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Volumn 70, Issue 15-16, 2009, Pages 1696-1707

Evolution of morphine biosynthesis in opium poppy

Author keywords

Benzylisoquinoline alkaloids; Metabolite profiling; Morphine; Papaver somniferum; Papaveraceae; Short chain dehydrogenase reductase; Transcript profiling

Indexed keywords

ALKALOID; BENZYLISOQUINOLINE DERIVATIVE; MORPHINE; RETICULINE;

EID: 70350710764     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2009.07.006     Document Type: Review
Times cited : (76)

References (70)
  • 2
    • 36849084099 scopus 로고    scopus 로고
    • Metabolic engineering of morphinan alkaloids by over-expression and RNAi suppression of salutaridinol 7-O-acetyltransferase in opium poppy
    • Allen R.S., Miller J.A.C., Chitty J.A., Fist A.J., Gerlach W.L., and Larkin P.J. Metabolic engineering of morphinan alkaloids by over-expression and RNAi suppression of salutaridinol 7-O-acetyltransferase in opium poppy. Plant Biotechnol. J. 6 (2008) 22-30
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 22-30
    • Allen, R.S.1    Miller, J.A.C.2    Chitty, J.A.3    Fist, A.J.4    Gerlach, W.L.5    Larkin, P.J.6
  • 3
    • 0037319699 scopus 로고    scopus 로고
    • The chalcone synthase superfamily of type III polyketide synthases
    • Austin M.B., and Noel J.P. The chalcone synthase superfamily of type III polyketide synthases. Nat. Prod. Rep. 20 (2003) 79-110
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 79-110
    • Austin, M.B.1    Noel, J.P.2
  • 4
    • 42549123527 scopus 로고    scopus 로고
    • The functional divergence of short chain dehydrogenases involved in tropinone reduction
    • Brock A., Brandt W., and Dräger B. The functional divergence of short chain dehydrogenases involved in tropinone reduction. Plant J. 54 (2008) 388-401
    • (2008) Plant J. , vol.54 , pp. 388-401
    • Brock, A.1    Brandt, W.2    Dräger, B.3
  • 5
    • 0037016691 scopus 로고    scopus 로고
    • Molecular cloning and characterization of coclaurine N-methyltransferase from cultured cells of Coptis japonica
    • Choi K.B., Morishige T., Shitan N., Yazaki K., and Sato F. Molecular cloning and characterization of coclaurine N-methyltransferase from cultured cells of Coptis japonica. J. Biol. Chem. 277 (2002) 830-835
    • (2002) J. Biol. Chem. , vol.277 , pp. 830-835
    • Choi, K.B.1    Morishige, T.2    Shitan, N.3    Yazaki, K.4    Sato, F.5
  • 6
    • 55549145475 scopus 로고    scopus 로고
    • A role for a menthone reductase in resistance against microbial pathogens in plants
    • Choi H.W., Lee B.G., Kim N.H., Park Y., Lim C.W., Song H.K., and Hwang B.K. A role for a menthone reductase in resistance against microbial pathogens in plants. Plant Physiol. 148 (2008) 383-401
    • (2008) Plant Physiol. , vol.148 , pp. 383-401
    • Choi, H.W.1    Lee, B.G.2    Kim, N.H.3    Park, Y.4    Lim, C.W.5    Song, H.K.6    Hwang, B.K.7
  • 7
    • 20444446002 scopus 로고    scopus 로고
    • Monoterpene metabolism cloning, expression, and characterization of menthone reductases from peppermint
    • Davis E.M., Ringer K.L., McConkey M.E., and Croteau R. Monoterpene metabolism cloning, expression, and characterization of menthone reductases from peppermint. Plant Physiol. 137 (2005) 873-881
    • (2005) Plant Physiol. , vol.137 , pp. 873-881
    • Davis, E.M.1    Ringer, K.L.2    McConkey, M.E.3    Croteau, R.4
  • 8
    • 20344383308 scopus 로고
    • Purification and properties of 1,2-dehydroretuculine reductase from Papaver somniferum seedlings
    • De-Eknamkul W., and Zenk M.H. Purification and properties of 1,2-dehydroretuculine reductase from Papaver somniferum seedlings. Phytochemistry 31 (1992) 813-821
    • (1992) Phytochemistry , vol.31 , pp. 813-821
    • De-Eknamkul, W.1    Zenk, M.H.2
  • 9
    • 0025751609 scopus 로고
    • Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack
    • Dittrich H., and Kutchan T.M. Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Proc. Natl. Acad. Sci. USA 88 (1991) 9969-9973
