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Volumn 37, Issue C, 2003, Pages 231-251

Chapter ten The chemical wizardry of isoprenoid metabolism in plants

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EID: 34848830200     PISSN: 00799920     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-9920(03)80025-4     Document Type: Article
Times cited : (2)

References (59)
  • 1
    • 0001142042 scopus 로고
    • Secreting glandular trichomes-more than just hairs
    • Wagner G.J. Secreting glandular trichomes-more than just hairs. Plant Physiol. 96 (1991) 675-679
    • (1991) Plant Physiol. , vol.96 , pp. 675-679
    • Wagner, G.J.1
  • 3
    • 0035072835 scopus 로고    scopus 로고
    • Suppression of a P450 hydroxylase gene in plant trichome glands enhances natural-product-based aphid resistance
    • Wang E.M., Wang R., Deparasis J., Loughrin J.H., Gan S.S., and Wagner G.J. Suppression of a P450 hydroxylase gene in plant trichome glands enhances natural-product-based aphid resistance. Nature Biotech. 19 (2001) 371-374
    • (2001) Nature Biotech. , vol.19 , pp. 371-374
    • Wang, E.M.1    Wang, R.2    Deparasis, J.3    Loughrin, J.H.4    Gan, S.S.5    Wagner, G.J.6
  • 4
    • 0028593985 scopus 로고
    • Isolation of phytoalexin-deficient mutants of Arabidopsis thaliana and characterization of their interactions with bacterial pathogens
    • Glazebrook J., and Ausubel F.M. Isolation of phytoalexin-deficient mutants of Arabidopsis thaliana and characterization of their interactions with bacterial pathogens. Proc. Natl. Acad. Sci. USA 91 (1994) 8955-8959
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8955-8959
    • Glazebrook, J.1    Ausubel, F.M.2
  • 5
    • 0030458877 scopus 로고    scopus 로고
    • Transformation-mediated chromosome loss and disruption of a gene for pisatin demethylase decrease the virulence of Nectria haematococca on pea
    • Wasmann C.C., and Vanetten H.D. Transformation-mediated chromosome loss and disruption of a gene for pisatin demethylase decrease the virulence of Nectria haematococca on pea. Mol. Plant-Microbe Inter. 9 (1996) 793-803
    • (1996) Mol. Plant-Microbe Inter. , vol.9 , pp. 793-803
    • Wasmann, C.C.1    Vanetten, H.D.2
  • 6
    • 0000334309 scopus 로고
    • 2 Classes of plant antibiotics-phytoalexins versus phytoanticipins
    • Vanetten H.D., Mansfield J.W., Bailey J.A., and Farmer E.E. 2 Classes of plant antibiotics-phytoalexins versus phytoanticipins. Plant Cell 6 (1994) 1191-1192
    • (1994) Plant Cell , vol.6 , pp. 1191-1192
    • Vanetten, H.D.1    Mansfield, J.W.2    Bailey, J.A.3    Farmer, E.E.4
  • 7
    • 0028946960 scopus 로고
    • Host-range of a plant-pathogenic fungus determined by a saponin detoxifying enzyme
    • Bowyer P., Clarke B.R., Lunness P., Daniels M.J., and Osbourn A.E. Host-range of a plant-pathogenic fungus determined by a saponin detoxifying enzyme. Science 267 (1995) 371-374
    • (1995) Science , vol.267 , pp. 371-374
    • Bowyer, P.1    Clarke, B.R.2    Lunness, P.3    Daniels, M.J.4    Osbourn, A.E.5
  • 10
    • 35448991792 scopus 로고    scopus 로고
    • Emerging microtubule stabilizing agents for cancer chemotherapy
    • Myles D.C. Emerging microtubule stabilizing agents for cancer chemotherapy. Annual Reports Med. Chem. 37 (2002) 125-132
    • (2002) Annual Reports Med. Chem. , vol.37 , pp. 125-132
    • Myles, D.C.1
  • 12
    • 0031913980 scopus 로고    scopus 로고
    • New insecticides with ecdysteroidal and juvenile hormone activity
    • Dhadialla T.S., Carlson G.R., and Le D.P. New insecticides with ecdysteroidal and juvenile hormone activity. Annu. Rev. of Entomol. 43 (1998) 545-569
