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Volumn 5, Issue 2-3, 2006, Pages 271-282

Cytochrome P450s in flavonoid metabolism

Author keywords

Aliphatic hydroxylation; Aromatic hydroxylation; Flavonoid skeleton formation; Isoflavonoid; Phytoalexins

Indexed keywords

2 HYDROXYISOFLAVANONE SYNTHASE; 3' HYDROXYLASE; 3,9 DIHYDROXYPTEROCARPAN 6A HYDROXYLASE; ANTHOCYANIN; CYTOCHROME P450; CYTOCHROME P450 71D9; CYTOCHROME P450 75; CYTOCHROME P450 81E; CYTOCHROME P450 93A; CYTOCHROME P450 93B; CYTOCHROME P450 93C; ENZYME; FLAVANONE 2 HYDROXYLASE; FLAVONE DERIVATIVE; FLAVONE SYNTHASE II; FLAVONOID; FLAVONOID 3',5' HYDROXYLASE; FLAVONOID 6 HYDROXYLASE; FLAVONOL 6 HYDROXYLASE; FLAVONOL DERIVATIVE; GLYCEOL; GLYCEOLLIN; ISOFLAVONE 2' HYDROXYLASE; ISOFLAVONE 3' HYDROXYLASE; ISOFLAVONOID; OXYGENASE; PHYTOALEXIN; PTEROCARPAN DERIVATIVE; TANNIN; VEGETABLE PROTEIN;

EID: 33845431238     PISSN: 15687767     EISSN: 1572980X     Source Type: Journal    
DOI: 10.1007/s11101-006-9007-3     Document Type: Review
Times cited : (101)

References (85)
  • 1
    • 0030739662 scopus 로고    scopus 로고
    • Cloning of cytochrome P450 cDNAs from cultured Glycyrrhiza echinata L. cells and their transcriptional activation by elicitor-treatment
    • Akashi T, Aoki T, Takahashi T, Kameya N, Nakamura I, Ayabe S (1997) Cloning of cytochrome P450 cDNAs from cultured Glycyrrhiza echinata L. cells and their transcriptional activation by elicitor-treatment. Plant Sci 126:39-47
    • (1997) Plant Sci , vol.126 , pp. 39-47
    • Akashi, T.1    Aoki, T.2    Takahashi, T.3    Kameya, N.4    Nakamura, I.5    Ayabe, S.6
  • 2
    • 0032541027 scopus 로고    scopus 로고
    • Identification of a cytochrome P450 cDNA encoding (2S)-flavanone 2-hydroxylase of licorice (Glycyrrhiza echinata L.; Fabaceae) which represents licodione synthase and flavone synthase II
    • Akashi T, Aoki T, Ayabe S (1998a) Identification of a cytochrome P450 cDNA encoding (2S)-flavanone 2-hydroxylase of licorice (Glycyrrhiza echinata L.; Fabaceae) which represents licodione synthase and flavone synthase II. FEBS Lett 431:287-90
    • (1998) FEBS Lett , vol.431 , pp. 287-290
    • Akashi, T.1    Aoki, T.2    Ayabe, S.3
  • 3
    • 0032500379 scopus 로고    scopus 로고
    • CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2′-hydroxylase
    • Akashi T, Aoki T, Ayabe S (1998b) CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2′-hydroxylase. Biochem Biophys Res Commun 251:67-70
    • (1998) Biochem Biophys Res Commun , vol.251 , pp. 67-70
    • Akashi, T.1    Aoki, T.2    Ayabe, S.3
  • 4
    • 0033230703 scopus 로고    scopus 로고
    • Cloning and functional expression of a cytochrome P450 cDNA encoding 2-hydroxyisoflavanone synthase involved in biosynthesis of the isoflavonoid skeleton in licorice
    • Akashi T, Aoki T, Ayabe S (1999a) Cloning and functional expression of a cytochrome P450 cDNA encoding 2-hydroxyisoflavanone synthase involved in biosynthesis of the isoflavonoid skeleton in licorice. Plant Physiol 121:821-828
    • (1999) Plant Physiol , vol.121 , pp. 821-828
    • Akashi, T.1    Aoki, T.2    Ayabe, S.3
  • 5
    • 0033228156 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of a novel cytochrome 450, flavone synthase II, that catalyzes direct conversion of flavanones to flavones
    • Akashi T, Fukuchi-Mizutani M, Aoki T, Ueyama Y, Yonekura-Sakakibara K, Tanaka Y, Kusumi T, Ayabe S (1999b) Molecular cloning and biochemical characterization of a novel cytochrome 450, flavone synthase II, that catalyzes direct conversion of flavanones to flavones. Plant Cell Physiol 40:1182-1186
    • (1999) Plant Cell Physiol , vol.40 , pp. 1182-1186
    • Akashi, T.1    Fukuchi-Mizutani, M.2    Aoki, T.3    Ueyama, Y.4    Yonekura-Sakakibara, K.5    Tanaka, Y.6    Kusumi, T.7    Ayabe, S.8
  • 6
    • 18144363888 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of 2-hydroxyisoflavanone dehydratase. Involvement of carboxylesterase-like proteins in leguminous isoflavone biosynthesis
    • Akashi T, Aoki T, Ayabe S (2005) Molecular and biochemical characterization of 2-hydroxyisoflavanone dehydratase. Involvement of carboxylesterase-like proteins in leguminous isoflavone biosynthesis. Plant Physiol 137:882-891
    • (2005) Plant Physiol , vol.137 , pp. 882-891
    • Akashi, T.1    Aoki, T.2    Ayabe, S.3
  • 7
    • 14544274121 scopus 로고    scopus 로고
    • Molecular characterization and functional expression of flavonol 6-hydroxylase