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9969-9973
    • Dittrich, H.1    Kutchan, T.M.2
  • 10
    • 0033976087 scopus 로고    scopus 로고
    • Molecular evolution of the chalcone synthase multigene family in the morning glory genome
    • Durbin M.L., McCaig B., and Clegg M.T. Molecular evolution of the chalcone synthase multigene family in the morning glory genome. Plant Mol. Biol. 42 (2000) 79-92
    • (2000) Plant Mol. Biol. , vol.42 , pp. 79-92
    • Durbin, M.L.1    McCaig, B.2    Clegg, M.T.3
  • 12
    • 42249094600 scopus 로고    scopus 로고
    • Thebaine synthase: a new enzyme in the morphine pathway in Papaver somniferum
    • Fisinger U., Grobe N., and Zenk M. Thebaine synthase: a new enzyme in the morphine pathway in Papaver somniferum. Nat. Prod. Commun. 2 (2006) 249-253
    • (2006) Nat. Prod. Commun. , vol.2 , pp. 249-253
    • Fisinger, U.1    Grobe, N.2    Zenk, M.3
  • 13
    • 34247403338 scopus 로고    scopus 로고
    • Knockdown of berberine bridge enzyme by RNAi accumulates (S)-reticuline and activates a silent pathway in cultured California poppy cells
    • Fujii N., Inui T., Iwasa K., Morishige T., and Sato F. Knockdown of berberine bridge enzyme by RNAi accumulates (S)-reticuline and activates a silent pathway in cultured California poppy cells. Transgenic Res. 16 (2007) 363-375
    • (2007) Transgenic Res. , vol.16 , pp. 363-375
    • Fujii, N.1    Inui, T.2    Iwasa, K.3    Morishige, T.4    Sato, F.5
  • 14
    • 0036009782 scopus 로고    scopus 로고
    • Characterization of phenylpropene O-methyltransferases from sweet basil: facile change of substrate specificity and convergent evolution within a plant O-methyltransferase family
    • Gang D.R., Lavid N., Zubieta C., Chen F., Beuerle T., Lewinsohn E., Noel J.P., and Pichersky E. Characterization of phenylpropene O-methyltransferases from sweet basil: facile change of substrate specificity and convergent evolution within a plant O-methyltransferase family. Plant Cell 14 (2002) 505-519
    • (2002) Plant Cell , vol.14 , pp. 505-519
    • Gang, D.R.1    Lavid, N.2    Zubieta, C.3    Chen, F.4    Beuerle, T.5    Lewinsohn, E.6    Noel, J.P.7    Pichersky, E.8
  • 15
    • 34249804156 scopus 로고    scopus 로고
    • Molecular modeling and site-directed mutagenesis reveal the benzylisoquinoline binding site of the short-chain dehydrogenase/reductase salutaridine reductase
    • Geissler R., Brandt W., and Ziegler J. Molecular modeling and site-directed mutagenesis reveal the benzylisoquinoline binding site of the short-chain dehydrogenase/reductase salutaridine reductase. Plant Physiol. 143 (2007) 1493-1503
    • (2007) Plant Physiol. , vol.143 , pp. 1493-1503
    • Geissler, R.1    Brandt, W.2    Ziegler, J.3
  • 16
    • 44049113918 scopus 로고
    • Formation of salutaridine from (R)-reticuline by a membrane bound cytochrome P450 enzyme from Papaver somniferum
    • Gerardy R., and Zenk M.H. Formation of salutaridine from (R)-reticuline by a membrane bound cytochrome P450 enzyme from Papaver somniferum. Phytochemistry 32 (1993) 79-86
    • (1993) Phytochemistry , vol.32 , pp. 79-86
    • Gerardy, R.1    Zenk, M.H.2
  • 17
    • 0000613388 scopus 로고
    • Purification and characterization of salutaridine: NADPH 7-oxidoreductase from Papaver somniferum
    • Gerardy R., and Zenk M.H. Purification and characterization of salutaridine: NADPH 7-oxidoreductase from Papaver somniferum. Phytochemistry 34 (1993) 125-132
    • (1993) Phytochemistry , vol.34 , pp. 125-132
    • Gerardy, R.1    Zenk, M.H.2
  • 18
    • 69949174213 scopus 로고    scopus 로고
    • CYP719B1 is salutaridine synthase, the C-C phenol-coupling enzyme of morphine biosynthesis in opium poppy
    • doi:10.1074/jbc.M109.033373
    • Gesell, A., Rolf, M., Ziegler, J., Diaz-Chavez, M.L., Huang, F.C., Kutchan, T.M., 2009. CYP719B1 is salutaridine synthase, the C-C phenol-coupling enzyme of morphine biosynthesis in opium poppy. J. Biol. Chem. 2009, doi:10.1074/jbc.M109.033373.
