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Volumn 65, Issue , 2014, Pages 225-257

Triterpene biosynthesis in plants

Author keywords

metabolic gene clusters; oxidosqualene cyclases; specialized metabolites; sterols; synthetic biology

Indexed keywords

SAPONIN; TRITERPENE;

EID: 84899736825     PISSN: 15435008     EISSN: 15452123     Source Type: Book Series    
DOI: 10.1146/annurev-arplant-050312-120229     Document Type: Review
Times cited : (587)

References (167)
  • 1
    • 36349025257 scopus 로고    scopus 로고
    • Enzymatic synthesis of cyclic triterpenes
    • Abe I. 2007. Enzymatic synthesis of cyclic triterpenes. Nat. Prod. Rep. 24:1311-31
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 1311-1331
    • Abe, I.1
  • 2
    • 3042733473 scopus 로고    scopus 로고
    • Mechanism and stereochemistry of enzymatic cyclization of 24,30-bisnor-2,3-oxidosqualene by recombinant β-amyrin synthase
    • Abe I, Sakano Y, Sodeyama M, Tanaka H, Noguchi H, et al. 2004. Mechanism and stereochemistry of enzymatic cyclization of 24,30-bisnor-2,3-oxidosqualene by recombinant β-amyrin synthase. J. Am. Chem. Soc. 126:6880-81
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6880-6881
    • Abe, I.1    Sakano, Y.2    Sodeyama, M.3    Tanaka, H.4    Noguchi, H.5
  • 3
    • 1642340664 scopus 로고    scopus 로고
    • Enzymatic cyclization of 22,23-dihydro- 2,3-oxidosqualene into euph-7-en-3β-ol and bacchar-12-en-3β-ol by recombinant β-amyrin synthase
    • Abe I, Sakano Y, Tanaka H, Lou W, Noguchi H, et al. 2004. Enzymatic cyclization of 22,23-dihydro- 2,3-oxidosqualene into euph-7-en-3β-ol and bacchar-12-en-3β-ol by recombinant β-amyrin synthase. J. Am. Chem. Soc. 126:3426-27
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3426-3427
    • Abe, I.1    Sakano, Y.2    Tanaka, H.3    Lou, W.4    Noguchi, H.5
  • 4
    • 15544364507 scopus 로고    scopus 로고
    • Genomics-based selection and functional characterization of triterpene glycosyltransferases from the model legume Medicago truncatula
    • Achnine L, Huhman DV, Farag MA, Sumner LW, Blount JW, Dixon RA. 2005. Genomics-based selection and functional characterization of triterpene glycosyltransferases from the model legume Medicago truncatula. Plant J. 41:875-87
    • (2005) Plant J. , vol.41 , pp. 875-887
    • Achnine, L.1    Huhman, D.V.2    Farag, M.A.3    Sumner, L.W.4    Blount, J.W.5    Dixon, R.A.6
  • 5
    • 84870792724 scopus 로고    scopus 로고
    • UDP-glycosyltransferases from the UGT73C subfamily in Barbarea vulgaris catalyze sapogenin 3-O-glucosylation in saponin-mediated insect resistance
    • Augustin JM, Drok S, Shinoda T, Sanmiya K, Nielsen JK, et al. 2012. UDP-glycosyltransferases from the UGT73C subfamily in Barbarea vulgaris catalyze sapogenin 3-O-glucosylation in saponin-mediated insect resistance. Plant Physiol. 160:1881-95
    • (2012) Plant Physiol. , vol.160 , pp. 1881-1895
    • Augustin, J.M.1    Drok, S.2    Shinoda, T.3    Sanmiya, K.4    Nielsen, J.K.5
  • 6
    • 79952900480 scopus 로고    scopus 로고
    • Molecular activities, biosynthesis and evolution of triterpenoid saponins
    • Augustin JM, Kuzina V, Andersen SB, Bak S. 2011. Molecular activities, biosynthesis and evolution of triterpenoid saponins. Phytochemistry 72:435-57
    • (2011) Phytochemistry , vol.72 , pp. 435-457
    • Augustin, J.M.1    Kuzina, V.2    Andersen, S.B.3    Bak, S.4
  • 7
    • 33750689113 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a multifunctional triterpene synthase cDNA from a mangrove species Kandelia candel (L.) Druce
    • Basyuni M, Oku H, Inafuku M, Baba S, Iwasaki H, et al. 2006. Molecular cloning and functional expression of a multifunctional triterpene synthase cDNA from a mangrove species Kandelia candel (L.) Druce. Phytochemistry 67:2517-24
    • (2006) Phytochemistry , vol.67 , pp. 2517-2524
    • Basyuni, M.1    Oku, H.2    Inafuku, M.3    Baba, S.4    Iwasaki, H.5
  • 8
    • 34748823517 scopus 로고    scopus 로고
    • Triterpene synthases from the Okinawan mangrove tribe, Rhizophoraceae
    • Basyuni M, Oku H, Tsujimoto E, Kinjo K, Baba S, Takara K. 2007. Triterpene synthases from the Okinawan mangrove tribe, Rhizophoraceae. FEBS J. 274:5028-42
    • (2007) FEBS J. , vol.274 , pp. 5028-5042
    • Basyuni, M.1    Oku, H.2    Tsujimoto, E.3    Kinjo, K.4    Baba, S.5    Takara, K.6
  • 9
    • 0037238414 scopus 로고    scopus 로고
    • Steroid biosynthesis in prokaryotes: Identification of myxobacterial steroids and cloning of the first bacterial 2,3(S)- oxidosqualene cyclase from the myxobacterium Stigmatella aurantiaca
    • Bode HB, Zeggel B, Silakowski B, Wenzel SC, Reichenbach H, et al. 2003. Steroid biosynthesis in prokaryotes: identification of myxobacterial steroids and cloning of the first bacterial 2,3(S)- oxidosqualene cyclase from the myxobacterium Stigmatella aurantiaca. Mol. Microbiol. 47:471-81
    • (2003) Mol. Microbiol. , vol.47 , pp. 471-481
    • Bode, H.B.1    Zeggel, B.2    Silakowski, B.3    Wenzel, S.C.4    Reichenbach, H.5
  • 11
    • 79959941055 scopus 로고    scopus 로고
    • An unusual plant triterpene synthase with predominantα-amyrin- producing activity identified by characterizing oxidosqualene cyclases from Malus × domestica
    • Brendolise C, Yauk Y-K, Eberhard ED, Wang M, Chagne D, et al. 2011. An unusual plant triterpene synthase with predominantα-amyrin-producing activity identified by characterizing oxidosqualene cyclases from Malus × domestica. FEBS J. 278:2485-99
    • (2011) FEBS J. , vol.278 , pp. 2485-2499
    • Brendolise, C.1    Yauk, Y.-K.2    Eberhard, E.D.3    Wang, M.4    Chagne, D.5
  • 12
    • 34748872633 scopus 로고    scopus 로고
    • Chemical composition of the epicuticular and intracuticular wax layers on the adaxial side of Ligustrum vulgare leaves
    • Buschhaus C, Herz H, Jetter R. 2007. Chemical composition of the epicuticular and intracuticular wax layers on the adaxial side of Ligustrum vulgare leaves. New Phytol. 176:311-16
    • (2007) New Phytol. , vol.176 , pp. 311-316
    • Buschhaus, C.1    Herz, H.2    Jetter, R.3
  • 13
    • 84867137564 scopus 로고    scopus 로고
    • Composition and physiological function of the wax layers coating Arabidopsis leaves: β-Amyrin negatively affects the intracuticular water barrier
    • Buschhaus C, Jetter R. 2012. Composition and physiological function of the wax layers coating Arabidopsis leaves: β-Amyrin negatively affects the intracuticular water barrier. Plant Physiol. 160:1120-29
    • (2012) Plant Physiol. , vol.160 , pp. 1120-1129
    • Buschhaus, C.1    Jetter, R.2
  • 14
    • 47549107647 scopus 로고    scopus 로고
    • Molecular characterization of β-amyrin synthase from Aster sedifolius L. and triterpenoid saponin analysis
    • Cammareri M, Consiglio MF, Pecchia P, Corea G, Lanzotti V, et al. 2008. Molecular characterization of β-amyrin synthase from Aster sedifolius L. and triterpenoid saponin analysis. Plant Sci. 175:255-61
    • (2008) Plant Sci. , vol.175 , pp. 255-261
    • Cammareri, M.1    Consiglio, M.F.2    Pecchia, P.3    Corea, G.4    Lanzotti, V.5
  • 16
    • 77955822715 scopus 로고    scopus 로고
    • Diterpene synthases and the nature of the isoprene fold
    • Cao R, Zhang Y, Mann FM, Huang C, Mukkamala D et al. 2010. Diterpene synthases and the nature of the isoprene fold. Proteins 78:2417-32
    • (2010) Proteins , vol.78 , pp. 2417-2432
    • Cao, R.1    Zhang, Y.2    Mann, F.M.3    Huang, C.4    Mukkamala, D.5
  • 17
    • 84859165041 scopus 로고    scopus 로고
    • A genome-wide phylogenetic reconstruction of family 1 UDP-glycosyltransferases revealed the expansion of the family during the adaptation of plants to life on land
    • Caputi L, Malnoy M, Goremykin V, Nikiforova S, Martens S. 2012. A genome-wide phylogenetic reconstruction of family 1 UDP-glycosyltransferases revealed the expansion of the family during the adaptation of plants to life on land. Plant J. 69:1030-42
    • (2012) Plant J. , vol.69 , pp. 1030-1042
    • Caputi, L.1    Malnoy, M.2    Goremykin, V.3    Nikiforova, S.4    Martens, S.5
  • 18
    • 84905538254 scopus 로고    scopus 로고
    • Medicago truncatula CYP716A12 is a multifunctional oxidase involved in the biosynthesis of hemolytic saponins
    • Carelli M, Biazzi E, Panara F, Tava A, Scaramelli L, et al. 2011. Medicago truncatula CYP716A12 is a multifunctional oxidase involved in the biosynthesis of hemolytic saponins. Plant Cell 23:3070-81
    • (2011) Plant Cell , vol.23 , pp. 3070-3081
    • Carelli, M.1    Biazzi, E.2    Panara, F.3    Tava, A.4    Scaramelli, L.5
  • 19
    • 47049087906 scopus 로고    scopus 로고
    • Akinetic analysis of regiospecific glucosylation by two glycosyltransferases of Arabidopsis thaliana: Domain swapping to introduce new activities
    • Cartwright AM, Lim EK, Kleanthous C, Bowles DJ. 2008. Akinetic analysis of regiospecific glucosylation by two glycosyltransferases of Arabidopsis thaliana: domain swapping to introduce new activities. J. Biol. Chem. 283:15724-31
    • (2008) J. Biol. Chem. , vol.283 , pp. 15724-15731
    • Cartwright, A.M.1    Lim, E.K.2    Kleanthous, C.3    Bowles, D.J.4
  • 20
    • 84876471789 scopus 로고    scopus 로고
    • An effective strategy for exploring unknown metabolic pathways by genome mining
    • Castillo DA, Kolesnikova MD, Matsuda SPT. 2013. An effective strategy for exploring unknown metabolic pathways by genome mining. J. Am. Chem. Soc. 135:5885-94
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 5885-5894
    • Castillo, D.A.1    Kolesnikova, M.D.2    Matsuda, S.P.T.3
  • 21
    • 0036008773 scopus 로고    scopus 로고
    • The genetics and molecular genetics of terpene and sterol origami
    • Chappell J. 2002. The genetics and molecular genetics of terpene and sterol origami. Curr. Opin. Plant Biol. 5:151-57
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 151-157
    • Chappell, J.1
  • 22
    • 0027146637 scopus 로고
    • Isolation of an Arabidopsis thaliana gene encoding cycloartenol synthase by functional expression in a yeast mutant lacking lanosterol synthase by the use of a chromatographic screen
    • Corey EJ, Matsuda SP, Bartel B. 1993. Isolation of an Arabidopsis thaliana gene encoding cycloartenol synthase by functional expression in a yeast mutant lacking lanosterol synthase by the use of a chromatographic screen. Proc. Natl. Acad. Sci. USA 90:11628-32
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11628-11632
    • Corey, E.J.1    Matsuda, S.P.2    Bartel, B.3
  • 26
    • 30144439471 scopus 로고    scopus 로고
    • Revisited after 50 years: The "stereochemical interpretation of the biogenetic isoprene rule for the triterpenes."