    • (1998) Annu. Rev. of Entomol. , vol.43 , pp. 545-569
    • Dhadialla, T.S.1    Carlson, G.R.2    Le, D.P.3
  • 13
    • 0033667684 scopus 로고    scopus 로고
    • Bitter taste, phytonutrients, and the consumer: A review
    • Drewnowski A., and Gomez-Carneros C. Bitter taste, phytonutrients, and the consumer: A review. Amer. J. Clin. Nutr. 72 (2000) 1424-1435
    • (2000) Amer. J. Clin. Nutr. , vol.72 , pp. 1424-1435
    • Drewnowski, A.1    Gomez-Carneros, C.2
  • 14
    • 0029479411 scopus 로고
    • Biotechnological investigation for the prevention of biofouling. 1. Biological and biochemical principles for the prevention of biofouling
    • Abarzua S., and Jakubowski S. Biotechnological investigation for the prevention of biofouling. 1. Biological and biochemical principles for the prevention of biofouling. Marine Ecology Prog. Series 123 (1995) 301-312
    • (1995) Marine Ecology Prog. Series , vol.123 , pp. 301-312
    • Abarzua, S.1    Jakubowski, S.2
  • 15
    • 0026798725 scopus 로고
    • The effect of lubricant additives on fretting wear
    • Qui Y., and Roylance B.J. The effect of lubricant additives on fretting wear. Lubrication Engineering 48 (1992) 801-808
    • (1992) Lubrication Engineering , vol.48 , pp. 801-808
    • Qui, Y.1    Roylance, B.J.2
  • 16
    • 0027368126 scopus 로고
    • Isoprenoid biosynthesis in bacteria-a novel pathway for the early steps leading to isopentenyl diphosphate
    • Rohmer M., Knani M., Simonin P., Sutter B., and Sahm H. Isoprenoid biosynthesis in bacteria-a novel pathway for the early steps leading to isopentenyl diphosphate. Biochem. J. 295 (1993) 517-524
    • (1993) Biochem. J. , vol.295 , pp. 517-524
    • Rohmer, M.1    Knani, M.2    Simonin, P.3    Sutter, B.4    Sahm, H.5
  • 17
    • 0029922877 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate and pyruvate as precursors of isoprenic units in an alternative non-mevalonate pathway for terpenoid biosynthesis
    • Rohmer M., Seemann M., Horbach S., Bringermeyer S., and Sahm H. Glyceraldehyde 3-phosphate and pyruvate as precursors of isoprenic units in an alternative non-mevalonate pathway for terpenoid biosynthesis. J. Amer. Chem. Soc. 118 (1996) 2564-2566
    • (1996) J. Amer. Chem. Soc. , vol.118 , pp. 2564-2566
    • Rohmer, M.1    Seemann, M.2    Horbach, S.3    Bringermeyer, S.4    Sahm, H.5
  • 18
    • 0033513375 scopus 로고    scopus 로고
    • The 1-deoxy-D-xylulose-5-phosphate pathway of isoprenoid biosynthesis in plants
    • Lichtenthaler H.K. The 1-deoxy-D-xylulose-5-phosphate pathway of isoprenoid biosynthesis in plants. Annu. Rev. Plant Physiol. Plant Mol. Bio. 50 (1999) 47-65
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Bio. , vol.50 , pp. 47-65
    • Lichtenthaler, H.K.1
  • 19
    • 0033198833 scopus 로고    scopus 로고
    • Incorporation of 1-[1-C-13]deoxy-D-xylulose in chamomile sesquiterpenes
    • Adam K.P., Thiel R., and Zapp J. Incorporation of 1-[1-C-13]deoxy-D-xylulose in chamomile sesquiterpenes. Arch. Biochem. Biophys. 369 (1999) 127-132
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 127-132
    • Adam, K.P.1    Thiel, R.2    Zapp, J.3
  • 20
    • 51249175606 scopus 로고
    • Sterol composition during the life cycle of the soybean and the squash
    • Fenner G.P., Patterson G.W., and Koines P.M. Sterol composition during the life cycle of the soybean and the squash. Lipids 21 (1986) 48-51
    • (1986) Lipids , vol.21 , pp. 48-51
    • Fenner, G.P.1    Patterson, G.W.2    Koines, P.M.3
  • 21
    • 85051489349 scopus 로고
    • Terpenoid biosynthesis: the basic pathway and formation of monoterpenes, sesquiterpenes and diterpenes
    • Moore T.S. (Ed), CRC Press, Boca Raton, FL.