    • (2009) J. Biol. Chem , pp. 2009
    • Gesell, A.1    Rolf, M.2    Ziegler, J.3    Diaz-Chavez, M.L.4    Huang, F.C.5    Kutchan, T.M.6
  • 19
    • 0035947598 scopus 로고    scopus 로고
    • Porcine carbonyl reductase structural basis for a functional monomer in short chain dehydrogenases/reductases
    • Ghosh D., Sawicki M., Pletnev V., Erman M., Ohno S., Nakajin S., and Duax W.L. Porcine carbonyl reductase structural basis for a functional monomer in short chain dehydrogenases/reductases. J. Biol. Chem. 276 (2001) 18457-18463
    • (2001) J. Biol. Chem. , vol.276 , pp. 18457-18463
    • Ghosh, D.1    Sawicki, M.2    Pletnev, V.3    Erman, M.4    Ohno, S.5    Nakajin, S.6    Duax, W.L.7
  • 20
    • 0035903228 scopus 로고    scopus 로고
    • Molecular characterization of the salutaridinol 7-O-acetyltransferase involved in morphine biosynthesis in opium poppy Papaver somniferum
    • Grothe T., Lenz R., and Kutchan T.M. Molecular characterization of the salutaridinol 7-O-acetyltransferase involved in morphine biosynthesis in opium poppy Papaver somniferum. J. Biol. Chem. 276 (2001) 30717-30723
    • (2001) J. Biol. Chem. , vol.276 , pp. 30717-30723
    • Grothe, T.1    Lenz, R.2    Kutchan, T.M.3
  • 21
    • 57749093230 scopus 로고    scopus 로고
    • A novel 2-oxoacid-dependent dioxygenase involved in the formation of the goiterogenic 2-hydroxybut-3-enyl glucosinolate and generalist insect resistance in Arabidopsis
    • Hansen B.G., Kerwin R.E., Ober J.A., Lambrix V.M., Mitchell-Olds T., Gershenzon J., Halkier B.A., and Kliebenstein D.J. A novel 2-oxoacid-dependent dioxygenase involved in the formation of the goiterogenic 2-hydroxybut-3-enyl glucosinolate and generalist insect resistance in Arabidopsis. Plant Physiol. 148 (2008) 2096-2108
    • (2008) Plant Physiol. , vol.148 , pp. 2096-2108
    • Hansen, B.G.1    Kerwin, R.E.2    Ober, J.A.3    Lambrix, V.M.4    Mitchell-Olds, T.5    Gershenzon, J.6    Halkier, B.A.7    Kliebenstein, D.J.8
  • 23
    • 2142751582 scopus 로고    scopus 로고
    • 1,2-Dehydroreticuline synthase, the branch point enzyme opening the morphinan biosynthetic pathway
    • Hirata K., Poeaknapo C., Schmidt J., and Zenk M.H. 1,2-Dehydroreticuline synthase, the branch point enzyme opening the morphinan biosynthetic pathway. Phytochemistry 65 (2004) 1039-1046
    • (2004) Phytochemistry , vol.65 , pp. 1039-1046
    • Hirata, K.1    Poeaknapo, C.2    Schmidt, J.3    Zenk, M.H.4
  • 24
    • 0034161828 scopus 로고    scopus 로고
    • Distribution of morphinan and benzo[c]phenanthridine alkaloid gene transcript accumulation in Papaver somniferum
    • Huang F.C., and Kutchan T.M. Distribution of morphinan and benzo[c]phenanthridine alkaloid gene transcript accumulation in Papaver somniferum. Phytochemistry 53 (2000) 555-564
