Schroeder G., St-Pierre B., Crouch N.P., Hotze M., Schmidt D.S., Matern U., Schroeder J. Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P450 CYP72A1 as secologanin synthase. Plant J. 2000, 24:797-804.
    • (2000) Plant J. , vol.24 , pp. 797-804
    • Irmler, S.1    Schroeder, G.2    St-Pierre, B.3    Crouch, N.P.4    Hotze, M.5    Schmidt, D.S.6    Matern, U.7    Schroeder, J.8
  • 20
    • 0033977809 scopus 로고    scopus 로고
    • Secologanin synthase which catalyzes the oxidative cleavage of loganin into secologanin is a cytochrome P450
    • Yamamoto H., Katano N., Ooi A., Inoue K. Secologanin synthase which catalyzes the oxidative cleavage of loganin into secologanin is a cytochrome P450. Phytochemistry 2000, 53:7-12.
    • (2000) Phytochemistry , vol.53 , pp. 7-12
    • Yamamoto, H.1    Katano, N.2    Ooi, A.3    Inoue, K.4
  • 21
    • 0011376688 scopus 로고
    • National Chung-Shing University, Taichung, Taiwan.
    • Liu Y.C. Ligneous Plants of Taiwan 1972, National Chung-Shing University, Taichung, Taiwan, pp. 500.
    • (1972) Ligneous Plants of Taiwan , pp. 500
    • Liu, Y.C.1
  • 22
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 2004, 5:150-163.
    • (2004) Brief. Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 24
    • 0015356037 scopus 로고
    • Purification of biologically active globin messenger RNA by chromatography on oligo thymidylic acid cellulose
    • Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligo thymidylic acid cellulose. Proc. Natl. Acad. Sci. U.S.A. 1972, 69:1408-1412.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 1408-1412
    • Aviv, H.1    Leder, P.2
  • 26
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg A.P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 1983, 132:6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 27
    • 0028928192 scopus 로고
    • Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C-O phenol-coupling cytochrome P-450 from the higher plant Berberis stolonifera
    • Kraus P.F.X., Kutchan T.M. Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C-O phenol-coupling cytochrome P-450 from the higher plant Berberis stolonifera. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:2071-2075.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2071-2075
    • Kraus, P.F.X.1    Kutchan, T.M.2
  • 28
    • 79955697696 scopus 로고    scopus 로고
    • Functional expression of geraniol 10-hydroxylase reveals its dual function in the biosynthesis of terpenoid and phenylpropanoid
    • Sung P.H., Huang F.C., Do Y.Y., Huang P.L. Functional expression of geraniol 10-hydroxylase reveals its dual function in the biosynthesis of terpenoid and phenylpropanoid. J. Agric. Food. Chem. 2011, 59:4637-4643.
    • (2011) J. Agric. Food. Chem. , vol.59 , pp. 4637-4643
    • Sung, P.H.1    Huang, F.C.2    Do, Y.Y.3    Huang, P.L.4
  • 29
    • 0027630948 scopus 로고
    • Isolation and characterization of a cDNA clone from Catharanthus roseus encoding NADPH:cytochrome P-450 reductase, an enzyme essential for reactions catalysed by cytochrome P-450 mono-oxygenases in plants
    • Meijer A.H., Lopes Cardoso M.I., Voskuilen J.T., de Waal A., Verpoort R., Hoge J.H.C. Isolation and characterization of a cDNA clone from Catharanthus roseus encoding NADPH:cytochrome P-450 reductase, an enzyme essential for reactions catalysed by cytochrome P-450 mono-oxygenases in plants. Plant J. 1993, 4:47-60.
    • (1993) Plant J. , vol.4 , pp. 47-60
    • Meijer, A.H.1    Lopes Cardoso, M.I.2    Voskuilen, J.T.3    de Waal, A.4    Verpoort, R.5    Hoge, J.H.C.6
  • 30
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G., Steppuhn J., Herrmann R.G. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 1989, 180:535-545.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 31
    • 26444495083 scopus 로고    scopus 로고
    • Enhancement of isoflavone synthase activity by co-expression of P450 reductase from rice
    • Kim D.H., Kim B.G., Lee H.J., Lim Y., Hur H.G., Ahn J.H. Enhancement of isoflavone synthase activity by co-expression of P450 reductase from rice. Biotechnol. Lett. 2005, 27:1291-1294.