    • Gershenzon J., and Croteau R. Terpenoid biosynthesis: the basic pathway and formation of monoterpenes, sesquiterpenes and diterpenes. In: Moore T.S. (Ed). Lipid Metabolism in Plants (1993), CRC Press, Boca Raton, FL. 340-388
    • (1993) Lipid Metabolism in Plants , pp. 340-388
    • Gershenzon, J.1    Croteau, R.2
  • 22
    • 0035896350 scopus 로고    scopus 로고
    • Defensive function of herbivore-induced plant volatile emissions in nature
    • Kessler A., and Baldwin I.T. Defensive function of herbivore-induced plant volatile emissions in nature. Science 291 (2001) 2141-2144
    • (2001) Science , vol.291 , pp. 2141-2144
    • Kessler, A.1    Baldwin, I.T.2
  • 23
    • 0001328602 scopus 로고
    • Induction of sesquiterpene cyclase and suppression of squalene synthetase activities in plant cell cultures treated with fungal elicitor
    • Vögeli U., and Chappell J. Induction of sesquiterpene cyclase and suppression of squalene synthetase activities in plant cell cultures treated with fungal elicitor. Plant Physiol. 88 (1988) 1291-1296
    • (1988) Plant Physiol. , vol.88 , pp. 1291-1296
    • Vögeli, U.1    Chappell, J.2
  • 24
    • 0001598604 scopus 로고
    • Purification and characterization of an inducible sesquiterpene cyclase from elicitor-treated tobacco cell suspension cultures
    • Vögeli U., Freeman J.W., and Chappell J. Purification and characterization of an inducible sesquiterpene cyclase from elicitor-treated tobacco cell suspension cultures. Plant Physiol. 93 (1989) 182-187
    • (1989) Plant Physiol. , vol.93 , pp. 182-187
    • Vögeli, U.1    Freeman, J.W.2    Chappell, J.3
  • 25
    • 0026482962 scopus 로고
    • A gene family for an elicitor-induced sesquiterpene cyclase in tobacco
    • Facchini P.J., and Chappell J. A gene family for an elicitor-induced sesquiterpene cyclase in tobacco. Proc. Natl. Acad. Sci. USA 89 (1992) 11088-11092
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11088-11092
    • Facchini, P.J.1    Chappell, J.2
  • 26
    • 0031251759 scopus 로고    scopus 로고
    • Regulation of sesquiterpene cyclase gene expression: characterization of an elicitor and pathogen inducible promoter
    • Yin S., Mei L., Newman J., Back K., and Chappell J. Regulation of sesquiterpene cyclase gene expression: characterization of an elicitor and pathogen inducible promoter. Plant Physiol. 115 (1997) 437-451
    • (1997) Plant Physiol. , vol.115 , pp. 437-451
    • Yin, S.1    Mei, L.2    Newman, J.3    Back, K.4    Chappell, J.5
  • 27
    • 0032518190 scopus 로고    scopus 로고
    • Molecular characterization of tobacco squalene synthase and regulation in response to fungal elicitor
    • Devarenne T.P., Shin D.H., Back K., Yin S., and Chappell J. Molecular characterization of tobacco squalene synthase and regulation in response to fungal elicitor. Arch. Biochem. Biophys. 349 (1998) 205-215
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 205-215
    • Devarenne, T.P.1    Shin, D.H.2    Back, K.3    Yin, S.4    Chappell, J.5
  • 28
    • 0035984066 scopus 로고    scopus 로고
    • Regulation of squalene synthase, a key enzyme of sterol biosynthesis in tobacco
    • Devarenne T.P., Ghosh A., and Chappell J. Regulation of squalene synthase, a key enzyme of sterol biosynthesis in tobacco. Plant Physiol. 129 (2002) 1095-1106
    • (2002) Plant Physiol. , vol.129 , pp. 1095-1106
    • Devarenne, T.P.1    Ghosh, A.2    Chappell, J.3
  • 30
    • 0029948274 scopus 로고    scopus 로고
    • Aristolochene synthase. Elucidation of the cryptic germacrene A synthase activity using the anomalous substrate dihydrofarnesyl diphosphate