    • (2000) Phytochemistry , vol.53 , pp. 555-564
    • Huang, F.C.1    Kutchan, T.M.2
  • 25
    • 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., and Sato F. 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 (2003) 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
  • 26
    • 33846827049 scopus 로고    scopus 로고
    • Molecular cloning and characterization of methylenedioxy bridge-forming enzymes involved in stylopine biosynthesis in Eschscholzia californica
    • Ikezawa N., Iwasa K., and Sato F. Molecular cloning and characterization of methylenedioxy bridge-forming enzymes involved in stylopine biosynthesis in Eschscholzia californica. FEBS J. 274 (2007) 1019-1035
    • (2007) FEBS J. , vol.274 , pp. 1019-1035
    • Ikezawa, N.1    Iwasa, K.2    Sato, F.3
  • 27
    • 42249110738 scopus 로고    scopus 로고
    • Molecular cloning and characterization of CYP80G2, a cytochrome P450 which catalyzes an intramolecular C-C phenol coupling of (S)-reticuline in magnoflorine biosynthesis, from cultured Coptis japonica cells
    • Ikezawa N., Iwasa K., and Sato F. Molecular cloning and characterization of CYP80G2, a cytochrome P450 which catalyzes an intramolecular C-C phenol coupling of (S)-reticuline in magnoflorine biosynthesis, from cultured Coptis japonica cells. J. Biol. Chem. 283 (2008) 8810-8821
    • (2008) J. Biol. Chem. , vol.283 , pp. 8810-8821
    • Ikezawa, N.1    Iwasa, K.2    Sato, F.3
  • 28
    • 58149242229 scopus 로고    scopus 로고
    • CYP719A subfamily of cytochrome P450 oxygenases and isoquinoline alkaloid biosynthesis in Eschscholzia californica
    • Ikezawa N., Iwasa K., and Sato F. CYP719A subfamily of cytochrome P450 oxygenases and isoquinoline alkaloid biosynthesis in Eschscholzia californica. Plant Cell Rep. 28 (2009) 123-133
    • (2009) Plant Cell Rep. , vol.28 , pp. 123-133
    • Ikezawa, N.1    Iwasa, K.2    Sato, F.3
  • 29
    • 33847228083 scopus 로고    scopus 로고
    • Overexpression of Coptis japonica norcoclaurine 6-O-methyltransferase overcomes the rate-limiting step in benzylisoquinoline alkaloid biosynthesis in cultured Eschscholzia californica
    • Inui T., Tamura K., Fujii N., Morishige T., and Sato F. Overexpression of Coptis japonica norcoclaurine 6-O-methyltransferase overcomes the rate-limiting step in benzylisoquinoline alkaloid biosynthesis in cultured Eschscholzia californica. Plant Cell Physiol. 48 (2007) 252-262
    • (2007) Plant Cell Physiol. , vol.48 , pp. 252-262
    • Inui, T.1    Tamura, K.2    Fujii, N.3    Morishige, T.4    Sato, F.5
  • 30
    • 0010426560 scopus 로고
    • Secondary compounds of the Ranunculiflorae
    • Jensen, U., 1995. Secondary compounds of the Ranunculiflorae. Plant Syst. Evol. (Suppl.) 9, 89-97.