    • Eschenmoser A, Arigoni D. 2005. Revisited after 50 years: the "stereochemical interpretation of the biogenetic isoprene rule for the triterpenes." Helv. Chim. Acta 88:3011-50
    • (2005) Helv. Chim. Acta , vol.88 , pp. 3011-3050
    • Eschenmoser, A.1    Arigoni, D.2
  • 27
    • 2442615925 scopus 로고    scopus 로고
    • Genome mining to identify new plant triterpenoids
    • Fazio GC, Xu R, Matsuda SP. 2004. Genome mining to identify new plant triterpenoids. J. Am. Chem. Soc. 126:5678-79
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5678-5679
    • Fazio, G.C.1    Xu, R.2    Matsuda, S.P.3
  • 29
    • 42549088178 scopus 로고    scopus 로고
    • Metabolic diversification-independent assembly of operon-like gene clusters in different plants
    • Field B, Osbourn AE. 2008. Metabolic diversification-independent assembly of operon-like gene clusters in different plants. Science 320:543-47
    • (2008) Science , vol.320 , pp. 543-547
    • Field, B.1    Osbourn, A.E.2
  • 30
    • 83255176933 scopus 로고    scopus 로고
    • CYP716A subfamily members are multifunctional oxidases in triterpenoid biosynthesis
    • Fukushima EO, Seki H, Ohyama K, Ono E, Umemoto N, et al. 2011. CYP716A subfamily members are multifunctional oxidases in triterpenoid biosynthesis. Plant Cell Physiol. 52:2050-61
    • (2011) Plant Cell Physiol. , vol.52 , pp. 2050-2061
    • Fukushima, E.O.1    Seki, H.2    Ohyama, K.3    Ono, E.4    Umemoto, N.5
  • 31
    • 84877983328 scopus 로고    scopus 로고
    • Combinatorial biosynthesis of legume natural and rare triterpenoids in engineered yeast
    • Fukushima EO, Seki H, Sawai S, Suzuki M, Ohyama K, et al. 2013. Combinatorial biosynthesis of legume natural and rare triterpenoids in engineered yeast. Plant Cell Physiol. 54:740-49
    • (2013) Plant Cell Physiol. , vol.54 , pp. 740-749
    • Fukushima, E.O.1    Seki, H.2    Sawai, S.3    Suzuki, M.4    Ohyama, K.5
  • 32
    • 84883335229 scopus 로고    scopus 로고
    • Biochemical analysis of a multi-functional cytochrome P450 (CYP51) enzyme required for synthesis of antimicrobial triterpenes in plants
    • Geisler K, Hughes RK, Sainsbury F, Lomonossoff GP, Rejzek M, et al. 2013. Biochemical analysis of a multi-functional cytochrome P450 (CYP51) enzyme required for synthesis of antimicrobial triterpenes in plants. Proc. Natl. Acad. Sci. USA 110:E3360-67
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110
    • Geisler, K.1    Hughes, R.K.2    Sainsbury, F.3    Lomonossoff, G.P.4    Rejzek, M.5
  • 33
    • 84870058336 scopus 로고    scopus 로고
    • Identification of marneral synthase, which is critical for growth and development in Arabidopsis
    • Go YS, Lee SB, Kim HJ, Kim J, Park H-Y, et al. 2012. Identification of marneral synthase, which is critical for growth and development in Arabidopsis. Plant J. 72:791-804
    • (2012) Plant J. , vol.72 , pp. 791-804
    • Go, Y.S.1    Lee, S.B.2    Kim, H.J.3    Kim, J.4    Park, H.-Y.5
  • 34
    • 0038717630 scopus 로고    scopus 로고
    • Cloning and characterization of the Dictyostelium discoideum cycloartenol synthase cDNA
    • Godzina SM, Lovato MA, Meyer MM, Foster KA, Wilson WK, et al. 2000. Cloning and characterization of the Dictyostelium discoideum cycloartenol synthase cDNA. Lipids 35:249-55
    • (2000) Lipids , vol.35 , pp. 249-255
    • Godzina, S.M.1    Lovato, M.A.2    Meyer, M.M.3    Foster, K.A.4    Wilson, W.K.5
  • 35
    • 33646151860 scopus 로고    scopus 로고
    • Cloning and characterization of a lupeol synthase involved in the synthesis of epicuticular wax crystals on stem and hypocotyl surfaces of Ricinus communis
    • Guhling O, Hobl B, Yeats T, Jetter R. 2006. Cloning and characterization of a lupeol synthase involved in the synthesis of epicuticular wax crystals on stem and hypocotyl surfaces of Ricinus communis. Arch. Biochem. Biophys. 448:60-72
    • (2006) Arch. Biochem. Biophys. , vol.448 , pp. 60-72
    • Guhling, O.1    Hobl, B.2    Yeats, T.3    Jetter, R.4
  • 36
    • 84872171321 scopus 로고    scopus 로고
    • Plant P450s as drivers for evolution of species-specific chemical diversity
    • Hamberger B, Bak S. 2013. Plant P450s as drivers for evolution of species-specific chemical diversity. Philos. Trans. R. Soc. B 368:20120426
    • (2013) Philos. Trans. R. Soc. B , vol.368 , pp. 20120426
    • Hamberger, B.1    Bak, S.2
  • 37
    • 84866386264 scopus 로고    scopus 로고
    • Cytochrome P450 CYP716A53v2 catalyzes the formation of protopanaxatriol from protopanaxadiol during ginsenoside biosynthesis in Panax ginseng
    • Han JY, Hwang HS, Choi SW, Kim HJ, Choi YE. 2012. Cytochrome P450 CYP716A53v2 catalyzes the formation of protopanaxatriol from protopanaxadiol during ginsenoside biosynthesis in Panax ginseng. Plant Cell Physiol. 53:1535-45
    • (2012) Plant Cell Physiol. , vol.53 , pp. 1535-1545
    • Han, J.Y.1    Hwang, H.S.2    Choi, S.W.3    Kim, H.J.4    Choi, Y.E.5
  • 38
    • 83255165496 scopus 로고    scopus 로고
    • The Cyt P450 enzyme CYP716A47 catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis in Panax ginseng
    • Han JY, Kim HJ, Kwon YS, Choi YE. 2011. The Cyt P450 enzyme CYP716A47 catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis in Panax ginseng. Plant Cell Physiol. 52:2062-73
    • (2011) Plant Cell Physiol. , vol.52 , pp. 2062-2073
    • Han, J.Y.1    Kim, H.J.2    Kwon, Y.S.3    Choi, Y.E.4
  • 39
    • 0042322325 scopus 로고    scopus 로고
    • The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor
    • Hansen KS, Kristensen C, Tattersall DB, Jones PR, Olsen CE, et al. 2003. The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor. Phytochemistry 64:143-51
    • (2003) Phytochemistry , vol.64 , pp. 143-151
    • Hansen, K.S.1    Kristensen, C.2    Tattersall, D.B.3    Jones, P.R.4    Olsen, C.E.5
  • 40
    • 0035818591 scopus 로고    scopus 로고
    • A new class of oxidosqualene cyclases directs synthesis of antimicrobial phytoprotectants in monocots
    • Haralampidis K, Bryan G, Qi X, Papadopoulou K, Bakht S, et al. 2001. A new class of oxidosqualene cyclases directs synthesis of antimicrobial phytoprotectants in monocots. Proc. Natl. Acad. Sci. USA 98:13431-36
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13431-13436
    • Haralampidis, K.1    Bryan, G.2    Qi, X.3    Papadopoulou, K.4    Bakht, S.5
  • 41
    • 0347297340 scopus 로고    scopus 로고
    • Chemical composition and ultrastructure of broad bean (Vicia faba L.) nodule endodermis in comparison to the root endodermis
    • Hartmann K, Peiter E, Koch K, Schubert S, Schreiber L. 2002. Chemical composition and ultrastructure of broad bean (Vicia faba L.) nodule endodermis in comparison to the root endodermis. Planta 215:14-25
    • (2002) Planta , vol.215 , pp. 14-25
    • Hartmann, K.1    Peiter, E.2    Koch, K.3    Schubert, S.4    Schreiber, L.5
  • 42
    • 0000566197 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA encoding cycloartenol synthase from Luffa cylindrica
    • Hayashi H, Hiraoka N, Ikeshiro Y, Yazaki K, Tanaka S, et al. 1999. Molecular cloning of a cDNA encoding cycloartenol synthase from Luffa cylindrica. Plant Physiol. 121:1384
    • (1999) Plant Physiol. , vol.121 , pp. 1384
    • Hayashi, H.1    Hiraoka, N.2    Ikeshiro, Y.3    Yazaki, K.4    Tanaka, S.5
  • 43
    • 0035213336 scopus 로고    scopus 로고
    • Molecular cloning and characterization of isomultiflorenol synthase, a new triterpene synthase from Luffa cylindrica, involved in biosynthesis of bryonolic acid
    • Hayashi H, Huang P, Inoue K, Hiraoka N, Ikeshiro Y, et al. 2001. Molecular cloning and characterization of isomultiflorenol synthase, a new triterpene synthase from Luffa cylindrica, involved in biosynthesis of bryonolic acid. Eur. J. Biochem. 268:6311-17
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6311-6317
    • Hayashi, H.1    Huang, P.2    Inoue, K.3    Hiraoka, N.4    Ikeshiro, Y.5
  • 44
    • 0034862884 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding β-amyrin synthase involved in glycyrrhizin and soyasaponin biosyntheses in licorice
    • Hayashi H, Huang P, Kirakosyan A, Inoue K, Hiraoka N, et al. 2001. Cloning and characterization of a cDNA encoding β-amyrin synthase involved in glycyrrhizin and soyasaponin biosyntheses in licorice. Biol. Pharm. Bull. 24:912-16
    • (2001) Biol. Pharm. Bull. , vol.24 , pp. 912-916
    • Hayashi, H.1    Huang, P.2    Kirakosyan, A.3    Inoue, K.4    Hiraoka, N.5
  • 45
    • 16644392005 scopus 로고    scopus 로고
    • Differential expression of three oxidosqualene cyclase mRNAs in Glycyrrhiza glabra
    • Hayashi H, Huang P, Takada S, Obinata M, Inoue K, et al. 2004. Differential expression of three oxidosqualene cyclase mRNAs in Glycyrrhiza glabra. Biol. Pharm. Bull. 27:1086-92
