메뉴 건너뛰기




Volumn 6, Issue 1, 2006, Pages 209-219

Isoprenoid biosynthesis in plants: Pathways, genes, regulation and metabolic engineering

Author keywords

Biosynthesis; Gene; Isoprenoid; Metabolic engineering; Pathway; Regulation

Indexed keywords

ACETYL COENZYME A ACYLTRANSFERASE; ALKALOID DERIVATIVE; ANTIBIOTIC AGENT; ANTIMALARIAL AGENT; ANTIPARASITIC AGENT; ARTEMISININ; CAROTENOID; HERBICIDE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; HYDROXYMETHYLGLUTARYL COENZYME A SYNTHASE; ISOPENTENYL DIPHOSPHATE; ISOPENTENYL DIPHOSPHATE DELTA ISOMERASE; ISOPRENOID; MEVALONATE KINASE; MEVALONIC ACID; PHOSPHOMEVALONATE KINASE; TERPENOID DERIVATIVE; XYLULOSE;

EID: 33644558723     PISSN: 17273048     EISSN: 18125719     Source Type: Journal    
DOI: 10.3923/jbs.2006.209.219     Document Type: Article
Times cited : (31)

References (78)
  • 1
    • 0029784144 scopus 로고    scopus 로고
    • Diversity and variability of plant secondary metabolism: A mechanistic view
    • Hartmann, T., 2000. Diversity and variability of plant secondary metabolism: a mechanistic view. Entomol. Gen. Application, 80: 177-188.
    • (2000) Entomol. Gen. Application , vol.80 , pp. 177-188
    • Hartmann, T.1
  • 2
    • 0002317514 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of plants
    • Rockville
    • Croteau, R., T.M. Kutchan and N.G. Lewis, 2000. Biochemistry and molecular biology of plants. Am. Soc. Plant Physiol., Rockville, pp: 1250-1318.
    • (2000) Am. Soc. Plant Physiol. , pp. 1250-1318
    • Croteau, R.1    Kutchan, T.M.2    Lewis, N.G.3
  • 3
    • 0015211527 scopus 로고
    • Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia
    • Wani, M.C., H.L. Taylor, M.E. Wall, P. Coggon and A.T. McPhail, 1971. Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia. J. Am. Chem. Soc., 93: 2325-2327.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 2325-2327
    • Wani, M.C.1    Taylor, H.L.2    Wall, M.E.3    Coggon, P.4    McPhail, A.T.5
  • 4
    • 1842423147 scopus 로고    scopus 로고
    • Recent progress in biotechnology and genetic engineering of medicinal plants in China
    • Chen, X.Y. and Z.H. Xu, 1996. Recent progress in biotechnology and genetic engineering of medicinal plants in China. Med. Chem. Res., 6: 215-224.
    • (1996) Med. Chem. Res. , vol.6 , pp. 215-224
    • Chen, X.Y.1    Xu, Z.H.2
  • 5
    • 4344648427 scopus 로고    scopus 로고
    • The effect of Ginkgo Biloba on healthy elderly subjects
    • Cieza, A., P. Maier and E. Poppel, 2003. The effect of Ginkgo Biloba on healthy elderly subjects. Fortschritte Der Medzin, 1: 10-15.
    • (2003) Fortschritte Der Medzin , vol.1 , pp. 10-15
    • Cieza, A.1    Maier, P.2    Poppel, E.3
  • 6
    • 0036005606 scopus 로고    scopus 로고
    • 25 terpenoid compounds
    • 25 terpenoid compounds. Nat. Prod. Rep., 19: 181-222.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 181-222
    • Dewick, P.M.1
  • 7
    • 0038723724 scopus 로고    scopus 로고
    • Metabolic crosstalk between cytosolic and plastidial pathways of isoprenoid biosynthesis: Unidirectional transport of intermediates across the chloroplast envelope membrane
    • Bick, J.A. and B.M. Lange, 2003. Metabolic crosstalk between cytosolic and plastidial pathways of isoprenoid biosynthesis: Unidirectional transport of intermediates across the chloroplast envelope membrane. Arch. Biochem. Biophys., 415: 146-154.
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 146-154
    • Bick, J.A.1    Lange, B.M.2
  • 8
    • 0026757898 scopus 로고
    • Phylogenetic analysis of the thiolase family: Implications for the evolutionary origin of peroxisomes