    • Anzellotti D, Ibrahim RK (2004) Molecular characterization and functional expression of flavonol 6-hydroxylase. BMC Plant Biol 4:20
    • (2004) BMC Plant Biol , vol.4 , pp. 20
    • Anzellotti, D.1    Ibrahim, R.K.2
  • 8
    • 0037319699 scopus 로고    scopus 로고
    • The chalcone synthase superfamily of type III polyketide synthases
    • Austin MB, Noel JP (2003) The chalcone synthase superfamily of type III polyketide synthases. Nat Prod Rep 20:79-110
    • (2003) Nat Prod Rep , vol.20 , pp. 79-110
    • Austin, M.B.1    Noel, J.P.2
  • 9
    • 0036031559 scopus 로고    scopus 로고
    • Cloning of cDNAs encoding P450s in the flavonoid/isoflavonoid pathway from elicited leguminous cell cultures
    • Ayabe S, Akashi T, Aoki T (2002) Cloning of cDNAs encoding P450s in the flavonoid/isoflavonoid pathway from elicited leguminous cell cultures. Methods Enzymol 357:360-369
    • (2002) Methods Enzymol , vol.357 , pp. 360-369
    • Ayabe, S.1    Akashi, T.2    Aoki, T.3
  • 10
    • 33645834129 scopus 로고    scopus 로고
    • Identification of the flavonoid hydroxylases from grapevine and their regulation during fruit development
    • Bogs J, Ebadi A, McDavid D, Robinson SP (2006) Identification of the flavonoid hydroxylases from grapevine and their regulation during fruit development. Plant Physiol 140:279-291
    • (2006) Plant Physiol , vol.140 , pp. 279-291
    • Bogs, J.1    Ebadi, A.2    McDavid, D.3    Robinson, S.P.4
  • 12
    • 0000680699 scopus 로고
    • Conversion of flavanone to flavone, dihydroflavonol and flavonol with an enzyme system from cell cultures of parsley
    • Britsch L, Heller W, Grisebach H (1981) Conversion of flavanone to flavone, dihydroflavonol and flavonol with an enzyme system from cell cultures of parsley. Z Naturforsch 36c:742-750
    • (1981) Z Naturforsch , vol.36 C , pp. 742-750
    • Britsch, L.1    Heller, W.2    Grisebach, H.3
  • 13
    • 0033179916 scopus 로고    scopus 로고
    • Isolation and characterization of a flavonoid 3′-hydroxylase cDNA clone corresponding to the Ht1 locus of Petunia hybrida
    • Brugliera F, Barri-Rewell G, Holton TA, Mason JG (1999) Isolation and characterization of a flavonoid 3′-hydroxylase cDNA clone corresponding to the Ht1 locus of Petunia hybrida. Plant J 19:441-451
    • (1999) Plant J , vol.19 , pp. 441-451
    • Brugliera, F.1    Barri-Rewell, G.2    Holton, T.A.3    Mason, J.G.4
  • 14
    • 0031766440 scopus 로고    scopus 로고
    • Molecular-genetic analysis of plant cytochrome P450-dependent monooxygenases
    • Chapple C (1998) Molecular-genetic analysis of plant cytochrome P450-dependent monooxygenases. Annu Rev Plant Physiol Plant Mol Biol 49:311-343
    • (1998) Annu Rev Plant Physiol Plant Mol Biol , vol.49 , pp. 311-343
    • Chapple, C.1
  • 15
    • 0030020915 scopus 로고    scopus 로고
    • Cytochrome P450-dependent methylenedioxy bridge formation in Cicer arietinum
    • Clemens S, Barz W (1996) Cytochrome P450-dependent methylenedioxy bridge formation in Cicer arietinum. Phytochemistry 41:457-460
    • (1996) Phytochemistry , vol.41 , pp. 457-460
    • Clemens, S.1    Barz, W.2
  • 16
    • 17144389026 scopus 로고    scopus 로고
    • Application of Bruchin B to pea pods results in the up-regulation of CYP93C18, a putative isoflavone synthase gene, and an increase in the level of pisatin, an isoflavone phytoalexin
    • Cooper LD, Doss RP, Price R, Peterson K, Oliver JE (2005) Application of Bruchin B to pea pods results in the up-regulation of CYP93C18, a putative isoflavone synthase gene, and an increase in the level of pisatin, an isoflavone phytoalexin. J Exp Bot 56:1229-1237
    • (2005) J Exp Bot , vol.56 , pp. 1229-1237
    • Cooper, L.D.1    Doss, R.P.2    Price, R.3    Peterson, K.4    Oliver, J.E.5
  • 17
    • 33644700143 scopus 로고    scopus 로고
    • Metabolic engineering of isoflavonoid biosynthesis in alfalfa
    • Deavours BE, Dixon RA (2005) Metabolic engineering of isoflavonoid biosynthesis in alfalfa. Plant Physiol 138:2245-2259
    • (2005) Plant Physiol , vol.138 , pp. 2245-2259
    • Deavours, B.E.1    Dixon, R.A.2
  • 18
    • 3242730436 scopus 로고    scopus 로고
    • Isoflavonoid biosynthesis and accumulation in developing soybean seeds
    • Dhaubhadel S, McGarvey BD, Williams R, Gijzen M (2003) Isoflavonoid biosynthesis and accumulation in developing soybean seeds. Plant Mol Biol 53:733-743
    • (2003) Plant Mol Biol , vol.53 , pp. 733-743
    • Dhaubhadel, S.1    McGarvey, B.D.2    Williams, R.3    Gijzen, M.4
  • 20
    • 0030111330 scopus 로고    scopus 로고