    • (1995) Plant Syst. Evol. (Suppl.) , vol.9 , pp. 89-97
    • Jensen, U.1
  • 32
    • 64949176017 scopus 로고    scopus 로고
    • RNAi suppression of the morphine biosynthetic gene salAT and evidence of association of pathway enzymes
    • Kempe K., Higashi Y., Frick S., Sabarna K., and Kutchan T.M. RNAi suppression of the morphine biosynthetic gene salAT and evidence of association of pathway enzymes. Phytochemistry 70 (2009) 579-589
    • (2009) Phytochemistry , vol.70 , pp. 579-589
    • Kempe, K.1    Higashi, Y.2    Frick, S.3    Sabarna, K.4    Kutchan, T.M.5
  • 33
    • 0028928192 scopus 로고
    • Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C-O phenol-coupling cytochrome P450 from the higher plant Berberis stolonifera
    • Kraus P.F., and Kutchan T.M. Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C-O phenol-coupling cytochrome P450 from the higher plant Berberis stolonifera. Proc. Natl. Acad. Sci. USA 92 (1995) 2071-2075
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2071-2075
    • Kraus, P.F.1    Kutchan, T.M.2
  • 34
    • 0035542786 scopus 로고    scopus 로고
    • The Arabidopsis epithiospecifier protein promotes the hydrolysis of glucosinolates to nitriles and influences Trichoplusia ni herbivory
    • Lambrix V., Reichelt M., Mitchell-Olds T., Kliebenstein D.J., and Gershenzon J. The Arabidopsis epithiospecifier protein promotes the hydrolysis of glucosinolates to nitriles and influences Trichoplusia ni herbivory. Plant Cell 13 (2001) 2793-2807
    • (2001) Plant Cell , vol.13 , pp. 2793-2807
    • Lambrix, V.1    Reichelt, M.2    Mitchell-Olds, T.3    Kliebenstein, D.J.4    Gershenzon, J.5
  • 35
    • 0028245117 scopus 로고
    • Closure of the oxide bridge in morphine biosynthesis
    • Lenz R., and Zenk M.H. Closure of the oxide bridge in morphine biosynthesis. Tetrahedron Lett. 35 (1994) 3897-4000
    • (1994) Tetrahedron Lett. , vol.35 , pp. 3897-4000
    • Lenz, R.1    Zenk, M.H.2
  • 36
    • 0029559296 scopus 로고
    • Acetyl coenzyme A: salutaridinol-7-O-acetyltransferase from Papaver somniferum plant cell cultures. The enzyme catalyzing the formation of thebaine in morphine biosynthesis
    • Lenz R., and Zenk M.H. Acetyl coenzyme A: salutaridinol-7-O-acetyltransferase from Papaver somniferum plant cell cultures. The enzyme catalyzing the formation of thebaine in morphine biosynthesis. J. Biol. Chem. 270 (1995) 31091-31096
    • (1995) J. Biol. Chem. , vol.270 , pp. 31091-31096
    • Lenz, R.1    Zenk, M.H.2
  • 37
    • 0028871826 scopus 로고
    • Purification and properties of codeinone reductase (NADPH) from Papaver somniferum cell cultures and differentiated plants
    • Lenz R., and Zenk M.H. Purification and properties of codeinone reductase (NADPH) from Papaver somniferum cell cultures and differentiated plants. Eur. J. Biochem. 233 (1995) 132-139
    • (1995) Eur. J. Biochem. , vol.233 , pp. 132-139
    • Lenz, R.1    Zenk, M.H.2
  • 38
    • 34447529465 scopus 로고    scopus 로고
    • Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy
    • Liscombe D.K., and Facchini P.J. Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy. J. Biol. Chem. 282 (2007) 14741-14751
    • (2007) J. Biol. Chem. , vol.282 , pp. 14741-14751
    • Liscombe, D.K.1    Facchini, P.J.2
  • 39
    • 20444396193 scopus 로고    scopus 로고
    • Evidence for the monophyletic evolution of benzylisoquinoline alkaloid biosynthesis in angiosperms
    • Liscombe D.K., MacLeod B.P., Loukanina N., Nandi O.I., and Facchini P.J. Evidence for the monophyletic evolution of benzylisoquinoline alkaloid biosynthesis in angiosperms. Phytochemistry 66 (2005) 2501-2520
    • (2005) Phytochemistry , vol.66 , pp. 2501-2520
    • Liscombe, D.K.1    MacLeod, B.P.2    Loukanina, N.3    Nandi, O.I.4    Facchini, P.J.5
  • 41
    • 34250332680 scopus 로고    scopus 로고
    • Functional analysis of norcoclaurine synthase in Coptis japonica
    • Minami H., Dubouzet E., Iwasa K., and Sato F. Functional analysis of norcoclaurine synthase in Coptis japonica. J. Biol. Chem. 282 (2007) 6274-6282
    • (2007) J. Biol. Chem. , vol.282 , pp. 6274-6282
    • Minami, H.1    Dubouzet, E.2    Iwasa, K.3    Sato, F.4
  • 42
    • 0034725710 scopus 로고    scopus 로고