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 1086-1092
    • Hayashi, H.1    Huang, P.2    Takada, S.3    Obinata, M.4    Inoue, K.5
  • 46
    • 0032399269 scopus 로고    scopus 로고
    • Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene
    • Herrera JBR, Bartel B, Wilson WK, Matsuda SPT. 1998. Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene. Phytochemistry 49:1905-11
    • (1998) Phytochemistry , vol.49 , pp. 1905-1911
    • Herrera, J.B.R.1    Bartel, B.2    Wilson, W.K.3    Matsuda, S.P.T.4
  • 48
    • 58749109023 scopus 로고    scopus 로고
    • Genevestigator V3: A reference expression database for the meta-analysis of transcriptomes
    • Hruz T, Laule O, Szabo G, Wessendorp F, Bleuler S, et al. 2008. Genevestigator V3: a reference expression database for the meta-analysis of transcriptomes. Adv. Bioinforma. 2008:420747
    • (2008) Adv. Bioinforma. , vol.2008 , pp. 420747
    • Hruz, T.1    Laule, O.2    Szabo, G.3    Wessendorp, F.4    Bleuler, S.5
  • 49
    • 84868091024 scopus 로고    scopus 로고
    • Molecular characterization of the pentacyclic triterpenoid biosynthetic pathway in Catharanthus roseus
    • Huang L, Li J, Ye H, Li C, Wang H, et al. 2012. Molecular characterization of the pentacyclic triterpenoid biosynthetic pathway in Catharanthus roseus. Planta 236:1571-81
    • (2012) Planta , vol.236 , pp. 1571-1581
    • Huang, L.1    Li, J.2    Ye, H.3    Li, C.4    Wang, H.5
  • 50
    • 70649085835 scopus 로고    scopus 로고
    • The genome of the cucumber, Cucumis sativus L
    • Huang S, Li R, Zhang Z, Li L, Gu X, et al. 2009. The genome of the cucumber, Cucumis sativus L. Nat. Genet. 41:1275-81
    • (2009) Nat. Genet. , vol.41 , pp. 1275-1281
    • Huang, S.1    Li, R.2    Zhang, Z.3    Li, L.4    Gu, X.5
  • 51
    • 79953113773 scopus 로고    scopus 로고
    • Overexpression of the UGT73C6 alters brassinosteroid glucoside formation in Arabidopsis thaliana
    • Husar S, Berthiller F, Fujioka S, Rozhon W, Khan M, et al. 2011. Overexpression of the UGT73C6 alters brassinosteroid glucoside formation in Arabidopsis thaliana. BMC Plant Biol. 11:51
    • (2011) BMC Plant Biol. , vol.11 , pp. 51
    • Husar, S.1    Berthiller, F.2    Fujioka, S.3    Rozhon, W.4    Khan, M.5
  • 52
    • 0035111648 scopus 로고    scopus 로고
    • Molecular cloning and expression in yeast of 2,3-oxidosqualene- triterpenoid cyclases from Arabidopsis thaliana
    • Husselstein-Muller T, Schaller H, Benveniste P. 2001. Molecular cloning and expression in yeast of 2,3-oxidosqualene-triterpenoid cyclases from Arabidopsis thaliana. Plant Mol. Biol. 45:75-92
    • (2001) Plant Mol. Biol. , vol.45 , pp. 75-92
    • Husselstein-Muller, T.1    Schaller, H.2    Benveniste, P.3
  • 53
    • 79959822842 scopus 로고    scopus 로고
    • Investigation of the potential for triterpene synthesis in rice through genome mining and metabolic engineering
    • Inagaki Y-S, Etherington G, Geisler K, Field B, Dokarry M, et al. 2011. Investigation of the potential for triterpene synthesis in rice through genome mining and metabolic engineering. New Phytol. 191:432-48
    • (2011) New Phytol. , vol.191 , pp. 432-448
    • Inagaki, Y.-S.1    Etherington, G.2    Geisler, K.3    Field, B.4    Dokarry, M.5
  • 54
    • 84880273715 scopus 로고    scopus 로고
    • Biosynthesis of antinutritional alkaloids in solanaceous crops is mediated by clustered genes
    • Itkin M, Heinig U, Tzfadia O, Bhide AJ, Shinde S, et al. 2013. Biosynthesis of antinutritional alkaloids in solanaceous crops is mediated by clustered genes. Science 341:175-79
    • (2013) Science , vol.341 , pp. 175-179
    • Itkin, M.1    Heinig, U.2    Tzfadia, O.3    Bhide, A.J.4    Shinde, S.5
  • 55
    • 84856455729 scopus 로고    scopus 로고
    • GLYCOALKALOID METABOLISM1 is required for steroidal alkaloid glycosylation and prevention of phytotoxicity in tomato
    • Itkin M, Rogachev I, Alkan N, Rosenberg T, Malitsky S, et al. 2011. GLYCOALKALOID METABOLISM1 is required for steroidal alkaloid glycosylation and prevention of phytotoxicity in tomato. Plant Cell 23:4507-25
    • (2011) Plant Cell , vol.23 , pp. 4507-4525
    • Itkin, M.1    Rogachev, I.2    Alkan, N.3    Rosenberg, T.4    Malitsky, S.5
  • 56
    • 79956071488 scopus 로고    scopus 로고
    • Triterpene cyclases from Oryza sativa L.: Cycloartenol, parkeol and achilleol B synthases
    • Ito R, Mori K, Hashimoto I, Nakano C, Sato T, Hoshino T. 2011. Triterpene cyclases from Oryza sativa L.: cycloartenol, parkeol and achilleol B synthases. Org. Lett. 13:2678-81
    • (2011) Org. Lett. , vol.13 , pp. 2678-2681
    • Ito, R.1    Mori, K.2    Hashimoto, I.3    Nakano, C.4    Sato, T.5    Hoshino, T.6
  • 57
    • 0037356157 scopus 로고    scopus 로고
    • Molecular cloning and characterization of triterpene synthases from Medicago truncatula and Lotus japonicus
    • Iturbe-Ormaetxe I, Haralampidis K, Papadopoulou K, Osbourn AE. 2003. Molecular cloning and characterization of triterpene synthases from Medicago truncatula and Lotus japonicus. Plant Mol. Biol. 51:731-43
    • (2003) Plant Mol. Biol. , vol.51 , pp. 731-743
    • Iturbe-Ormaetxe, I.1    Haralampidis, K.2    Papadopoulou, K.3    Osbourn, A.E.4
  • 58
    • 78951490648 scopus 로고    scopus 로고
    • Chemical composition and microstructure of waxy plant surfaces: Triterpenoids and fatty acid derivatives on leaves of Kalanchoe daigremontiana
    • Jetter R, Sodhi R. 2011. Chemical composition and microstructure of waxy plant surfaces: triterpenoids and fatty acid derivatives on leaves of Kalanchoe daigremontiana. Surf. Interface Anal. 43:326-30
    • (2011) Surf. Interface Anal. , vol.43 , pp. 326-330
    • Jetter, R.1    Sodhi, R.2
  • 59
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM. 1992. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8:275-82
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 60
    • 23144460921 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding β-amyrin synthase from petroleum plant Euphorbia tirucalli L
    • Kajikawa M, Yamato KT, Fukuzawa H, Sakai Y, Uchida H, Ohyama K. 2005. Cloning and characterization of a cDNA encoding β-amyrin synthase from petroleum plant Euphorbia tirucalli L. Phytochemistry 66:1759-66
    • (2005) Phytochemistry , vol.66 , pp. 1759-1766
    • Kajikawa, M.1    Yamato, K.T.2    Fukuzawa, H.3    Sakai, Y.4    Uchida, H.5    Ohyama, K.6
  • 61
    • 0036549820 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of cDNAs encoding oxidosqualene cyclases from Costus speciosus
    • Kawano N, Ichinose K, Ebizuka Y. 2002. Molecular cloning and functional expression of cDNAs encoding oxidosqualene cyclases from Costus speciosus. Biol. Pharm. Bull. 25:477-82
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 477-482
    • Kawano, N.1    Ichinose, K.2    Ebizuka, Y.3
  • 62
    • 41549107616 scopus 로고    scopus 로고
    • Engineering triterpene production in Saccharomyces cerevisiae β-amyrin synthase from Artemisia annua
    • Kirby J, Romanini DW, Paradise EM, Keasling JD. 2008. Engineering triterpene production in Saccharomyces cerevisiae β-amyrin synthase from Artemisia annua. FEBS J. 275:1852-59
    • (2008) FEBS J. , vol.275 , pp. 1852-1859
    • Kirby, J.1    Romanini, D.W.2    Paradise, E.M.3    Keasling, J.D.4
  • 63
    • 84864510955 scopus 로고    scopus 로고
    • Making newmolecules-evolution of pathways for novel metabolites in plants
    • Kliebenstein DJ, Osbourn A. 2012. Making newmolecules-evolution of pathways for novel metabolites in plants. Curr. Opin. Plant Biol. 15:415-23
    • (2012) Curr. Opin. Plant Biol. , vol.15 , pp. 415-423
    • Kliebenstein, D.J.1    Osbourn, A.2
  • 64
    • 17744386028 scopus 로고    scopus 로고
    • A novel glucosyltransferase involved in steroid saponin biosynthesis in Solanum aculeatissimum
    • Kohara A, Nakajima C, Hashimoto K, Ikenaga T, Tanaka H, et al. 2005. A novel glucosyltransferase involved in steroid saponin biosynthesis in Solanum aculeatissimum. Plant Mol. Biol. 57:225-39
    • (2005) Plant Mol. Biol. , vol.57 , pp. 225-239
    • Kohara, A.1    Nakajima, C.2    Hashimoto, K.3    Ikenaga, T.4    Tanaka, H.5
  • 65
    • 33846815083 scopus 로고    scopus 로고
    • Characterization and engineering of glycosyltransferases responsible for steroid saponin biosynthesis in solanaceous plants
    • Kohara A, Nakajima C, Yoshida S, Muranaka T. 2007. Characterization and engineering of glycosyltransferases responsible for steroid saponin biosynthesis in solanaceous plants. Phytochemistry 68:478-86
    • (2007) Phytochemistry , vol.68 , pp. 478-486
    • Kohara, A.1    Nakajima, C.2    Yoshida, S.3    Muranaka, T.4
  • 69