    • Cane D.E., and Tsantrizos Y.S. Aristolochene synthase. Elucidation of the cryptic germacrene A synthase activity using the anomalous substrate dihydrofarnesyl diphosphate. J. Amer. Chem. Soc. 118 (1996) 10037-10040
    • (1996) J. Amer. Chem. Soc. , vol.118 , pp. 10037-10040
    • Cane, D.E.1    Tsantrizos, Y.S.2
  • 31
    • 0034624597 scopus 로고    scopus 로고
    • Stereochemistry of the cyclization-rearrangement of (+)-copalyl diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene synthase from Abies grandis
    • Ravn M.M., Coates R.M., Flory J.E., Peters R.J., and Croteau R. Stereochemistry of the cyclization-rearrangement of (+)-copalyl diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene synthase from Abies grandis. Org. Lett. 2 (2000) 573-576
    • (2000) Org. Lett. , vol.2 , pp. 573-576
    • Ravn, M.M.1    Coates, R.M.2    Flory, J.E.3    Peters, R.J.4    Croteau, R.5
  • 32
    • 0034620687 scopus 로고    scopus 로고
    • Demonstration of germacrene A as an intermediate in 5-epi-aristolochene synthase catalysis
    • Rising K.A., Starks C.M., Noel J.P., and Chappell J. Demonstration of germacrene A as an intermediate in 5-epi-aristolochene synthase catalysis. J. Amer. Chem. Soc. 122 (2000) 6526
    • (2000) J. Amer. Chem. Soc. , vol.122 , pp. 6526
    • Rising, K.A.1    Starks, C.M.2    Noel, J.P.3    Chappell, J.4
  • 33
    • 0035423821 scopus 로고    scopus 로고
    • Mechanism of monoterpene cyclization: Stereochemical aspects of the transformation of noncyclizable substrate analogs by recombinant (-)-limonene synthase, (+)-bornyl diphosphate synthase, and (-)-pinene synthase
    • Schwab W., Williams D.C., Davis E.M., and Croteau R. Mechanism of monoterpene cyclization: Stereochemical aspects of the transformation of noncyclizable substrate analogs by recombinant (-)-limonene synthase, (+)-bornyl diphosphate synthase, and (-)-pinene synthase. Arch. Biochem. Biophys. 392 (2001) 123-136
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 123-136
    • Schwab, W.1    Williams, D.C.2    Davis, E.M.3    Croteau, R.4
  • 34
    • 0032169258 scopus 로고    scopus 로고
    • Truncation of limonene synthase preprotein provides a fully active 'pseudomature'
    • Williams D.C., McGarvey D.J., Katahira E.J., and Croteau R. Truncation of limonene synthase preprotein provides a fully active 'pseudomature'. Biochem. 37 (1998) 12213-12220
    • (1998) Biochem. , vol.37 , pp. 12213-12220
    • Williams, D.C.1    McGarvey, D.J.2    Katahira, E.J.3    Croteau, R.4
  • 35
    • 0029956966 scopus 로고    scopus 로고
    • Identifying functional domains within terpene cyclases using a domain-swapping strategy
    • Back K.W., and Chappell J. Identifying functional domains within terpene cyclases using a domain-swapping strategy. Proc. Natl. Acad. Sci. USA 93 (1996) 6841-6845
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6841-6845
    • Back, K.W.1    Chappell, J.2
  • 36
    • 0034653496 scopus 로고    scopus 로고
    • Terpenoid secondary metabolism in Arabidopsis thaliana: cDNA cloning, characterization and functional expression of a myrcene/(E)-beta-ocimene synthase
    • Bohlmann J., Martin D., Oldham N.J., and Gershenzon J. Terpenoid secondary metabolism in Arabidopsis thaliana: cDNA cloning, characterization and functional expression of a myrcene/(E)-beta-ocimene synthase. Arch. Biochem. Biophys. 375 (2000) 261-269
    • (2000) Arch. Biochem. Biophys. , vol.375 , pp. 261-269
    • Bohlmann, J.1    Martin, D.2    Oldham, N.J.3    Gershenzon, J.4
  • 37
    • 0033567360 scopus 로고    scopus 로고
    • cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis
    • Bohlmann J., Phillips M., Ramachandiran V., Katoh S., and Croteau R. cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis. Arch. Biochem. Biophys. 368 (1999) 232-243
    • (1999) Arch. Biochem. Biophys. , vol.368 , pp. 232-243
    • Bohlmann, J.1    Phillips, M.2    Ramachandiran, V.3    Katoh, S.4    Croteau, R.5
  • 38
    • 0030845284 scopus 로고    scopus 로고
    • Monoterpene synthases from grand fir (Abies grandis)-cDNA isolation, characterization, and functional expression of myrcene synthase, (-)(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase
    • Bohlmann J., Steele C.L., and Croteau R. Monoterpene synthases from grand fir (Abies grandis)-cDNA isolation, characterization, and functional expression of myrcene synthase, (-)(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784-21792
    • (1997) J. Biol. Chem. , vol.272 , pp. 21784-21792
    • Bohlmann, J.1    Steele, C.L.2    Croteau, R.3
  • 39
    • 0034655963 scopus 로고    scopus 로고
    • Aristolochene synthase: purification, molecular cloning, high-level expression in Escherichia coli, and characterization of the Aspergillus terreus cyclase
    • Cane D.E., and Kang I. Aristolochene synthase: purification, molecular cloning, high-level expression in Escherichia coli, and characterization of the Aspergillus terreus cyclase. Arch. Biochem. Biophys. 376 (2000) 354-364
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 354-364
    • Cane, D.E.1    Kang, I.2
  • 40
    • 0030589641 scopus 로고    scopus 로고
    • High level expression of Ricinus communis casbene synthase in Escherichia coli and characterization of the recombinant enzyme
    • Hill A.M., Cane D.E., Mau C.J.D., and West C.A. High level expression of Ricinus communis casbene synthase in Escherichia coli and characterization of the recombinant enzyme. Arch. Biochem. Biophys. 336 (1996) 283-289
    • (1996) Arch. Biochem. Biophys. , vol.336 , pp. 283-289
    • Hill, A.M.1    Cane, D.E.2    Mau, C.J.D.3    West, C.A.4
  • 41
    • 0032102787 scopus 로고    scopus 로고
    • Overproduction
    • Escherichia coli, of soluble taxadiene synthase, a key enzyme in the taxol biosynthetic pathway
    • Huang E.X., Huang Q.L., Wildung M.R., Croteau R., and Scott A.I. Overproduction. Escherichia coli, of soluble taxadiene synthase, a key enzyme in the taxol biosynthetic pathway. Protein Expression Purification 13 (1998) 90-96
    • (1998) Protein Expression Purification , vol.13 , pp. 90-96
    • Huang, E.X.1    Huang, Q.L.2    Wildung, M.R.3    Croteau, R.4    Scott, A.I.5
  • 42
    • 0000828106 scopus 로고    scopus 로고
    • Abietadiene synthase from grand fir (Abies grandis)-cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase involved in resin acid biosynthesis
    • Vogel B.S., Wildung M.R., Vogel G., and Croteau R. Abietadiene synthase from grand fir (Abies grandis)-cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase involved in resin acid biosynthesis. J. Biol. Chem. 271 (1996) 23262-23268
    • (1996) J. Biol. Chem. , vol.271 , pp. 23262-23268
    • Vogel, B.S.1    Wildung, M.R.2    Vogel, G.3    Croteau, R.4
  • 43
    • 0034234699 scopus 로고    scopus 로고
    • Heterologous expression and characterization of a "pseudomature" form of taxadiene synthase involved in paclitaxel (Taxol) biosynthesis and evaluation of a potential intermediate and inhibitors of the multistep diterpene cyclization reaction
    • Williams D.C., Wildung M.R., Jin A.Q.W., Dalal D., Oliver J.S., Coates R.M., and Croteau R. Heterologous expression and characterization of a "pseudomature" form of taxadiene synthase involved in paclitaxel (Taxol) biosynthesis and evaluation of a potential intermediate and inhibitors of the multistep diterpene cyclization reaction. Arch. Biochem. Biophys. 379 (2000) 137-146