    • Molecular characterization of the S-adenosyl-l-methionine: 3′-hydroxy-N-methylcoclaurine 4′-O-methyltransferase involved in isoquinoline alkaloid biosynthesis in Coptis japonica
    • Morishige T., Tsujita T., Yamada Y., and Sato F. Molecular characterization of the S-adenosyl-l-methionine: 3′-hydroxy-N-methylcoclaurine 4′-O-methyltransferase involved in isoquinoline alkaloid biosynthesis in Coptis japonica. J. Biol. Chem. 275 (2000) 23398-23405
    • (2000) J. Biol. Chem. , vol.275 , pp. 23398-23405
    • Morishige, T.1    Tsujita, T.2    Yamada, Y.3    Sato, F.4
  • 43
    • 0036439059 scopus 로고    scopus 로고
    • Molecular cloning of columbamine O-methyltransferase from cultured Coptis japonica cells
    • Morishige T., Dubouzet E., Choi K.B., Yazaki K., and Sato F. Molecular cloning of columbamine O-methyltransferase from cultured Coptis japonica cells. Eur. J. Biochem. 269 (2002) 5659-5667
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5659-5667
    • Morishige, T.1    Dubouzet, E.2    Choi, K.B.3    Yazaki, K.4    Sato, F.5
  • 44
    • 0033227533 scopus 로고    scopus 로고
    • Two tropinone reductases, that catalyze opposite stereospecific reductions in tropane alkaloid biosynthesis, are localized in plant root with different cell-specific patterns
    • Nakajima K., and Hashimoto T. Two tropinone reductases, that catalyze opposite stereospecific reductions in tropane alkaloid biosynthesis, are localized in plant root with different cell-specific patterns. Plant Cell Physiol. 40 (1999) 1099-1107
    • (1999) Plant Cell Physiol. , vol.40 , pp. 1099-1107
    • Nakajima, K.1    Hashimoto, T.2
  • 45
    • 0027449067 scopus 로고
    • Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor
    • Nakajima K., Hashimoto T., and Yamada Y. Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 9591-9595
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9591-9595
    • Nakajima, K.1    Hashimoto, T.2    Yamada, Y.3
  • 46
    • 0033593052 scopus 로고    scopus 로고
    • Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase
    • Ober D., and Hartmann T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14777-14782
    • Ober, D.1    Hartmann, T.2
  • 47
    • 0034534251 scopus 로고    scopus 로고
    • Phylogenetic origin of a secondary pathway: the case of pyrrolizidine alkaloids
    • Ober D., and Hartmann T. Phylogenetic origin of a secondary pathway: the case of pyrrolizidine alkaloids. Plant Mol. Biol. 44 (2000) 445-450
    • (2000) Plant Mol. Biol. , vol.44 , pp. 445-450
    • Ober, D.1    Hartmann, T.2
  • 48
    • 0031021249 scopus 로고    scopus 로고
    • Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions
    • Oppermann U.C., Filling C., Berndt K.D., Persson B., Benach J., Ladenstein R., and Jörnvall H. Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions. Biochemistry 36 (1997) 34-40
    • (1997) Biochemistry , vol.36 , pp. 34-40
    • Oppermann, U.C.1    Filling, C.2    Berndt, K.D.3    Persson, B.4    Benach, J.5    Ladenstein, R.6    Jörnvall, H.7
  • 49
    • 0347317979 scopus 로고    scopus 로고
    • (R,S)-Reticuline 7-O-methyltransferase and (R,S)-norcoclaurine 6-O-methyltransferase of Papaver somniferum - cDNA cloning and characterization of methyl transfer enzymes of alkaloid biosynthesis in opium poppy
    • Ounaroon A., Decker G., Schmidt J., Lottspeich F., and Kutchan T.M. (R,S)-Reticuline 7-O-methyltransferase and (R,S)-norcoclaurine 6-O-methyltransferase of Papaver somniferum - cDNA cloning and characterization of methyl transfer enzymes of alkaloid biosynthesis in opium poppy. Plant J. 36 (2003) 808-819
    • (2003) Plant J. , vol.36 , pp. 808-819
    • Ounaroon, A.1    Decker, G.2    Schmidt, J.3    Lottspeich, F.4    Kutchan, T.M.5
  • 50
    • 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., and 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. 13 (1998) 793-801
    • (1998) Plant J. , vol.13 , pp. 793-801
    • Pauli, H.H.1    Kutchan, T.M.2
  • 51
    • 70349499351 scopus 로고    scopus 로고
    • Pienkny, S., Brandt, W., Schmidt, J., Kramell, R., Ziegler, J., 2009. Functional characterization of a novel benzylisoquinoline O-methyltransferase suggests its involvement in papaverine biosynthesis in opium poppy (Papaver somniferum L.). Plant J. doi:10.1111/j.1365-313X.2009.03937.x.