    • Cloning of wound-induced cytochrome P450 monooxygenases expressed in pea
    • Frank MR, Deyneka JM, Schuler MA (1996) Cloning of wound-induced cytochrome P450 monooxygenases expressed in pea. Plant Physiol 110:1035-1046
    • (1996) Plant Physiol , vol.110 , pp. 1035-1046
    • Frank, M.R.1    Deyneka, J.M.2    Schuler, M.A.3
  • 21
    • 33645001521 scopus 로고    scopus 로고
    • The diphenylether herbicide lactofen induces cell death and expression of defense-related genes in soybean
    • Graham MY (2005) The diphenylether herbicide lactofen induces cell death and expression of defense-related genes in soybean. Plant Physiol 139:1784-1794
    • (2005) Plant Physiol , vol.139 , pp. 1784-1794
    • Graham, M.Y.1
  • 22
    • 84944003615 scopus 로고
    • Elicitor induction of cytochrome P-450 monooxygenases in cell suspension cultures of chickpea (Cicer arietinum L.) and their involvement in pterocarpan phytoalexin biosynthesis
    • Gunia W, Hinderer W, Wittkampf U, Barz W (1991) Elicitor induction of cytochrome P-450 monooxygenases in cell suspension cultures of chickpea (Cicer arietinum L.) and their involvement in pterocarpan phytoalexin biosynthesis. Z Naturforsch 46c:58-66
    • (1991) Z Naturforsch , vol.46 C , pp. 58-66
    • Gunia, W.1    Hinderer, W.2    Wittkampf, U.3    Barz, W.4
  • 23
    • 0001034897 scopus 로고
    • Enzymatic rearrangement of flavanone to isoflavone
    • Hagmann M, Grisebach H (1984) Enzymatic rearrangement of flavanone to isoflavone. FEBS Lett 175:199-202
    • (1984) FEBS Lett , vol.175 , pp. 199-202
    • Hagmann, M.1    Grisebach, H.2
  • 24
    • 0025884986 scopus 로고
    • P-450-Dependent oxidative rearrangement in isoflavone biosynthesis: Reconstitution of P-450 and NADPH: P-450 reductase
    • Hakamatsuka T, Hashim MF, Ebizuka Y, Sankawa U (1991) P-450-Dependent oxidative rearrangement in isoflavone biosynthesis: reconstitution of P-450 and NADPH: P-450 reductase. Tetrahedron 47:5969-5978
    • (1991) Tetrahedron , vol.47 , pp. 5969-5978
    • Hakamatsuka, T.1    Hashim, M.F.2    Ebizuka, Y.3    Sankawa, U.4
  • 25
    • 0032575879 scopus 로고    scopus 로고
    • Purification of 2-hydroxyisoflavanone dehydratase from the cell cultures of Pueraria lobata
    • Hakamatsuka T, Mori K, Ishida S, Ebizuka Y, Sankawa U (1998) Purification of 2-hydroxyisoflavanone dehydratase from the cell cultures of Pueraria lobata. Phytochemistry 49:497-505
    • (1998) Phytochemistry , vol.49 , pp. 497-505
    • Hakamatsuka, T.1    Mori, K.2    Ishida, S.3    Ebizuka, Y.4    Sankawa, U.5
  • 26
    • 2442548759 scopus 로고    scopus 로고
    • The A-ring specific hydroxylation of flavonols in position 6 in Tagetes sp. is catalyzed by a cytochrome P450 dependent monooxygenase
    • Halbwirth H, Forkmann G, Stich K (2004) The A-ring specific hydroxylation of flavonols in position 6 in Tagetes sp. is catalyzed by a cytochrome P450 dependent monooxygenase. Plant Sci 167:129-135
    • (2004) Plant Sci , vol.167 , pp. 129-135
    • Halbwirth, H.1    Forkmann, G.2    Stich, K.3
  • 27
    • 0025163193 scopus 로고
    • Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis
    • Hashim MF, Hakamatsuka T, Ebizuka Y, Sankawa U (1990) Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis. FEBS Lett 271:219-222
    • (1990) FEBS Lett , vol.271 , pp. 219-222
    • Hashim, M.F.1    Hakamatsuka, T.2    Ebizuka, Y.3    Sankawa, U.4
  • 28
    • 0035852752 scopus 로고    scopus 로고
    • The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes three steps of the gibberellin biosynthesis pathway
    • Helliwell CA, Chandler PM, Poole A, Dennis ES, Peacock WJ (2001) The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes three steps of the gibberellin biosynthesis pathway. Proc Natl Acad Sci USA 98:2065-2070
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2065-2070
    • Helliwell, C.A.1    Chandler, P.M.2    Poole, A.3    Dennis, E.S.4    Peacock, W.J.5
  • 29
    • 0001032494 scopus 로고
    • Microsomal isoflavone 2′- and 3′-hydroxylases from chickpea (Cicer arietinum L.) cell suspensions induced for pterocarpan phytoalexin formation
    • Hinderer W, Flentje U, Barz W (1987) Microsomal isoflavone 2′- and 3′-hydroxylases from chickpea (Cicer arietinum L.) cell suspensions induced for pterocarpan phytoalexin formation. FEBS Lett 214:101-106
    • (1987) FEBS Lett , vol.214 , pp. 101-106
    • Hinderer, W.1    Flentje, U.2    Barz, W.3
  • 31
    • 0141755310 scopus 로고    scopus 로고