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 137-146
    • Williams, D.C.1    Wildung, M.R.2    Jin, A.Q.W.3    Dalal, D.4    Oliver, J.S.5    Coates, R.M.6    Croteau, R.7
  • 44
    • 0029797251 scopus 로고    scopus 로고
    • Trichodiene synthase. probing the role of the highly conserved aspartate-rich region by site-directed mutagenesis
    • Cane D.E., Xue Q., and Fitzsimons B.C. Trichodiene synthase. probing the role of the highly conserved aspartate-rich region by site-directed mutagenesis. Biochem. 35 (1996) 12369-12376
    • (1996) Biochem. , vol.35 , pp. 12369-12376
    • Cane, D.E.1    Xue, Q.2    Fitzsimons, B.C.3
  • 45
    • 0034682766 scopus 로고    scopus 로고
    • Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillum roqueforti
    • Caruthers J.M., Kang I., Rynkiewicz M.J., Cane D.E., and Christianson D.W. Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillum roqueforti. J. Biol. Chem. 275 (2000) 25533-25539
    • (2000) J. Biol. Chem. , vol.275 , pp. 25533-25539
    • Caruthers, J.M.1    Kang, I.2    Rynkiewicz, M.J.3    Cane, D.E.4    Christianson, D.W.5
  • 46
    • 0030777210 scopus 로고    scopus 로고
    • Crystal structure of pentalenene synthase: Mechanistic insights on terpenoid cyclization reactions in biology
    • Lesburg C.A., Zhai G.Z., Cane D.E., and Christianson D.W. Crystal structure of pentalenene synthase: Mechanistic insights on terpenoid cyclization reactions in biology. Science 277 (1997) 1820-1824
    • (1997) Science , vol.277 , pp. 1820-1824
    • Lesburg, C.A.1    Zhai, G.Z.2    Cane, D.E.3    Christianson, D.W.4
  • 47
    • 0035923697 scopus 로고    scopus 로고
    • Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade
    • Rynkiewicz M.J., Cane D.E., and Christianson D.W. Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade. Proc. Natl. Acad. Sci. USA 98 (2001) 13543-13548
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13543-13548
    • Rynkiewicz, M.J.1    Cane, D.E.2    Christianson, D.W.3
  • 48
    • 0030796451 scopus 로고    scopus 로고
    • Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase
    • Starks C.M., Back K.W., Chappell J., and Noel J.P. Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase. Science 277 (1997) 1815-1820
    • (1997) Science , vol.277 , pp. 1815-1820
    • Starks, C.M.1    Back, K.W.2    Chappell, J.3    Noel, J.P.4
  • 49
    • 0036774941 scopus 로고    scopus 로고
    • Natural sesquiterpenoids
    • Fraga B.M. Natural sesquiterpenoids. Natural Products Rep. 19 (2002) 650-672
    • (2002) Natural Products Rep. , vol.19 , pp. 650-672
    • Fraga, B.M.1
  • 50
    • 0033179201 scopus 로고    scopus 로고
    • Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha) species: cDNA isolation, characterization, and functional expression of (-)-4S-limonene-3-hydroxylase and (-)-4S-limonene-6-hydroxylase
    • Lupien S., Karp F., Wildung M., and Croteau R. Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha) species: cDNA isolation, characterization, and functional expression of (-)-4S-limonene-3-hydroxylase and (-)-4S-limonene-6-hydroxylase. Arch. Biochem. Biophys. 368 (1999) 181-192
    • (1999) Arch. Biochem. Biophys. , vol.368 , pp. 181-192
    • Lupien, S.1    Karp, F.2    Wildung, M.3    Croteau, R.4
  • 51
    • 0035264179 scopus 로고    scopus 로고
    • Hydroxylation of limonene enantiomers and analogs by recombinant (-)-limonene 3- and 6-hydroxylases from mint (Mentha) species: Evidence for catalysis within sterically constrained active sites