    • Pienkny, S., Brandt, W., Schmidt, J., Kramell, R., Ziegler, J., 2009. Functional characterization of a novel benzylisoquinoline O-methyltransferase suggests its involvement in papaverine biosynthesis in opium poppy (Papaver somniferum L.). Plant J. doi:10.1111/j.1365-313X.2009.03937.x.
  • 52
    • 0141790402 scopus 로고    scopus 로고
    • Monoterpene double-bond reductases of the (-)-menthol biosynthetic pathway: isolation and characterization of cDNAs encoding (-)-isopiperitenone reductase and (+)-pulegone reductase of peppermint
    • Ringer K.L., McConkey M.E., Davis E.M., Rushing G.W., and Croteau R. Monoterpene double-bond reductases of the (-)-menthol biosynthetic pathway: isolation and characterization of cDNAs encoding (-)-isopiperitenone reductase and (+)-pulegone reductase of peppermint. Arch. Biochem. Biophys. 418 (2003) 80-92
    • (2003) Arch. Biochem. Biophys. , vol.418 , pp. 80-92
    • Ringer, K.L.1    McConkey, M.E.2    Davis, E.M.3    Rushing, G.W.4    Croteau, R.5
  • 53
    • 6444243887 scopus 로고    scopus 로고
    • Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis
    • Samanani N., Liscombe D.K., and Facchini P.J. Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis. Plant J. 40 (2004) 302-313
    • (2004) Plant J. , vol.40 , pp. 302-313
    • Samanani, N.1    Liscombe, D.K.2    Facchini, P.J.3
  • 56
    • 29444432259 scopus 로고    scopus 로고
    • Putrescine N-methyltransferase in Solanum tuberosum L., a calystegine-forming plant
    • Stenzel O., Teuber M., and Dräger B. Putrescine N-methyltransferase in Solanum tuberosum L., a calystegine-forming plant. Planta 223 (2006) 200-212
    • (2006) Planta , vol.223 , pp. 200-212
    • Stenzel, O.1    Teuber, M.2    Dräger, B.3
  • 57
    • 0029137429 scopus 로고
    • Molecular cloning and characterization of S-adenosyl-l-methionine: scoulerine-9-O-methyltransferase from cultured cells of Coptis japonica
    • Takeshita N., Fujiwara H., Mimura H., Fitchen J.H., Yamada Y., and Sato F. Molecular cloning and characterization of S-adenosyl-l-methionine: scoulerine-9-O-methyltransferase from cultured cells of Coptis japonica. Plant Cell Physiol. 36 (1995) 29-36
    • (1995) Plant Cell Physiol. , vol.36 , pp. 29-36
    • Takeshita, N.1    Fujiwara, H.2    Mimura, H.3    Fitchen, J.H.4    Yamada, Y.5    Sato, F.6
  • 60
    • 33646157726 scopus 로고    scopus 로고
    • Terpene synthases and the regulation, diversity and biological roles of terpene metabolism
    • Tholl D. Terpene synthases and the regulation, diversity and biological roles of terpene metabolism. Curr. Opin. Plant Biol. 9 (2006) 297-304
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 297-304
    • Tholl, D.1
  • 61
    • 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., and 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. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 62
    • 0038025413 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of three distinct N-methyltransferases involved in the caffeine biosynthetic pathway in coffee plants
    • Uefuji H., Ogita S., Yamaguchi Y., Koizumi N., and Sano H. Molecular cloning and functional characterization of three distinct N-methyltransferases involved in the caffeine biosynthetic pathway in coffee plants. Plant Physiol. 132 (2003) 372-380
    • (2003) Plant Physiol. , vol.132 , pp. 372-380
    • Uefuji, H.1    Ogita, S.2    Yamaguchi, Y.3    Koizumi, N.4    Sano, H.5