    • 84885433874 scopus 로고    scopus 로고
    • A metabolic gene cluster in Lotus japonicus discloses novel enzyme functions and products in triterpene biosynthesis
    • Krokida A, Delis C, Geisler K, Garagounis C, Tsikou D, et al. 2013. A metabolic gene cluster in Lotus japonicus discloses novel enzyme functions and products in triterpene biosynthesis. New Phytol. 200:675-90
    • (2013) New Phytol. , vol.200 , pp. 675-690
    • Krokida, A.1    Delis, C.2    Geisler, K.3    Garagounis, C.4    Tsikou, D.5
  • 70
    • 84861208439 scopus 로고    scopus 로고
    • β-Amyrin oxidation by oat CYP51H10 expressed heterologously in yeast cells: The first example of CYP51-dependent metabolism other than the 14-demethylation of sterol precursors
    • Kunii M, Kitahama Y, Fukushima EO, Seki H, Muranaka T, et al. 2012. β-Amyrin oxidation by oat CYP51H10 expressed heterologously in yeast cells: the first example of CYP51-dependent metabolism other than the 14-demethylation of sterol precursors. Biol. Pharm. Bull. 35:801-4
    • (2012) Biol. Pharm. Bull. , vol.35 , pp. 801-804
    • Kunii, M.1    Kitahama, Y.2    Fukushima, E.O.3    Seki, H.4    Muranaka, T.5
  • 71
    • 0032529028 scopus 로고    scopus 로고
    • β-Amyrin synthase: Cloning of the oxidosqualene cyclase that catalyzes the formation of the most popular triterpene among higher plants
    • Kushiro T, Shibuya M, Ebizuka Y. 1998. β-Amyrin synthase: cloning of the oxidosqualene cyclase that catalyzes the formation of the most popular triterpene among higher plants. Eur. J. Biochem. 256:238-44
    • (1998) Eur. J. Biochem. , vol.256 , pp. 238-244
    • Kushiro, T.1    Shibuya, M.2    Ebizuka, Y.3
  • 72
    • 0034718068 scopus 로고    scopus 로고
    • Mutational studies on triterpene synthases: Engineering lupeol synthase into β-amyrin synthase
    • Kushiro T, Shibuya M, Masuda K, Ebizuka Y. 2000. Mutational studies on triterpene synthases: engineering lupeol synthase into β-amyrin synthase. J. Am. Chem. Soc. 122:6816-24
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6816-6824
    • Kushiro, T.1    Shibuya, M.2    Masuda, K.3    Ebizuka, Y.4
  • 73
    • 0034734610 scopus 로고    scopus 로고
    • A novel multifunctional triterpene synthase from Arabidopsis thaliana
    • Kushiro T, Shibuya M, Masuda K, Ebizuka Y. 2000. A novel multifunctional triterpene synthase from Arabidopsis thaliana. Tetrahedron Lett. 41:7705-10
    • (2000) Tetrahedron Lett. , vol.41 , pp. 7705-7710
    • Kushiro, T.1    Shibuya, M.2    Masuda, K.3    Ebizuka, Y.4
  • 74
    • 71049135626 scopus 로고    scopus 로고
    • Identification of defense compounds in Barbarea vulgaris against the herbivore Phyllotreta nemorum by an ecometabolomic approach
    • Kuzina V, Ekstrøm CT, Andersen SB, Nielsen JK, Olsen CE, et al. 2009. Identification of defense compounds in Barbarea vulgaris against the herbivore Phyllotreta nemorum by an ecometabolomic approach. Plant Physiol. 151:1077-90
    • (2009) Plant Physiol. , vol.151 , pp. 1077-1090
    • Kuzina, V.1    Ekstrøm, C.T.2    Andersen, S.B.3    Nielsen, J.K.4    Olsen, C.E.5
  • 75
    • 34547781221 scopus 로고    scopus 로고
    • Lanosterol biosynthesis in the prokaryote Methylococcus capsulatus: Insight into the evolution of sterol biosynthesis
    • Lamb DC, Jackson CJ, Warrilow AGS, Manning NJ, Kelly DE, Kelly SL. 2007. Lanosterol biosynthesis in the prokaryote Methylococcus capsulatus: insight into the evolution of sterol biosynthesis. Mol. Biol. Evol. 24:1714-21
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1714-1721
    • Lamb, D.C.1    Jackson, C.J.2    Warrilow, A.G.S.3    Manning, N.J.4    Kelly, D.E.5    Kelly, S.L.6
  • 76
    • 26844446540 scopus 로고    scopus 로고
    • Enzyme redesign: Two mutations cooperate to convert cycloartenol synthase into an accurate lanosterol synthase
    • Lodeiro S, Schulz-Gasch T, Matsuda SPT. 2005. Enzyme redesign: two mutations cooperate to convert cycloartenol synthase into an accurate lanosterol synthase. J. Am. Chem. Soc. 127:14132-33
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14132-14133
    • Lodeiro, S.1    Schulz-Gasch, T.2    Matsuda, S.P.T.3
  • 77
    • 34548757971 scopus 로고    scopus 로고
    • An oxidosqualene cyclasemakes numerous products by diverse mechanisms: A challenge to prevailing concepts of triterpene biosynthesis
    • Lodeiro S, Xiong Q, Wilson WK, Kolesnikova MD, Onak CS, Matsuda SPT. 2007. An oxidosqualene cyclasemakes numerous products by diverse mechanisms: a challenge to prevailing concepts of triterpene biosynthesis. J. Am. Chem. Soc. 129:11213-22
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11213-11222
    • Lodeiro, S.1    Xiong, Q.2    Wilson, W.K.3    Kolesnikova, M.D.4    Onak, C.S.5    Matsuda, S.P.T.6
  • 78
    • 0001967059 scopus 로고    scopus 로고
    • Chemical composition of the slippery epicuticular wax blooms on Macaranga (Euphorbiaceae) ant-plants
    • Markstadter C, Federle W, Jetter R, Riederer M, Holldobler B. 2000. Chemical composition of the slippery epicuticular wax blooms on Macaranga (Euphorbiaceae) ant-plants. Chemoecology 10:33-40
    • (2000) Chemoecology , vol.10 , pp. 33-40
    • Markstadter, C.1    Federle, W.2    Jetter, R.3    Riederer, M.4    Holldobler, B.5
  • 79
    • 34247267753 scopus 로고    scopus 로고
    • Saponin biosynthesis in Saponaria vaccaria. CDNAs encoding β-amyrin synthase and a triterpene carboxylic acid glucosyltransferase
    • Meesapyodsuk D, Balsevich J, Reed DW, Covello PS. 2007. Saponin biosynthesis in Saponaria vaccaria. cDNAs encoding β-amyrin synthase and a triterpene carboxylic acid glucosyltransferase. Plant Physiol. 143:959-69
    • (2007) Plant Physiol. , vol.143 , pp. 959-969
    • Meesapyodsuk, D.1    Balsevich, J.2    Reed, D.W.3    Covello, P.S.4
  • 80
    • 35348896591 scopus 로고    scopus 로고
    • The chlamydomonas genome reveals the evolution of key animal and plant functions
    • Merchant SS, Prochnik SE, Vallon O, Harris EH, Karpowicz SJ, et al. 2007. The Chlamydomonas genome reveals the evolution of key animal and plant functions. Science 318:245-50
    • (2007) Science , vol.318 , pp. 245-250
    • Merchant, S.S.1    Prochnik, S.E.2    Vallon, O.3    Harris, E.H.4    Karpowicz, S.J.5
  • 81
    • 1542297375 scopus 로고    scopus 로고
    • Serine carboxypeptidase-like acyltransferases
    • Milkowski C, Strack D. 2004. Serine carboxypeptidase-like acyltransferases. Phytochemical 65:517-24
    • (2004) Phytochemical , vol.65 , pp. 517-524
    • Milkowski, C.1    Strack, D.2
  • 82
    • 84861900283 scopus 로고    scopus 로고
    • The 50th anniversary and new horizons of cytochrome P450 research: Expanding knowledge on the multiplicity and versatility of P450 and its industrial applications
    • Mizutani M. 2012. The 50th anniversary and new horizons of cytochrome P450 research: expanding knowledge on the multiplicity and versatility of P450 and its industrial applications. Biol. Pharm. Bull. 35:824-32
    • (2012) Biol. Pharm. Bull. , vol.35 , pp. 824-832
    • Mizutani, M.1
  • 83
    • 0031079999 scopus 로고    scopus 로고
    • Cloning and expression of solanidine UDPglucose glucosyltransferase from potato
    • Moehs CP, Allen PV, Friedman M, Belknap WR. 1997. Cloning and expression of solanidine UDPglucose glucosyltransferase from potato. Plant J. 11:227-36
    • (1997) Plant J. , vol.11 , pp. 227-236
    • Moehs, C.P.1    Allen, P.V.2    Friedman, M.3    Belknap, W.R.4
  • 84
    • 33749529751 scopus 로고    scopus 로고
    • Cation-π interaction in the polyolefin cyclization cascade uncovered by incorporating unnatural amino acids into the catalytic sites of squalene cyclase
    • Morikubo N, Fukuda Y, Ohtake K, Shinya N, Kiga D, et al. 2006. Cation-π interaction in the polyolefin cyclization cascade uncovered by incorporating unnatural amino acids into the catalytic sites of squalene cyclase. J. Am. Chem. Soc. 128:13184-94
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13184-13194
    • Morikubo, N.1    Fukuda, Y.2    Ohtake, K.3    Shinya, N.4    Kiga, D.5
  • 85
    • 0001031993 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of triterpene synthases from pea (Pisum sativum): New α-amyrin-producing enzyme is a multifunctional triterpene synthase
    • Morita M, Shibuya M, Kushiro T, Masuda K, Ebizuka Y. 2000. Molecular cloning and functional expression of triterpene synthases from pea (Pisum sativum): new α-amyrin-producing enzyme is a multifunctional triterpene synthase. Eur. J. Biochem. 267:3453-60
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3453-3460
    • Morita, M.1    Shibuya, M.2    Kushiro, T.3    Masuda, K.4    Ebizuka, Y.5
  • 86
    • 0030737556 scopus 로고    scopus 로고