    • (2005) Biotechnol. Lett. , vol.27 , pp. 1291-1294
    • Kim, D.H.1    Kim, B.G.2    Lee, H.J.3    Lim, Y.4    Hur, H.G.5    Ahn, J.H.6
  • 32
    • 0013569329 scopus 로고
    • Coding nucleotide sequence of rat NADPH-cytochrome P450 oxidoreductase cDNA and identication of flavin-binding domains
    • Porter T.D., Kasper C.B. Coding nucleotide sequence of rat NADPH-cytochrome P450 oxidoreductase cDNA and identication of flavin-binding domains. Proc. Natl. Acad. Sci. U.S.A. 1985, 82:973-977.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 973-977
    • Porter, T.D.1    Kasper, C.B.2
  • 33
    • 0023044638 scopus 로고
    • NADPH-cytochrome P450 oxidoreductase: flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins
    • Porter T.D., Kasper C.B. NADPH-cytochrome P450 oxidoreductase: flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins. Biochemistry 1986, 25:1682-1687.
    • (1986) Biochemistry , vol.25 , pp. 1682-1687
    • Porter, T.D.1    Kasper, C.B.2
  • 34
    • 28044460323 scopus 로고    scopus 로고
    • Distribution of anticancer drug camptothecin in Nothapodytes foetida
    • Fulzele D.P., Satdive R.K. Distribution of anticancer drug camptothecin in Nothapodytes foetida. Fitoterapia 2005, 76:643-648.
    • (2005) Fitoterapia , vol.76 , pp. 643-648
    • Fulzele, D.P.1    Satdive, R.K.2
  • 36
    • 4944264246 scopus 로고    scopus 로고
    • Camptothecin, over four decades of surprising findings
    • Lorence A., Nessler C.L. Camptothecin, over four decades of surprising findings. Phytochemistry 2004, 65:2735-2749.
    • (2004) Phytochemistry , vol.65 , pp. 2735-2749
    • Lorence, A.1    Nessler, C.L.2
  • 37
    • 0032033414 scopus 로고    scopus 로고
    • Molecular cloning and functional heterologous expression of two alleles encoding (S)-N-methylcoclaurine 3(-hydroxylase (CYP80B1), a new methyl jasmonate-inducible cytochrome P-450-dependent monooxygenase of benzylisoquinoline alkaloid biosynthesis
    • Pauli H.H., Kutchan T.M. Molecular cloning and functional heterologous expression of two alleles encoding (S)-N-methylcoclaurine 3(-hydroxylase (CYP80B1), a new methyl jasmonate-inducible cytochrome P-450-dependent monooxygenase of benzylisoquinoline alkaloid biosynthesis. Plant J. 1998, 13:793-801.
    • (1998) Plant J. , vol.13 , pp. 793-801
    • Pauli, H.H.1    Kutchan, T.M.2
  • 38
    • 0142036457 scopus 로고    scopus 로고
    • Light-induced cytochrome P450-dependent enzyme in indole alkaloid biosynthesis: tabersonine 16-hydroxylase
    • Schröder G., Unterbusch E., Kaltenbach M., Schmidt J., Strack D., De Luca V., Schröder J. Light-induced cytochrome P450-dependent enzyme in indole alkaloid biosynthesis: tabersonine 16-hydroxylase. FEBS Lett. 1999, 458:97-102.
    • (1999) FEBS Lett. , vol.458 , pp. 97-102
    • Schröder, G.1    Unterbusch, E.2    Kaltenbach, M.3    Schmidt, J.4    Strack, D.5    De Luca, V.6    Schröder, J.7
  • 39
    • 15944383707 scopus 로고    scopus 로고
    • Coexpression in yeast of Taxus cytochrome P450 reductase with cytochrome P450 oxygenases involved in taxol biosynthesis
    • Jennewein S., Park H., DeJong J.M., Long R.M., Arthur P.B., Croteau R.B. Coexpression in yeast of Taxus cytochrome P450 reductase with cytochrome P450 oxygenases involved in taxol biosynthesis. Biotechnol. Bioeng. 2005, 89:588-598.
    • (2005) Biotechnol. Bioeng. , vol.89 , pp. 588-598
    • Jennewein, S.1    Park, H.2    DeJong, J.M.3    Long, R.M.4    Arthur, P.B.5    Croteau, R.B.6
  • 40
    • 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


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