    • Molecular cloning and characterization of CYP719, a methylenedioxy bridge-forming enzyme that belongs to a novel P450 family, from cultured Coptis japonica cells
    • Ikezawa N, Tanaka M, Nagayoshi M, Shinkyo R, Sakaki T, Inouye K, Sato F (2003) Molecular cloning and characterization of CYP719, a methylenedioxy bridge-forming enzyme that belongs to a novel P450 family, from cultured Coptis japonica cells. J Biol Chem 278:38557-38565
    • (2003) J Biol Chem , vol.278 , pp. 38557-38565
    • Ikezawa, N.1    Tanaka, M.2    Nagayoshi, M.3    Shinkyo, R.4    Sakaki, T.5    Inouye, K.6    Sato, F.7
  • 32
    • 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, Schröder G, St-Pierre B, Crouch NP, Hotze M, Schmidt J, Strack D, Matern U, Schröder J (2000) Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P450 CYP72A1 as secologanin synthase. Plant J 24:797-804
    • (2000) Plant J , vol.24 , pp. 797-804
    • Irmler, S.1    Schröder, G.2    St-Pierre, B.3    Crouch, N.P.4    Hotze, M.5    Schmidt, J.6    Strack, D.7    Matern, U.8    Schröder, J.9
  • 34
    • 0033951110 scopus 로고    scopus 로고
    • Identification and expression of isoflavone synthase, the key enzyme for biosynthesis of isoflavones in legumes
    • Jung W, Yu O, Lau SM, O'Keefe DP, Odell J, Fader G, McGonigle B (2000) Identification and expression of isoflavone synthase, the key enzyme for biosynthesis of isoflavones in legumes. Nature Biotechnol 18:208-212
    • (2000) Nature Biotechnol , vol.18 , pp. 208-212
    • Jung, W.1    Yu, O.2    Lau, S.M.3    O'Keefe, D.P.4    Odell, J.5    Fader, G.6    McGonigle, B.7
  • 35
  • 36
    • 9144235668 scopus 로고    scopus 로고
    • Oxidation and rearrangements of flavanones by mammalian cytochrome P450
    • Kagawa H, Takahashi T, Ohta S, Harigaya Y (2004) Oxidation and rearrangements of flavanones by mammalian cytochrome P450. Xenobiotica 34:797-810
    • (2004) Xenobiotica , vol.34 , pp. 797-810
    • Kagawa, H.1    Takahashi, T.2    Ohta, S.3    Harigaya, Y.4
  • 37
    • 0033167145 scopus 로고    scopus 로고
    • Flavonoid hydroxylase from Catharanthus roseus: CDNA, heterologous expression, enzyme properties and cell-type specific expression in plants
    • Kaltenbach M, Schröder G, Schmelzer E, Lutz V, Schröder J (1999) Flavonoid hydroxylase from Catharanthus roseus: cDNA, heterologous expression, enzyme properties and cell-type specific expression in plants. Plant J 19:183-193
    • (1999) Plant J , vol.19 , pp. 183-193
    • Kaltenbach, M.1    Schröder, G.2    Schmelzer, E.3    Lutz, V.4    Schröder, J.5
  • 38
    • 2142799601 scopus 로고    scopus 로고
    • Cloning and expression of the isoflavone synthase gene (IFS-Tp) from Trifolium pratense
    • Kim BG, Kim SY, Song HS, Lee C, Hur HG, Kim SI, Ahn JH (2003) Cloning and expression of the isoflavone synthase gene (IFS-Tp) from Trifolium pratense. Mol Cells 15:301-306
    • (2003) Mol Cells , vol.15 , pp. 301-306
    • Kim, B.G.1    Kim, S.Y.2    Song, H.S.3    Lee, C.4    Hur, H.G.5    Kim, S.I.6    Ahn, J.H.7
  • 39
    • 0035544119 scopus 로고    scopus 로고
    • Differential expression of two cytochrome P450s involved in the biosynthesis of flavones and anthocyanins in chemo-varietal forms of Perilla frutescens
    • Kitada C, Gong Z, Tanaka Y, Yamazaki M, Saito K (2001) Differential expression of two cytochrome P450s involved in the biosynthesis of flavones and anthocyanins in chemo-varietal forms of Perilla frutescens. Plant Cell Physiol 42:1338-1344
    • (2001) Plant Cell Physiol , vol.42 , pp. 1338-1344
    • Kitada, C.1    Gong, Z.2    Tanaka, Y.3    Yamazaki, M.4    Saito, K.5
  • 40
    • 0023040739 scopus 로고
    • Enzymic synthesis of isoflavones
    • Kochs G, Grisebach H (1986) Enzymic synthesis of isoflavones. Eur J Biochem 155:311-318
    • (1986) Eur J Biochem , vol.155 , pp. 311-318
    • Kochs, G.1    Grisebach, H.2
  • 41
    • 84944438028 scopus 로고
    • Induction and characterization of a NADPH-dependent flavone synthase from cell cultures of soybean
    • Kochs G, Grisebach H (1987) Induction and characterization of a NADPH-dependent flavone synthase from cell cultures of soybean. Z Naturforsch 42c:343-348
    • (1987) Z Naturforsch , vol.42 C , pp. 343-348
    • Kochs, G.1    Grisebach, H.2
  • 42
    • 0024728582 scopus 로고
    • Phytoalexin synthesis in soybean: Purification and reconstitution of cytochrome P450 3,9-dihydroxypterocarpan 6a-hydroxylase and separation from cytochrome P450 cinnamate 4-hydroxylase