  • 63
    • 0033152629 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of codeinone reductase: the penultimate enzyme in morphine biosynthesis in the opium poppy Papaver somniferum
    • Unterlinner B., Lenz R., and Kutchan T.M. Molecular cloning and functional expression of codeinone reductase: the penultimate enzyme in morphine biosynthesis in the opium poppy Papaver somniferum. Plant J. 18 (1999) 465-475
    • (1999) Plant J. , vol.18 , pp. 465-475
    • Unterlinner, B.1    Lenz, R.2    Kutchan, T.M.3
  • 64
    • 0033799536 scopus 로고    scopus 로고
    • Glycosyltransferases in plant natural product synthesis: characterization of a supergene family
    • Vogt T., and Jones P. Glycosyltransferases in plant natural product synthesis: characterization of a supergene family. Trends Plant Sci. 5 (2000) 380-386
    • (2000) Trends Plant Sci. , vol.5 , pp. 380-386
    • Vogt, T.1    Jones, P.2
  • 65
    • 44949127129 scopus 로고    scopus 로고
    • Alkaloid biosynthesis: metabolism and trafficking
    • Ziegler J., and Facchini P.J. Alkaloid biosynthesis: metabolism and trafficking. Annu. Rev. Plant Biol. 59 (2008) 735-769
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 735-769
    • Ziegler, J.1    Facchini, P.J.2
  • 66
    • 26644468125 scopus 로고    scopus 로고
    • Comparative macroarray analysis of morphine containing Papaver somniferum and eight morphine free Papaver species identifies an O-methyltransferase involved in benzylisoquinoline biosynthesis
    • Ziegler J., Diaz-Chavez M.L., Kramell R., Ammer C., and Kutchan T.M. Comparative macroarray analysis of morphine containing Papaver somniferum and eight morphine free Papaver species identifies an O-methyltransferase involved in benzylisoquinoline biosynthesis. Planta 222 (2005) 458-471
    • (2005) Planta , vol.222 , pp. 458-471
    • Ziegler, J.1    Diaz-Chavez, M.L.2    Kramell, R.3    Ammer, C.4    Kutchan, T.M.5
  • 67
    • 33749241876 scopus 로고    scopus 로고
    • Comparative transcript and alkaloid profiling in Papaver species identifies a short chain dehydrogenase/reductase involved in morphine biosynthesis
    • Ziegler J., Voigtländer S., Schmidt J., Kramell R., Miersch O., Ammer C., Gesell A., and Kutchan T.M. Comparative transcript and alkaloid profiling in Papaver species identifies a short chain dehydrogenase/reductase involved in morphine biosynthesis. Plant J. 48 (2006) 177-192
    • (2006) Plant J. , vol.48 , pp. 177-192
    • Ziegler, J.1    Voigtländer, S.2    Schmidt, J.3    Kramell, R.4    Miersch, O.5    Ammer, C.6    Gesell, A.7    Kutchan, T.M.8
  • 68
    • 0035119588 scopus 로고    scopus 로고
    • Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases
    • Zubieta C., He X.Z., Dixon R.A., and Noel J.P. Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases. Nat. Struct. Biol. 8 (2001) 271-279
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 271-279
    • Zubieta, C.1    He, X.Z.2    Dixon, R.A.3    Noel, J.P.4
  • 69
    • 0035983842 scopus 로고    scopus 로고
    • Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase
    • Zubieta C., Kota P., Ferrer J.L., Dixon R.A., and Noel J.P. Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase. Plant Cell 14 (2002) 1265-1277
    • (2002) Plant Cell , vol.14 , pp. 1265-1277
    • Zubieta, C.1    Kota, P.2    Ferrer, J.L.3    Dixon, R.A.4    Noel, J.P.5
  • 70


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