    • Molecular cloning of pea cDNA encoding cycloartenol synthase and its functional expression in yeast
    • Morita M, Shibuya M, Lee MS, Sankawa U, Ebizuka Y. 1997. Molecular cloning of pea cDNA encoding cycloartenol synthase and its functional expression in yeast. Biol. Pharm. Bull. 20:770-75
    • (1997) Biol. Pharm. Bull. , vol.20 , pp. 770-775
    • Morita, M.1    Shibuya, M.2    Lee, M.S.3    Sankawa, U.4    Ebizuka, Y.5
  • 87
    • 67149126750 scopus 로고    scopus 로고
    • Product profile of PEN3: The last unexamined oxidosqualene cyclase in Arabidopsis thaliana
    • Morlacchi P, Wilson WK, Xiong Q, Bhaduri A, Sttivend D, et al. 2009. Product profile of PEN3: the last unexamined oxidosqualene cyclase in Arabidopsis thaliana. Org. Lett. 11:2627-30
    • (2009) Org. Lett. , vol.11 , pp. 2627-2630
    • Morlacchi, P.1    Wilson, W.K.2    Xiong, Q.3    Bhaduri, A.4    Sttivend, D.5
  • 88
    • 84883054025 scopus 로고    scopus 로고
    • Bioengineering of plant (tri)terpenoids: From metabolic engineering of plants to synthetic biology in vivo and in vitro
    • Moses T, Pollier J, Thevelein JM, Goossens A. 2013. Bioengineering of plant (tri)terpenoids: from metabolic engineering of plants to synthetic biology in vivo and in vitro. New Phytol. 200:27-43
    • (2013) New Phytol. , vol.200 , pp. 27-43
    • Moses, T.1    Pollier, J.2    Thevelein, J.M.3    Goossens, A.4
  • 89
    • 84876778902 scopus 로고    scopus 로고
    • Modularity of plant metabolic gene clusters: A trio of linked genes that are collectively required for acylation of triterpenes in oat
    • Mugford ST, Louveau T, Melton R, Qi X, Bakht S, et al. 2013. Modularity of plant metabolic gene clusters: a trio of linked genes that are collectively required for acylation of triterpenes in oat. Plant Cell 25:1078-92
    • (2013) Plant Cell , vol.25 , pp. 1078-1092
    • Mugford, S.T.1    Louveau, T.2    Melton, R.3    Qi, X.4    Bakht, S.5
  • 90
    • 84866972572 scopus 로고    scopus 로고
    • Serine carboxypeptidase-like acyltransferases from plants
    • Mugford ST, Milkowski C. 2012. Serine carboxypeptidase-like acyltransferases from plants. Methods Enzymol. 516:279-97
    • (2012) Methods Enzymol. , vol.516 , pp. 279-297
    • Mugford, S.T.1    Milkowski, C.2
  • 91
    • 77956646584 scopus 로고    scopus 로고
    • Evolution of serine carboxypeptidase-like acyl transferases in the monocots
    • Mugford ST, Osbourn A. 2010. Evolution of serine carboxypeptidase-like acyl transferases in the monocots. Plant Signal. Behav. 5:193-95
    • (2010) Plant Signal. Behav. , vol.5 , pp. 193-195
    • Mugford, S.T.1    Osbourn, A.2
  • 92
    • 70349678827 scopus 로고    scopus 로고
    • A serine carboxypeptidase-like acyltransferase is required for synthesis of antimicrobial compounds and disease resistance in oats
    • Mugford ST, Qi X, Bakht S, Hill L, Wegel E, et al. 2009. A serine carboxypeptidase-like acyltransferase is required for synthesis of antimicrobial compounds and disease resistance in oats. Plant Cell 21:2473-84
    • (2009) Plant Cell , vol.21 , pp. 2473-2484
    • Mugford, S.T.1    Qi, X.2    Bakht, S.3    Hill, L.4    Wegel, E.5
  • 93
    • 42549107196 scopus 로고    scopus 로고
    • Sad3 and Sad4 are required for saponin biosynthesis and root development in oat
    • Mylona P, Owatworakit A, Papadopoulou K, Jenner H, Qin B, et al. 2008. Sad3 and Sad4 are required for saponin biosynthesis and root development in oat. Plant Cell 20:201-12
    • (2008) Plant Cell , vol.20 , pp. 201-212
    • Mylona, P.1    Owatworakit, A.2    Papadopoulou, K.3    Jenner, H.4    Qin, B.5
  • 94
    • 77953200019 scopus 로고    scopus 로고
    • Genomic and coexpression analyses predict multiple genes involved in triterpene saponin biosynthesis in Medicago truncatula
    • Naoumkina MA, Modolo LV, Huhman DV, Urbanczyk-Wochniak E, Tang Y, et al. 2010. Genomic and coexpression analyses predict multiple genes involved in triterpene saponin biosynthesis in Medicago truncatula. Plant Cell 22:850-66
    • (2010) Plant Cell , vol.22 , pp. 850-866
    • Naoumkina, M.A.1    Modolo, L.V.2    Huhman, D.V.3    Urbanczyk-Wochniak, E.4    Tang, Y.5
  • 95
    • 79953234390 scopus 로고    scopus 로고
    • A P450-centric view of plant evolution
    • Nelson D, Werck-Reichhart D. 2011. A P450-centric view of plant evolution. Plant J. 66:194-211
    • (2011) Plant J. , vol.66 , pp. 194-211
    • Nelson, D.1    Werck-Reichhart, D.2
  • 96
    • 0141927428 scopus 로고    scopus 로고
    • Antioxidant activity of compounds from themedicinal herb Aster tataricus
    • Ng TB, Liu F, Lu Y, Cheng CHK, Wang Z. 2003. Antioxidant activity of compounds from themedicinal herb Aster tataricus. Comp. Biochem. Physiol. C 136:109-15
    • (2003) Comp. Biochem. Physiol. C , vol.136 , pp. 109-115
    • Ng, T.B.1    Liu, F.2    Lu, Y.3    Cheng, C.H.K.4    Wang, Z.5
  • 97
    • 58849148672 scopus 로고    scopus 로고
    • Dual biosynthetic pathways to phytosterol via cyclartenol and lanosterol in Arabidopsis
    • Ohyama K, Suzuki M, Kikuchi J, Saito K, Maranaka T. 2009. Dual biosynthetic pathways to phytosterol via cyclartenol and lanosterol in Arabidopsis. Proc. Natl. Acad. Sci. USA 106:725-30
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 725-730
    • Ohyama, K.1    Suzuki, M.2    Kikuchi, J.3    Saito, K.4    Maranaka, T.5
  • 98
    • 84856158159 scopus 로고    scopus 로고
    • Terpene biosynthesis: Modularity rules
    • Oldfield E, Lin FY. 2012. Terpene biosynthesis: modularity rules. Angew. Chem. 51:1124-37
    • (2012) Angew. Chem. , vol.51 , pp. 1124-1137
    • Oldfield, E.1    Lin, F.Y.2
  • 99
    • 80052059686 scopus 로고    scopus 로고
    • The saponins-polar isoprenoids with important and diverse biological activities
    • Osbourn A, Goss RJM, Field RA. 2011. The saponins-polar isoprenoids with important and diverse biological activities. Nat. Prod. Rep. 28:1261-68
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 1261-1268
    • Osbourn, A.1    Goss, R.J.M.2    Field, R.A.3
  • 101
    • 11944267083 scopus 로고
    • Hopanoids. 1. Geohopanoids-The most abundant natural products on Earth
    • Ourisson G, Albrecht P. 1992. Hopanoids. 1. Geohopanoids-the most abundant natural products on Earth. Acc. Chem. Res. 25:398-402
    • (1992) Acc. Chem. Res. , vol.25 , pp. 398-402
    • Ourisson, G.1    Albrecht, P.2
  • 102
    • 84873622194 scopus 로고    scopus 로고
    • Glycosyltransferases from oat (Avena) implicated in the acylation of avenacins
    • Owatworakit A, Townsend B, Louveau T, Jenner J, Rejzek M, et al. 2013. Glycosyltransferases from oat (Avena) implicated in the acylation of avenacins. J. Biol. Chem. 288:3696-704
    • (2013) J. Biol. Chem. , vol.288 , pp. 3696-3704
    • Owatworakit, A.1    Townsend, B.2    Louveau, T.3    Jenner, J.4    Rejzek, M.5
  • 107
    • 2542634233 scopus 로고    scopus 로고
    • A gene cluster for secondary metabolism in oat: Implications for the evolution of metabolic diversity in plants
    • Qi X, Bakht S, Leggett M, Maxwell C, Melton R, Osbourn A. 2004. A gene cluster for secondary metabolism in oat: implications for the evolution of metabolic diversity in plants. Proc. Natl. Acad. Sci. USA 101:8233-38
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8233-8238
    • Qi, X.1    Bakht, S.2    Leggett, M.3    Maxwell, C.4    Melton, R.5    Osbourn, A.6
  • 108
    • 33845497658 scopus 로고    scopus 로고
    • A different function for a member of an ancient and highly conserved cytochrome P450 family: From essential sterols to plant defense
    • Qi X, Bakht S, Qin B, Leggett M, Hemmings A, et al. 2006. A different function for a member of an ancient and highly conserved cytochrome P450 family: from essential sterols to plant defense. Proc. Natl. Acad. Sci. USA 103:18848-53
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18848-18853
    • Qi, X.1    Bakht, S.2    Qin, B.3    Leggett, M.4    Hemmings, A.5
  • 109
    • 84863784511 scopus 로고    scopus 로고
    • The triterpene cyclase protein family: A systematic analysis
    • Racolta S, Juhl PB, Sirim D, Pleiss J. 2012. The triterpene cyclase protein family: a systematic analysis. Proteins 80:2009-19
    • (2012) Proteins , vol.80 , pp. 2009-2019
    • Racolta, S.1    Juhl, P.B.2    Sirim, D.3    Pleiss, J.4
  • 110
    • 1142281936 scopus 로고    scopus 로고
    • Conversion of squalene to the pentacarbocyclic hopene
    • Reinert DJ, Balliano G, Schulz GE. 2004. Conversion of squalene to the pentacarbocyclic hopene. Chem. Biol. 11:121-26
    • (2004) Chem. Biol. , vol.11 , pp. 121-126
    • Reinert, D.J.1    Balliano, G.2    Schulz, G.E.3
  • 111
    • 0025230340 scopus 로고
    • Enzymic reaction selectivity by negative catalysis or how do enzymes deal with highly reactive intermediates?