    • Kochs G, Grisebach H (1989) Phytoalexin synthesis in soybean: purification and reconstitution of cytochrome P450 3,9-dihydroxypterocarpan 6a-hydroxylase and separation from cytochrome P450 cinnamate 4-hydroxylase. Arch Biochem Biophys 273:543-553
    • (1989) Arch Biochem Biophys , vol.273 , pp. 543-553
    • Kochs, G.1    Grisebach, H.2
  • 43
    • 0026517769 scopus 로고
    • Further characterization of cytochrome P450 involved in phytoalexin synthesis in soybean: Cytochrome P450 cinnamate 4-hydroxylase and 3,9-dihydroxypterocarpan 6a-hydroxylase
    • Kochs G, Werck-Reichhart D, Grisebach H (1992) Further characterization of cytochrome P450 involved in phytoalexin synthesis in soybean: cytochrome P450 cinnamate 4-hydroxylase and 3,9-dihydroxypterocarpan 6a-hydroxylase. Arch Biochem Biophys 293:187-194
    • (1992) Arch Biochem Biophys , vol.293 , pp. 187-194
    • Kochs, G.1    Werck-Reichhart, D.2    Grisebach, H.3
  • 45
    • 1542267812 scopus 로고    scopus 로고
    • Structural and functional divergence of insect CYP6B proteins: From specialist to generalist cytochrome P450
    • Li X, Baudry J, Berenbaum MR, Schuler MA (2004) Structural and functional divergence of insect CYP6B proteins: From specialist to generalist cytochrome P450. Proc Natl Acad Sci USA 101:2939-2944
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2939-2944
    • Li, X.1    Baudry, J.2    Berenbaum, M.R.3    Schuler, M.A.4
  • 46
    • 0037195078 scopus 로고    scopus 로고
    • Bottlenecks for metabolic engineering of isoflavone glycoconjugates in Arabidopsis
    • Liu CJ, Blount JW, Steele CL, Dixon RA (2002) Bottlenecks for metabolic engineering of isoflavone glycoconjugates in Arabidopsis. Proc Natl Acad Sci USA 99:14578-14583
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14578-14583
    • Liu, C.J.1    Blount, J.W.2    Steele, C.L.3    Dixon, R.A.4
  • 47
    • 0344961689 scopus 로고    scopus 로고
    • Regiospecific hydroxylation of isoflavones by cytochrome P450 81E enzymes from Medicago truncatula
    • Liu CJ, Huhman D, Sumner LW, Dixon RA (2003) Regiospecific hydroxylation of isoflavones by cytochrome P450 81E enzymes from Medicago truncatula. Plant J 36:471-484
    • (2003) Plant J , vol.36 , pp. 471-484
    • Liu, C.J.1    Huhman, D.2    Sumner, L.W.3    Dixon, R.A.4
  • 48
    • 0033179201 scopus 로고    scopus 로고
    • Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha) species: cDNA isolation, characterization, and functional expression of (-)-4S-limonene-3-hydroxylase and (-)-4S-limonene-6-hydroxylase
    • Lupien S, Karp F, Wildung M, Croteau R (1999) Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha) species: cDNA isolation, characterization, and functional expression of (-)-4S-limonene-3-hydroxylase and (-)-4S-limonene-6-hydroxylase. Arch Biochem Biophys 368:181-192
    • (1999) Arch Biochem Biophys , vol.368 , pp. 181-192
    • Lupien, S.1    Karp, F.2    Wildung, M.3    Croteau, R.4
  • 49
    • 0028206101 scopus 로고
    • A gene from the fungal plant pathogen Nectria haematococca that encodes the phytoalexin-detoxifying enzyme pisatin demethylase defines a new cytochrome P450 family
    • Maloney AP, VanEtten HD (1994) A gene from the fungal plant pathogen Nectria haematococca that encodes the phytoalexin-detoxifying enzyme pisatin demethylase defines a new cytochrome P450 family. Mol Gen Genet 243:506-514
    • (1994) Mol Gen Genet , vol.243 , pp. 506-514
    • Maloney, A.P.1    VanEtten, H.D.2
  • 50
    • 0033375553 scopus 로고    scopus 로고
    • Cloning and expression of flavone synthase II from Gerbera hybrids
    • Martens S, Forkmann G (1999) Cloning and expression of flavone synthase II from Gerbera hybrids. Plant J 20:611-618
    • (1999) Plant J , vol.20 , pp. 611-618
    • Martens, S.1    Forkmann, G.2
  • 51
    • 26444611245 scopus 로고    scopus 로고
    • Flavones and flavone synthases
    • Martens S, Mithöfer A (2005) Flavones and flavone synthases. Phytochemistry 66:2399-2407
    • (2005) Phytochemistry , vol.66 , pp. 2399-2407
    • Martens, S.1    Mithöfer, A.2
  • 52
    • 2442535725 scopus 로고
    • Role of oxygenases in pisatin biosynthesis and in the fungal degradation of maackiain
    • Matthews DE, Weiner EJ, Matthews PS, VanEtten HD (1987) Role of oxygenases in pisatin biosynthesis and in the fungal degradation of maackiain. Plant Physiol 83:365-370
    • (1987) Plant Physiol , vol.83 , pp. 365-370
    • Matthews, D.E.1    Weiner, E.J.2    Matthews, P.S.3    VanEtten, H.D.4
  • 53
    • 38249026250 scopus 로고
    • The 6a oxygen of the pterocarpan glycinol is derived from molecular oxygen