    • Wust M., Little D.B., Schalk M., and Croteau R. Hydroxylation of limonene enantiomers and analogs by recombinant (-)-limonene 3- and 6-hydroxylases from mint (Mentha) species: Evidence for catalysis within sterically constrained active sites. Arch. Biochem. Biophys. 387 (2001) 125-136
    • (2001) Arch. Biochem. Biophys. , vol.387 , pp. 125-136
    • Wust, M.1    Little, D.B.2    Schalk, M.3    Croteau, R.4
  • 52
    • 0034710909 scopus 로고    scopus 로고
    • A single amino acid substitution (F363I) converts the regiochemistry of the spearmint (-)-limonene hydroxylase from a C6-to a C3-hydroxylase
    • Schalk M., and Croteau R. A single amino acid substitution (F363I) converts the regiochemistry of the spearmint (-)-limonene hydroxylase from a C6-to a C3-hydroxylase. Proc. Natl. Acad. Sci. USA 97 (2000) 11948-11953
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11948-11953
    • Schalk, M.1    Croteau, R.2
  • 53
    • 0034235716 scopus 로고    scopus 로고
    • Functional expression of regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha spp.) in Escherichia coli and Saccharomyces cerevisiae
    • Haudenschild C., Schalk M., Karp F., and Croteau R. Functional expression of regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha spp.) in Escherichia coli and Saccharomyces cerevisiae. Arch. Biochem. Biophys. 379 (2000) 127-136
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 127-136
    • Haudenschild, C.1    Schalk, M.2    Karp, F.3    Croteau, R.4
  • 54
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome-P450 family-2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh O. Substrate recognition sites in cytochrome-P450 family-2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267 (1992) 83-90
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 55
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity
    • Williams P.A., Cosme J., Sridhar V., Johnson E.F., and McRee D.E. Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Molecular Cell 5 (2000) 121-131
    • (2000) Molecular Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 56
    • 0001669215 scopus 로고
    • 5-epi-aristolochene is a common precursor of the sesquiterpenoid phytoalexins capsidiol and debneyol
    • Whitehead I.M., Threlfall D.R., and Ewing D.F. 5-epi-aristolochene is a common precursor of the sesquiterpenoid phytoalexins capsidiol and debneyol. Phytochemistry 28 (1989) 775-779
    • (1989) Phytochemistry , vol.28 , pp. 775-779
    • Whitehead, I.M.1    Threlfall, D.R.2    Ewing, D.F.3
  • 58
    • 0035883986 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum.
    • Ralston L., Kwon S.T., Schoenbeck M., Ralston J., Schenk D.J., Coates R.M., and Chappell J. Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum. Arch. Biochem. Biophys. 393 (2001) 222-235
    • (2001) Arch. Biochem. Biophys. , vol.393 , pp. 222-235
    • Ralston, L.1    Kwon, S.T.2    Schoenbeck, M.3    Ralston, J.4    Schenk, D.J.5    Coates, R.M.6    Chappell, J.7
  • 59
    • 0032867296 scopus 로고    scopus 로고
    • The role of structure and molecular properties of terpenoids in determining their antimicrobial activity
    • Griffin S.G., Wyllie S.G., Markham J.L., and Leach D.N. The role of structure and molecular properties of terpenoids in determining their antimicrobial activity. Flavour and Frangrance J. 14 (1999) 322-332
    • (1999) Flavour and Frangrance J. , vol.14 , pp. 322-332
    • Griffin, S.G.1    Wyllie, S.G.2    Markham, J.L.3    Leach, D.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.