    • Rétey R. 1990. Enzymic reaction selectivity by negative catalysis or how do enzymes deal with highly reactive intermediates? Angew. Chem. Int. Ed. 29:355-61
    • (1990) Angew. Chem. Int. Ed. , vol.29 , pp. 355-361
    • Rétey, R.1
  • 113
    • 57749107463 scopus 로고    scopus 로고
    • Extremely high-level and rapid transient protein production in plants without the use of viral replication
    • Sainsbury F, Lomonossoff GP. 2008. Extremely high-level and rapid transient protein production in plants without the use of viral replication. Plant Physiol. 148:1212-18
    • (2008) Plant Physiol. , vol.148 , pp. 1212-1218
    • Sainsbury, F.1    Lomonossoff, G.P.2
  • 114
    • 78649720518 scopus 로고    scopus 로고
    • Rapid transient production in plants by replicating and non-replicating vectors yields high quality functional anti-HIV antibody
    • Sainsbury F, Sack M, Stadlmann J, Quendler H, Fischer R, et al. 2010. Rapid transient production in plants by replicating and non-replicating vectors yields high quality functional anti-HIV antibody. PLoS ONE 5:e13976
    • (2010) PLoS ONE , vol.5
    • Sainsbury, F.1    Sack, M.2    Stadlmann, J.3    Quendler, H.4    Fischer, R.5
  • 115
    • 84867660063 scopus 로고    scopus 로고
    • Using a virus-derived system to manipulate plant natural product biosynthetic pathways
    • Sainsbury F, Saxena P, Geisler K, Osbourn A, Lomonossoff G. 2012. Using a virus-derived system to manipulate plant natural product biosynthetic pathways. Methods Enzymol. 517:185-202
    • (2012) Methods Enzymol. , vol.517 , pp. 185-202
    • Sainsbury, F.1    Saxena, P.2    Geisler, K.3    Osbourn, A.4    Lomonossoff, G.5
  • 116
    • 68849097943 scopus 로고    scopus 로고
    • PEAQ: Versatile expression vectors for easy and quick transient expression of heterologous proteins in plants
    • Sainsbury F, Thuenemann EC, Lomonossoff GP. 2009. pEAQ: versatile expression vectors for easy and quick transient expression of heterologous proteins in plants. Plant Biotechnol. J. 7:682-93
    • (2009) Plant Biotechnol. J. , vol.7 , pp. 682-693
    • Sainsbury, F.1    Thuenemann, E.C.2    Lomonossoff, G.P.3
  • 117
    • 0035489578 scopus 로고    scopus 로고
    • Catalytic function of the residues of phenylalanine and tyrosine conserved in squalene-hopene cyclases
    • Sato T, Hoshino T. 2001. Catalytic function of the residues of phenylalanine and tyrosine conserved in squalene-hopene cyclases. Biosci. Biotechnol. Biochem. 65:2233-42
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 2233-2242
    • Sato, T.1    Hoshino, T.2
  • 118
    • 33745635730 scopus 로고    scopus 로고
    • Plant lanosterol synthase: Divergence of the sterol and triterpene biosynthetic pathways in eukaryotes
    • Sawai S, Akashi T, Sakurai N, Suzuki H, Shibata D, et al. 2006. Plant lanosterol synthase: divergence of the sterol and triterpene biosynthetic pathways in eukaryotes. Plant Cell Physiol. 47:673-77
    • (2006) Plant Cell Physiol. , vol.47 , pp. 673-677
    • Sawai, S.1    Akashi, T.2    Sakurai, N.3    Suzuki, H.4    Shibata, D.5
  • 119
    • 84892719565 scopus 로고    scopus 로고
    • Triterpenoid biosynthesis and engineering in plants
    • Sawai S, Saito K. 2011. Triterpenoid biosynthesis and engineering in plants. Front. Plant Sci. 2:25
    • (2011) Front. Plant Sci. , vol.2 , pp. 25
    • Sawai, S.1    Saito, K.2
  • 120
    • 29244486464 scopus 로고    scopus 로고
    • Functional and structural analysis of genes encoding oxidosqualene cyclases of Lotus japonicus
    • Sawai S, Shindo T, Sato S, Kaneko T, Tabata S, et al. 2006. Functional and structural analysis of genes encoding oxidosqualene cyclases of Lotus japonicus. Plant Sci. 170:247-57
    • (2006) Plant Sci. , vol.170 , pp. 247-257
    • Sawai, S.1    Shindo, T.2    Sato, S.3    Kaneko, T.4    Tabata, S.5
  • 121
    • 79953254244 scopus 로고    scopus 로고
    • Molecular characterization of an oxidosqualene cyclase that yields shionone, a unique tetracyclic triterpene ketone of Aster tataricus
    • Sawai S, Uchiyama H, Mizuno S, Aoki T, Akashi T, et al. 2011. Molecular characterization of an oxidosqualene cyclase that yields shionone, a unique tetracyclic triterpene ketone of Aster tataricus. FEBS Lett. 585:1031-36
    • (2011) FEBS Lett. , vol.585 , pp. 1031-1036
    • Sawai, S.1    Uchiyama, H.2    Mizuno, S.3    Aoki, T.4    Akashi, T.5
  • 122
    • 79959918556 scopus 로고    scopus 로고
    • Improved foreign gene expression in plants using a virus-encoded suppressor of RNA silencing modified to be developmentally harmless
    • Saxena P, Hsieh YC, Alvarado VY, Sainsbury F, Saunders K, et al. 2011. Improved foreign gene expression in plants using a virus-encoded suppressor of RNA silencing modified to be developmentally harmless. Plant Biotechnol. J. 9:703-12
    • (2011) Plant Biotechnol. J. , vol.9 , pp. 703-712
    • Saxena, P.1    Hsieh, Y.C.2    Alvarado, V.Y.3    Sainsbury, F.4    Saunders, K.5
  • 123
    • 84863085006 scopus 로고    scopus 로고
    • The Sg-1 glycosyltransferase locus regulates structural diversity of triterpenoid saponins of soybean
    • Sayama T, Ono E, Takagi K, Takada Y, Horikawa M, et al. 2012. The Sg-1 glycosyltransferase locus regulates structural diversity of triterpenoid saponins of soybean. Plant Cell 24:2123-38
    • (2012) Plant Cell , vol.24 , pp. 2123-2138
    • Sayama, T.1    Ono, E.2    Takagi, K.3    Takada, Y.4    Horikawa, M.5
  • 124
    • 62549137403 scopus 로고    scopus 로고
    • Methyl jasmonate induced accumulation of kalopanaxsaponin i in Nigella sativa
    • Scholz M, Lipinski M, Leupold M, Luftmann H, Harig L, et al. 2009. Methyl jasmonate induced accumulation of kalopanaxsaponin I in Nigella sativa. Phytochemistry 70:517-22
    • (2009) Phytochemistry , vol.70 , pp. 517-522
    • Scholz, M.1    Lipinski, M.2    Leupold, M.3    Luftmann, H.4    Harig, L.5
  • 125
    • 0037560988 scopus 로고    scopus 로고
    • Mutagenesis approaches to deduce structure-function relationships in terpene synthases
    • Segura MJR, Jackson BE, Matsuda SPT. 2003. Mutagenesis approaches to deduce structure-function relationships in terpene synthases. Nat. Prod. Rep. 20:304-17
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 304-317
    • Segura, M.J.R.1    Jackson, B.E.2    Matsuda, S.P.T.3
  • 126
    • 0034720899 scopus 로고    scopus 로고
    • Arabidopsis thaliana LUP1 converts oxidosqualene to multiple triterpene alcohols and a triterpene diol
    • Segura MJR, Meyer MM, Matsuda SPT. 2000. Arabidopsis thaliana LUP1 converts oxidosqualene to multiple triterpene alcohols and a triterpene diol. Org. Lett. 2:2257-59
    • (2000) Org. Lett. , vol.2 , pp. 2257-2259
    • Segura, M.J.R.1    Meyer, M.M.2    Matsuda, S.P.T.3
  • 127
    • 52949093520 scopus 로고    scopus 로고
    • Licorice β-amyrin 11-oxidase, a cytochrome P450 with a key role in the biosynthesis of the triterpene sweetener glycyrrhizin
    • Seki H, Ohyama K, Sawai S, Mizutani M, Ohnishi T, et al. 2008. Licorice β-amyrin 11-oxidase, a cytochrome P450 with a key role in the biosynthesis of the triterpene sweetener glycyrrhizin. Proc. Natl. Acad. Sci. USA 105:14204-9
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14204-14209
    • Seki, H.1    Ohyama, K.2    Sawai, S.3    Mizutani, M.4    Ohnishi, T.5
  • 128
    • 84855180697 scopus 로고    scopus 로고
    • Triterpene functional genomics in licorice for identification of CYP72A154 involved in the biosynthesis of glycyrrhizin
    • Seki H, Sawai S, Ohyama K, Mizutani M, Ohnishi T, et al. 2011. Triterpene functional genomics in licorice for identification of CYP72A154 involved in the biosynthesis of glycyrrhizin. Plant Cell 23:4112-23
    • (2011) Plant Cell , vol.23 , pp. 4112-4123
    • Seki, H.1    Sawai, S.2    Ohyama, K.3    Mizutani, M.4    Ohnishi, T.5
  • 130
    • 3242741346 scopus 로고    scopus 로고
    • Cucurbitadienol synthase, the first committed enzyme for cucurbitacin biosynthesis, is a distinct enzyme from cycloartenol synthase for phytosterol biosynthesis