    • Matthews DE, Plattner RD, VanEtten HD (1989) The 6a oxygen of the pterocarpan glycinol is derived from molecular oxygen. Phytochemistry 28:113-115
    • (1989) Phytochemistry , vol.28 , pp. 113-115
    • Matthews, D.E.1    Plattner, R.D.2    VanEtten, H.D.3
  • 55
    • 17044391118 scopus 로고    scopus 로고
    • Integrating genomics and metabolomics for engineering plant metabolic pathways
    • Oksman-Caldentey KM, Saito K (2005) Integrating genomics and metabolomics for engineering plant metabolic pathways. Curr Opin Biotechnol 16:174-179
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 174-179
    • Oksman-Caldentey, K.M.1    Saito, K.2
  • 56
    • 0028056992 scopus 로고
    • Licodione synthase, a cytochrome P450 monooxygenase catalyzing 2-hydroxylation of 5-deoxyflavanone, in cultured Glycyrrhiza echinata L. cells
    • Otani K, Takahashi T, Furuya T, Ayabe S (1994) Licodione synthase, a cytochrome P450 monooxygenase catalyzing 2-hydroxylation of 5-deoxyflavanone, in cultured Glycyrrhiza echinata L. cells. Plant Physiol 105:1427-1432
    • (1994) Plant Physiol , vol.105 , pp. 1427-1432
    • Otani, K.1    Takahashi, T.2    Furuya, T.3    Ayabe, S.4
  • 57
    • 0034641071 scopus 로고    scopus 로고
    • Cloning and characterization of eight cytochrome P450 cDNAs from chickpea (Cicer arietinum L.) cell suspension cultures
    • Overkamp S, Hein F, Barz W (2000) Cloning and characterization of eight cytochrome P450 cDNAs from chickpea (Cicer arietinum L.) cell suspension cultures. Plant Sci 155:101-108
    • (2000) Plant Sci , vol.155 , pp. 101-108
    • Overkamp, S.1    Hein, F.2    Barz, W.3
  • 58
    • 0035883986 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum)
    • Ralston L, Kwon ST, Schoenbeck M, Ralston J, Schenk DJ, Coates RM, Chappell J (2001) Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum). Arch Biochem Biophys 393:222-235
    • (2001) Arch Biochem Biophys , vol.393 , pp. 222-235
    • Ralston, L.1    Kwon, S.T.2    Schoenbeck, M.3    Ralston, J.4    Schenk, D.J.5    Coates, R.M.6    Chappell, J.7
  • 59
    • 2042528492 scopus 로고    scopus 로고
    • Microbial transformations of chalcones: Hydroxylation, O-demethylation, and cyclization to flavanones
    • Sanchez-Gonzalez M, Rosazza JP (2004) Microbial transformations of chalcones: hydroxylation, O-demethylation, and cyclization to flavanones. J Nat Prod 67:553-558
    • (2004) J Nat Prod , vol.67 , pp. 553-558
    • Sanchez-Gonzalez, M.1    Rosazza, J.P.2
  • 60
    • 0036735095 scopus 로고    scopus 로고
    • Key amino acid residues required for aryl migration catalyzed by the cytochrome P450 2-hydroxyisoflavanone synthase
    • Sawada Y, Kinoshita K, Akashi T, Aoki T, Ayabe S (2002) Key amino acid residues required for aryl migration catalyzed by the cytochrome P450 2-hydroxyisoflavanone synthase. Plant J 31:555-564
    • (2002) Plant J , vol.31 , pp. 555-564
    • Sawada, Y.1    Kinoshita, K.2    Akashi, T.3    Aoki, T.4    Ayabe, S.5
  • 61
    • 16244404948 scopus 로고    scopus 로고
    • Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue
    • Sawada Y, Ayabe S (2005) Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue. Biochem Biophys Res Commun 330:907-913
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 907-913
    • Sawada, Y.1    Ayabe, S.2
  • 62
    • 0033832157 scopus 로고    scopus 로고
    • Identification of the Arabidopsis thaliana flavonoid 3′-hydroxylase gene and functional expression of the encoded P450 enzyme
    • Schoenbohm C, Martens S, Eder C, Forkmann G, Weisshaar B (2000) Identification of the Arabidopsis thaliana flavonoid 3′-hydroxylase gene and functional expression of the encoded P450 enzyme. Biol Chem 381:749-753
    • (2000) Biol Chem , vol.381 , pp. 749-753
    • Schoenbohm, C.1    Martens, S.2    Eder, C.3    Forkmann, G.4    Weisshaar, B.5
  • 63
    • 0031841398 scopus 로고    scopus 로고
    • Identification of elicitor-induced cytochrome P450s of soybean (Glycine max L.) using differential display of mRNA
    • Schopfer CR, Ebel J (1998) Identification of elicitor-induced cytochrome P450s of soybean (Glycine max L.) using differential display of mRNA. Mol Gen Genet 258:315-322
    • (1998) Mol Gen Genet , vol.258 , pp. 315-322
    • Schopfer, C.R.1    Ebel, J.2
  • 64
    • 0031660180 scopus 로고    scopus 로고
    • Molecular characterization and functional expression of dihydroxypterocarpan 6a-hydroxylase, an enzyme specific for pterocarpanoid phytoalexin biosynthesis in soybean (Glycine max L.)
    • Schopfer CR, Kochs G, Lottspeich F, Ebel J (1998) Molecular characterization and functional expression of dihydroxypterocarpan 6a-hydroxylase, an enzyme specific for pterocarpanoid phytoalexin biosynthesis in soybean (Glycine max L.). FEBS Lett 432:182-186
    • (1998) FEBS Lett , vol.432 , pp. 182-186
    • Schopfer, C.R.1    Kochs, G.2    Lottspeich, F.3    Ebel, J.4
  • 66
    • 0034619747 scopus 로고    scopus 로고
    • Induction of isoflavonoid pathway in the model legume Lotus japonicus: Molecular characterization of enzymes involved in phytoalexin biosynthesis
    • Shimada N, Akashi T, Aoki T, Ayabe S (2000) Induction of isoflavonoid pathway in the model legume Lotus japonicus: molecular characterization of enzymes involved in phytoalexin biosynthesis. Plant Sci 160:37-47
    • (2000) Plant Sci , vol.160 , pp. 37-47
    • Shimada, N.1    Akashi, T.2    Aoki, T.3    Ayabe, S.4
  • 67
    • 0037355037 scopus 로고    scopus 로고
    • A cluster of genes encodes the two types of chalcone isomerase involved in the biosynthesis of general flavonoids and legume-specific 5-deoxy(iso)flavonoids in Lotus japonicus
    • Shimada N, Aoki T, Sato S, Nakamura Y, Tabata S, Ayabe S. (2003) A cluster of genes encodes the two types of chalcone isomerase involved in the biosynthesis of general flavonoids and legume-specific 5-deoxy(iso)flavonoids in Lotus japonicus. Plant Physiol 131:941-951
    • (2003) Plant Physiol , vol.131 , pp. 941-951
    • Shimada, N.1    Aoki, T.2    Sato, S.3    Nakamura, Y.4    Tabata, S.5    Ayabe, S.6
  • 68
    • 0033574012 scopus 로고    scopus 로고
    • Expression of a soybean cytochrome P450 monooxygenase cDNA in yeast and tobacco enhances the metabolism of phenylurea herbicides
    • Siminszky B, Corbin FT, Ward ER, Fleischmann TJ, Dewey RE (1999) Expression of a soybean cytochrome P450 monooxygenase cDNA in yeast and tobacco enhances the metabolism of phenylurea herbicides. Proc Natl Acad Sci USA 96:1750-1755
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1750-1755
    • Siminszky, B.1    Corbin, F.T.2    Ward, E.R.3    Fleischmann, T.J.4    Dewey, R.E.5
  • 69
    • 0033167088 scopus 로고    scopus 로고
    • Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean
    • Steele CL, Gijzen M, Qutob D, Dixon RA (1999) Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean. Arch Biochem Biophys 367:146-150
    • (1999) Arch Biochem Biophys , vol.367 , pp. 146-150
    • Steele, C.L.1    Gijzen, M.2    Qutob, D.3    Dixon, R.A.4
  • 70
    • 0000333932 scopus 로고
    • Oxidation of flavanones to flavones with flower extracts of Antirrhinum majus (snapdragon)
    • Stotz G, Forkmann G (1981) Oxidation of flavanones to flavones with flower extracts of Antirrhinum majus (snapdragon). Z Naturforsch 36c:737-741
    • (1981) Z Naturforsch , vol.36 C , pp. 737-741
    • Stotz, G.1    Forkmann, G.2
  • 72
    • 4544372259 scopus 로고    scopus 로고
    • The promoters of two isoflavone synthase genes respond differentially to nodulation and defense signals in transgenic soybean roots
    • Subramanian S, Hu X, Lu G, Odelland JT, Yu O (2004) The promoters of two isoflavone synthase genes respond differentially to nodulation and defense signals in transgenic soybean roots. Plant Mol Biol 54:623-639
    • (2004) Plant Mol Biol , vol.54 , pp. 623-639
    • Subramanian, S.1    Hu, X.2    Lu, G.3    Odelland, J.T.4    Yu, O.5
  • 73
    • 20444432384 scopus 로고    scopus 로고
    • RNA interference of soybean isoflavone synthase genes leads to silencing in tissues distal to the transformation site and to enhanced susceptibility to Phytophthora sojae
    • Subramanian S, Graham MY, Yu O, Graham TL (2005) RNA interference of soybean isoflavone synthase genes leads to silencing in tissues distal to the transformation site and to enhanced susceptibility to Phytophthora sojae. Plant Physiol 137:1345-1353
    • (2005) Plant Physiol , vol.137 , pp. 1345-1353
    • Subramanian, S.1    Graham, M.Y.2    Yu, O.3    Graham, T.L.4
  • 75
    • 33845390649 scopus 로고    scopus 로고
    • Flower colour and cytochromes P450
    • in press
    • Tanaka Y (2006) Flower colour and cytochromes P450. Phytochemistry Reviews: in press
    • (2006) Phytochemistry Reviews