    • Shibuya M, Adachi S, Ebizuka Y. 2004. Cucurbitadienol synthase, the first committed enzyme for cucurbitacin biosynthesis, is a distinct enzyme from cycloartenol synthase for phytosterol biosynthesis. Tetrahedron 60:6995-7003
    • (2004) Tetrahedron , vol.60 , pp. 6995-7003
    • Shibuya, M.1    Adachi, S.2    Ebizuka, Y.3
  • 131
    • 33644949950 scopus 로고    scopus 로고
    • Identification of β-amyrin and sophoradiol 24-hydroxylase by expressed sequence tag mining and functional expression assay
    • Shibuya M, Hoshino M, Katsube Y, Hayashi H, Kushiro T, Ebizuka Y. 2006. Identification of β-amyrin and sophoradiol 24-hydroxylase by expressed sequence tag mining and functional expression assay. FEBS J. 273:948-59
    • (2006) FEBS J. , vol.273 , pp. 948-959
    • Shibuya, M.1    Hoshino, M.2    Katsube, Y.3    Hayashi, H.4    Kushiro, T.5    Ebizuka, Y.6
  • 132
    • 57649104874 scopus 로고    scopus 로고
    • Identification of a product specific β-amyrin synthase from Arabidopsis thaliana
    • Shibuya M, Katsube Y, Otsuka M, Zhang H, Tansakul P, et al. 2009. Identification of a product specific β-amyrin synthase from Arabidopsis thaliana. Plant Physiol. Biochem. 47:26-30
    • (2009) Plant Physiol. Biochem. , vol.47 , pp. 26-30
    • Shibuya, M.1    Katsube, Y.2    Otsuka, M.3    Zhang, H.4    Tansakul, P.5
  • 133
    • 77952953046 scopus 로고    scopus 로고
    • Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin i in Glycine max
    • Shibuya M, Nishimura K, Yasuyama N, Ebizuka Y. 2010. Identification and characterization of glycosyltransferases involved in the biosynthesis of soyasaponin I in Glycine max. FEBS Lett. 584:2258-64
    • (2010) FEBS Lett. , vol.584 , pp. 2258-2264
    • Shibuya, M.1    Nishimura, K.2    Yasuyama, N.3    Ebizuka, Y.4
  • 134
    • 58149149531 scopus 로고    scopus 로고
    • Biosynthesis of baccharis oxide, a triterpene with a 3,10-oxide bridge in the A-ring
    • Shibuya M, Sagara A, Saitoh A, Kushiro T, Ebizuka Y. 2008. Biosynthesis of baccharis oxide, a triterpene with a 3,10-oxide bridge in the A-ring. Org. Lett. 10:5071-74
    • (2008) Org. Lett. , vol.10 , pp. 5071-5074
    • Shibuya, M.1    Sagara, A.2    Saitoh, A.3    Kushiro, T.4    Ebizuka, Y.5
  • 135
    • 33846786872 scopus 로고    scopus 로고
    • Origin of structural diversity in natural triterpenes: Direct synthesis of seco-triterpene skeletons by oxidosqualene cyclase
    • Shibuya M, Xiang T, Katsube Y, Otsuka M, Zhang H, Ebizuka Y. 2007. Origin of structural diversity in natural triterpenes: direct synthesis of seco-triterpene skeletons by oxidosqualene cyclase. J. Am. Chem. Soc. 129:1450-55
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1450-1455
    • Shibuya, M.1    Xiang, T.2    Katsube, Y.3    Otsuka, M.4    Zhang, H.5    Ebizuka, Y.6
  • 136
    • 0000506975 scopus 로고    scopus 로고
    • Two branches of the lupeol synthase gene in the molecular evolution of plant oxidosqualene cyclases
    • Shibuya M, Zhang H, Endo A, Shishikura K, Kushiro T, Ebizuka Y. 1999. Two branches of the lupeol synthase gene in the molecular evolution of plant oxidosqualene cyclases. Eur. J. Biochem. 266:302-7
    • (1999) Eur. J. Biochem. , vol.266 , pp. 302-307
    • Shibuya, M.1    Zhang, H.2    Endo, A.3    Shishikura, K.4    Kushiro, T.5    Ebizuka, Y.6
  • 137
    • 38049088826 scopus 로고    scopus 로고
    • Squalene cyclase and oxidosqualene cyclase from a fern
    • Shinozaki J, Shibuya M, Masuda K, Ebizuka Y. 2008. Squalene cyclase and oxidosqualene cyclase from a fern. FEBS Lett. 582:310-18
    • (2008) FEBS Lett. , vol.582 , pp. 310-318
    • Shinozaki, J.1    Shibuya, M.2    Masuda, K.3    Ebizuka, Y.4
  • 138
    • 0038482190 scopus 로고    scopus 로고
    • Biochemical characterisation of sinapoyl: Choline sinapoyltransferase, a serine carboxypeptidase-like protein that functions as an acyltransferase in plant secondary metabolism
    • Shirley AM, Chapple C. 2003. Biochemical characterisation of sinapoyl:choline sinapoyltransferase, a serine carboxypeptidase-like protein that functions as an acyltransferase in plant secondary metabolism. J. Biol. Chem. 278:19870-77
    • (2003) J. Biol. Chem. , vol.278 , pp. 19870-19877
    • Shirley, A.M.1    Chapple, C.2
  • 139
    • 33751500753 scopus 로고
    • Purification and characterization of solanidine glucosyltransferase from the potato (Solanum tuberosum)
    • Stapleton A, Allen PV, Friedman M, Belknap WR. 1991. Purification and characterization of solanidine glucosyltransferase from the potato (Solanum tuberosum). J. Agric. Food Chem. 39:1187-93
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 1187-1193
    • Stapleton, A.1    Allen, P.V.2    Friedman, M.3    Belknap, W.R.4
  • 140
    • 0036959970 scopus 로고    scopus 로고
    • A genomics approach to the early stages of triterpene saponin biosynthesis in Medicago truncatula
    • Suzuki H, Achnine L, Xu R, Matsuda SPT, Dixon RA. 2002. A genomics approach to the early stages of triterpene saponin biosynthesis in Medicago truncatula. Plant J. 32:1033-48
    • (2002) Plant J. , vol.32 , pp. 1033-1048
    • Suzuki, H.1    Achnine, L.2    Xu, R.3    Matsuda, S.P.T.4    Dixon, R.A.5
  • 142
    • 84876413596 scopus 로고    scopus 로고
    • Fruit cuticular waxes as a source of biologically active triterpenoids
    • Szakiel A, Paczkowski C, Pensec F, Bertsch C. 2012. Fruit cuticular waxes as a source of biologically active triterpenoids. Phytochem. Rev. 11:263-84
    • (2012) Phytochem. Rev. , vol.11 , pp. 263-284
    • Szakiel, A.1    Paczkowski, C.2    Pensec, F.3    Bertsch, C.4
  • 143
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, et al. 2011. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 28:2731-39
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5
  • 144
    • 33748809553 scopus 로고    scopus 로고
    • Dammarenediol-II synthase, the first dedicated enzyme for ginsenoside biosynthesis, in Panax ginseng
    • Tansakul P, Shibuya M, Kushiro T, Ebizuka Y. 2006. Dammarenediol-II synthase, the first dedicated enzyme for ginsenoside biosynthesis, in Panax ginseng. FEBS Lett. 580:5143-49
    • (2006) FEBS Lett. , vol.580 , pp. 5143-5149
    • Tansakul, P.1    Shibuya, M.2    Kushiro, T.3    Ebizuka, Y.4
  • 145
    • 8544273685 scopus 로고    scopus 로고
    • Insight into steroid scaffold formation from the structure of human oxidosqualene cyclase
    • Thoma R, Schulz-Gasch T, D'Arcy B, Benz J, Aebi J, et al. 2004. Insight into steroid scaffold formation from the structure of human oxidosqualene cyclase. Nature 432:118-22
    • (2004) Nature , vol.432 , pp. 118-122
    • Thoma, R.1    Schulz-Gasch, T.2    D'Arcy, B.3    Benz, J.4    Aebi, J.5
  • 146
    • 76149086185 scopus 로고    scopus 로고
    • Qualitative and quantitative saponin contents in five sea cucumbers from the Indian Ocean
    • van Dyck S, Gerbaux P, Flammang P. 2010. Qualitative and quantitative saponin contents in five sea cucumbers from the Indian Ocean. Mar. Drugs 8:173-89
    • (2010) Mar. Drugs , vol.8 , pp. 173-189
    • Van Dyck, S.1    Gerbaux, P.2    Flammang, P.3
  • 147
    • 33846219958 scopus 로고    scopus 로고
    • Saponins, classification and occurrence in the plant kingdom
    • Vincken J-P, Heng L, de Groot A, Gruppen H. 2007. Saponins, classification and occurrence in the plant kingdom. Phytochemistry 68:275-97
    • (2007) Phytochemistry , vol.68 , pp. 275-297
    • Vincken, J.-P.1    Heng, L.2    De Groot, A.3    Gruppen, H.4
  • 148
    • 0033799536 scopus 로고    scopus 로고
    • Glycosyltransferases in plant natural product synthesis: Characterization of a supergene family
    • Vogt T, Jones P. 2000. Glycosyltransferases in plant natural product synthesis: characterization of a supergene family. Trends Plant Sci. 5:380-86
    • (2000) Trends Plant Sci. , vol.5 , pp. 380-386
    • Vogt, T.1    Jones, P.2
  • 149
    • 78650984754 scopus 로고    scopus 로고
    • Two oxidosqualene cyclases responsible for biosynthesis of tomato fruit cuticular triterpenoids
    • Wang Z, Guhling O, Yao R, Li F, Yeats TH, et al. 2011. Two oxidosqualene cyclases responsible for biosynthesis of tomato fruit cuticular triterpenoids. Plant Physiol. 155:540-52
    • (2011) Plant Physiol. , vol.155 , pp. 540-552
    • Wang, Z.1    Guhling, O.2    Yao, R.3    Li, F.4    Yeats, T.H.5
  • 150
    • 77956918452 scopus 로고    scopus 로고
    • Cloning and characterization of oxidosqualene cyclases from Kalanchoe daigremontiana: Enzymes catalyzing up to 10 rearrangement steps yielding friedelin and other triterpenoids
    • Wang Z, Yeats T, Han H, Jetter R. 2010. Cloning and characterization of oxidosqualene cyclases from Kalanchoe daigremontiana: enzymes catalyzing up to 10 rearrangement steps yielding friedelin and other triterpenoids. J. Biol. Chem. 285:29703-12
    • (2010) J. Biol. Chem. , vol.285 , pp. 29703-29712
    • Wang, Z.1    Yeats, T.2    Han, H.3    Jetter, R.4
  • 151
    • 0031282642 scopus 로고    scopus 로고
    • UDP-glucose: Sterol glucosyltransferase: Cloning and functional expression in Escherichia coli
    • Warnecke DC, Baltrusch M, Buck F, Wolter FP, Heinz E. 1997. UDP-glucose:sterol glucosyltransferase: cloning and functional expression in Escherichia coli. Plant Mol. Biol. 35:597-603
    • (1997) Plant Mol. Biol. , vol.35 , pp. 597-603
    • Warnecke, D.C.1    Baltrusch, M.2    Buck, F.3    Wolter, F.P.4    Heinz, E.5
  • 152
    • 0027966829 scopus 로고
    • Purification of a membrane-bound UDP-glucose: Sterol β-D- glucosyltransferase based on its solubility in diethyl ether
    • Warnecke DC, Heinz E. 1994. Purification of a membrane-bound UDP-glucose: sterol β-D-glucosyltransferase based on its solubility in diethyl ether. Plant Physiol. 105:1067-73
    • (1994) Plant Physiol. , vol.105 , pp. 1067-1073
    • Warnecke, D.C.1    Heinz, E.2
  • 153
    • 21244452391 scopus 로고    scopus 로고
    • Enzyme mechanisms for triterpene cyclization: New pieces of the puzzle
    • Wendt KU. 2005. Enzyme mechanisms for triterpene cyclization: new pieces of the puzzle. Angew. Chem. Int. Ed. 44:3966-71
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 3966-3971
    • Wendt, K.U.1
  • 154
    • 0033548169 scopus 로고    scopus 로고
    • The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution
    • Wendt KU, Lenhart A, Schulz GE. 1999. The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution. J. Mol. Biol. 286:175-87
    • (1999) J. Mol. Biol. , vol.286 , pp. 175-187
    • Wendt, K.U.1    Lenhart, A.2    Schulz, G.E.3
  • 155
    • 0030769202 scopus 로고    scopus 로고
    • Structure and function of a squalene cyclase
    • Wendt KU, Poralla K, Schulz GE. 1997. Structure and function of a squalene cyclase. Science 277:1811-15
    • (1997) Science , vol.277 , pp. 1811-1815
    • Wendt, K.U.1    Poralla, K.2    Schulz, G.E.3
  • 157
    • 84862983375 scopus 로고    scopus 로고
    • A Papaver somniferum 10-gene cluster for synthesis of the anticancer alkaloid noscapine
    • Winzer T, Gazda V, He Z, Kaminski F, Kern M, et al. 2012. A Papaver somniferum 10-gene cluster for synthesis of the anticancer alkaloid noscapine. Science 336:1704-8
    • (2012) Science , vol.336 , pp. 1704-1708
    • Winzer, T.1    Gazda, V.2    He, Z.3    Kaminski, F.4    Kern, M.5
  • 158
    • 58149164757 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase: A chemistry-biology interdisciplinary study of the protein's structure-function- reaction mechanism relationships
    • Wu T-K, Chang C-H, Liu Y-T, Wang T-T. 2008. Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase: a chemistry-biology interdisciplinary study of the protein's structure-function-reaction mechanism relationships. Chem. Rec. 8:302-25
    • (2008) Chem. Rec. , vol.8 , pp. 302-325
    • Wu, T.-K.1    Chang, C.-H.2    Liu, Y.-T.3    Wang, T.-T.4
  • 159
    • 33646578835 scopus 로고    scopus 로고
    • Site-saturated mutagenesis of histidine 234 of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase demonstrates dual functions in cyclization and rearrangement reactions
    • Wu T-K, Liu Y-T, Chang C-H, Yu M-T, Wang H-J. 2006. Site-saturated mutagenesis of histidine 234 of Saccharomyces cerevisiae oxidosqualene- lanosterol cyclase demonstrates dual functions in cyclization and rearrangement reactions. J. Am. Chem. Soc. 128:6414-19
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6414-6419
    • Wu, T.-K.1    Liu, Y.-T.2    Chang, C.-H.3    Yu, M.-T.4    Wang, H.-J.5
  • 160
    • 33645924695 scopus 로고    scopus 로고
    • Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions
    • Wu T-K, Yu M-T, Liu Y-T, Chang C-H, Wang H-J, Diau EW-G. 2006. Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions. Org. Lett. 8:1319-22
    • (2006) Org. Lett. , vol.8 , pp. 1319-1322
    • Wu, T.-K.1    Yu, M.-T.2    Liu, Y.-T.3    Chang, C.-H.4    Wang, H.-J.5    Diau, E.W.-G.6
  • 161
    • 33746153480 scopus 로고    scopus 로고
    • A new triterpene synthase from Arabidopsis thaliana produces a tricyclic triterpene with two hydroxyl groups
    • Xiang T, Shibuya M, Katsube Y, Tsutsumi T, Otsuka M, et al. 2006. A new triterpene synthase from Arabidopsis thaliana produces a tricyclic triterpene with two hydroxyl groups. Org. Lett. 8:2835-38
    • (2006) Org. Lett. , vol.8 , pp. 2835-2838
    • Xiang, T.1    Shibuya, M.2    Katsube, Y.3    Tsutsumi, T.4    Otsuka, M.5
  • 162
    • 33646124608 scopus 로고    scopus 로고
    • An arabidopsis oxidosqualene cyclase catalyzes iridal skeleton formation by Grob fragmentation
    • Xiong Q, Wilson WK, Matsuda SPT. 2006. An Arabidopsis oxidosqualene cyclase catalyzes iridal skeleton formation by Grob fragmentation. Angew. Chem. Int. Ed. 45:1285-88
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 1285-1288
    • Xiong, Q.1    Wilson, W.K.2    Matsuda, S.P.T.3
  • 163
    • 0742307297 scopus 로고    scopus 로고
    • On the origins of triterpenoid skeletal diversity
    • Xu R, Fazio GC, Matsuda SPT. 2004. On the origins of triterpenoid skeletal diversity. Phytochemistry 65:261-91
    • (2004) Phytochemistry , vol.65 , pp. 261-291
    • Xu, R.1    Fazio, G.C.2    Matsuda, S.P.T.3
  • 164
    • 84856546682 scopus 로고    scopus 로고
    • Divergent evolution of oxidosqualene cyclases in plants
    • Xue Z, Duan L, Liu D, Guo J, Ge S, et al. 2012. Divergent evolution of oxidosqualene cyclases in plants. New Phytol. 193:1022-38
    • (2012) New Phytol. , vol.193 , pp. 1022-1038
    • Xue, Z.1    Duan, L.2    Liu, D.3    Guo, J.4    Ge, S.5
  • 165
    • 79953247573 scopus 로고    scopus 로고
    • An evolutionary view of functional diversity in family 1 glycosyltransferases
    • Yonekura-Sakakibara K, Hanada K. 2011. An evolutionary view of functional diversity in family 1 glycosyltransferases. Plant J. 66:182-93
    • (2011) Plant J. , vol.66 , pp. 182-193
    • Yonekura-Sakakibara, K.1    Hanada, K.2
  • 166
    • 84877986528 scopus 로고    scopus 로고
    • Functional characterization of amyrin synthase involved in ursolic acid biosynthesis in Catharanthus roseus leaf epidermis
    • Yu F, Thamm AMK, Reed D, Villa-Ruano N, Quesada AL, et al. 2013. Functional characterization of amyrin synthase involved in ursolic acid biosynthesis in Catharanthus roseus leaf epidermis. Phytochemistry 91:122-27
    • (2013) Phytochemistry , vol.91 , pp. 122-127
    • Yu, F.1    Thamm, A.M.K.2    Reed, D.3    Villa-Ruano, N.4    Quesada, A.L.5
  • 167
    • 1542649551 scopus 로고    scopus 로고
    • Oxidosqualene cyclases from cell suspension cultures of Betula platyphylla var. Japonica: Molecular evolution of oxidosqualene cyclases in higher plants
    • Zhang H, Shibuya M, Yokota S, Ebizuka Y. 2003. Oxidosqualene cyclases from cell suspension cultures of Betula platyphylla var. japonica: molecular evolution of oxidosqualene cyclases in higher plants. Biol. Pharm. Bull. 26:642-50
    • (2003) Biol. Pharm. Bull. , vol.26 , pp. 642-650
    • Zhang, H.1    Shibuya, M.2    Yokota, S.3    Ebizuka, Y.4


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