    • Tanaka, Y.1
  • 77
    • 0036715644 scopus 로고    scopus 로고
    • A single-base deletion in soybean flavonoid 3′-hydroxylase gene is associated with gray pubescence color
    • Toda K, Yang D, Yamanaka N, Watanabe S, Harada K, Takahashi R (2002) A single-base deletion in soybean flavonoid 3′-hydroxylase gene is associated with gray pubescence color. Plant Mol Biol 50:187-196
    • (2002) Plant Mol Biol , vol.50 , pp. 187-196
    • Toda, K.1    Yang, D.2    Yamanaka, N.3    Watanabe, S.4    Harada, K.5    Takahashi, R.6
  • 78
    • 0036677785 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of torenia flavonoid 3′-hydroxylase and flavone synthase II and modification of flower color by modulating the expression of these genes
    • Ueyama Y, Suzuki K, Fukuchi-Mizutani M, Fukui Y, Miyazaki K, Ohkawa H, Kusumi T, Tanaka Y (2002) Molecular and biochemical characterization of torenia flavonoid 3′-hydroxylase and flavone synthase II and modification of flower color by modulating the expression of these genes. Plant Sci 163:253-263
    • (2002) Plant Sci , vol.163 , pp. 253-263
    • Ueyama, Y.1    Suzuki, K.2    Fukuchi-Mizutani, M.3    Fukui, Y.4    Miyazaki, K.5    Ohkawa, H.6    Kusumi, T.7    Tanaka, Y.8
  • 79
    • 0024287676 scopus 로고
    • Induction of phytoalexin synthesis in soybean: Enzymatic cyclization of prenylated pterocarpans to glyceollin isomers
    • Welle R, Grisebach H (1988) Induction of phytoalexin synthesis in soybean: enzymatic cyclization of prenylated pterocarpans to glyceollin isomers. Arch Biochem Biophys 263:191-198
    • (1988) Arch Biochem Biophys , vol.263 , pp. 191-198
    • Welle, R.1    Grisebach, H.2
  • 80
    • 0031896512 scopus 로고    scopus 로고
    • Enzymatic hydroxylation of 6′-deoxychalcones with protein preparations from petals of Dahlia variabilis
    • Wimmer G, Halbwirth H, Wurst F, Forkmann G, Stich K (1998) Enzymatic hydroxylation of 6′-deoxychalcones with protein preparations from petals of Dahlia variabilis. Phytochemistry 47:1013-1016
    • (1998) Phytochemistry , vol.47 , pp. 1013-1016
    • Wimmer, G.1    Halbwirth, H.2    Wurst, F.3    Forkmann, G.4    Stich, K.5
  • 81
    • 3242655621 scopus 로고    scopus 로고
    • Metabolic channeling in plants
    • Winkel BSJ (2004) Metabolic channeling in plants. Annu Rev Plant Biol 55:85-107
    • (2004) Annu Rev Plant Biol , vol.55 , pp. 85-107
    • Winkel, B.S.J.1
  • 82
    • 0035900357 scopus 로고    scopus 로고
    • 8-Dimethylallylnaringenin 2′-hydroxylase, the crucial cytochrome P450 mono-oxygenase for lavandulylated flavanone formation in Sophora flavescens cultured cells
    • Yamamoto H, Yatou A, Inoue K (2001) 8-Dimethylallylnaringenin 2′-hydroxylase, the crucial cytochrome P450 mono-oxygenase for lavandulylated flavanone formation in Sophora flavescens cultured cells. Phytochemistry 58:671-676
    • (2001) Phytochemistry , vol.58 , pp. 671-676
    • Yamamoto, H.1    Yatou, A.2    Inoue, K.3
  • 83
    • 0033791950 scopus 로고    scopus 로고
    • Production of the isoflavones genistein and daidzein in non-legume dicot and monocot tissues
    • Yu O, Jung W, Shi J, Croes RA, Fader GM, McGonigle B, Odell JT (2000) Production of the isoflavones genistein and daidzein in non-legume dicot and monocot tissues. Plant Physiol 124:781-793
    • (2000) Plant Physiol , vol.124 , pp. 781-793
    • Yu, O.1    Jung, W.2    Shi, J.3    Croes, R.A.4    Fader, G.M.5    McGonigle, B.6    Odell, J.T.7
  • 84
    • 31044438226 scopus 로고    scopus 로고
    • Metabolic engineering of isoflavone biosynthesis
    • Yu O, McGonigle B (2005) Metabolic engineering of isoflavone biosynthesis. Adv Agron 86:147-190
    • (2005) Adv Agron , vol.86 , pp. 147-190
    • Yu, O.1    McGonigle, B.2
  • 85
    • 0344961262 scopus 로고    scopus 로고
    • Characterization of leachianone G 2′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures
    • Zhao P, Inoue K, Kouno I, Yamamoto H (2003) Characterization of leachianone G 2′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol 133:1306-1313
    • (2003) Plant Physiol , vol.133 , pp. 1306-1313
    • Zhao, P.1    Inoue, K.2    Kouno, I.3    Yamamoto, H.4


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