    • Igual, J.C., C. Gonzalez-Bosch, J. Dopazo and J.E. Perez-Ortin, 1992. Phylogenetic analysis of the thiolase family: Implications for the evolutionary origin of peroxisomes. J. Mol. Evol., 35: 147-155.
    • (1992) J. Mol. Evol. , vol.35 , pp. 147-155
    • Igual, J.C.1    Gonzalez-Bosch, C.2    Dopazo, J.3    Perez-Ortin, J.E.4
  • 9
    • 0022394722 scopus 로고
    • Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation
    • Luskey, K.L. and B. Stevens, 1985. Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation. J. Biol. Chem., 260: 10271-10277.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10271-10277
    • Luskey, K.L.1    Stevens, B.2
  • 10
    • 0023779728 scopus 로고
    • Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis
    • Basson, M.E., M. Thorsness, J. Finer-Moore, R.M. Stroud and J. Rine, 1988. Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis. Mol. Cell. Biol., 8: 3797-3808.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3797-3808
    • Basson, M.E.1    Thorsness, M.2    Finer-Moore, J.3    Stroud, R.M.4    Rine, J.5
  • 11
    • 0034089209 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of the mevalonate kinase gene from Arabidopsis thaliana
    • Lluch, M.A., A. Masferrer, M. Arro, A. Boronat and A. Ferrer, 2000. Molecular cloning and expression analysis of the mevalonate kinase gene from Arabidopsis thaliana. Plant Mol. Biol., 42: 365-376.
    • (2000) Plant Mol. Biol. , vol.42 , pp. 365-376
    • Lluch, M.A.1    Masferrer, A.2    Arro, M.3    Boronat, A.4    Ferrer, A.5
  • 12
    • 0025977152 scopus 로고
    • Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase
    • Tsay, Y.H. and G.W. Robinson, 1991. Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase. Mol. Cell Biol., 11: 620-631.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 620-631
    • Tsay, Y.H.1    Robinson, G.W.2
  • 13
    • 0028138514 scopus 로고
    • Mechanism of mevalonate pyrophosphate decarboxylase: Evidence for a carbocationic transition state
    • Dhe-Paganon, S., J. Magrath and R.H. Abeles, 1994. Mechanism of mevalonate pyrophosphate decarboxylase: evidence for a carbocationic transition state. Biochemistry, 33: 133551-133562.
    • (1994) Biochemistry , vol.33 , pp. 133551-133562
    • Dhe-Paganon, S.1    Magrath, J.2    Abeles, R.H.3
  • 14
    • 0037454345 scopus 로고    scopus 로고
    • Structure and mechanism of action of isopentenylpyrophosphate-dimethylallylpyrophosphate isomerase
    • Wouters, J., Y. Oudjama, S. Ghosh, V. Stalon, L. Droogmans and E. Oldfield, 2003. Structure and mechanism of action of isopentenylpyrophosphate-dimethylallylpyrophosphate isomerase. J. Am. Chem. Soc., 125: 3198-3199.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3198-3199
    • Wouters, J.1    Oudjama, Y.2    Ghosh, S.3    Stalon, V.4    Droogmans, L.5    Oldfield, E.6
  • 15
    • 0032522566 scopus 로고    scopus 로고
    • Mevalonate-derived isopentenyl diphosphate is the biosynthetic precursor of ubiquinone prenyl side chain in tobacco BY-2 cells
    • Disch, A., A. Hemmerlin, T.J. Bach and M. Rohmer, 1998. Mevalonate-derived isopentenyl diphosphate is the biosynthetic precursor of ubiquinone prenyl side chain in tobacco BY-2 cells. Biochem. J., 331: 615-621.
    • (1998) Biochem. J. , vol.331 , pp. 615-621
    • Disch, A.1    Hemmerlin, A.2    Bach, T.J.3    Rohmer, M.4
  • 16
    • 0027368126 scopus 로고
    • Isoprenoid biosynthesis in bacteria: A novel pathway for the early steps leading to isopentenyl diphosphate
    • Rohmer, M., M. Knani, P. Simonin, B. Sutter and H. Sahm, 1993. Isoprenoid biosynthesis in bacteria: a novel pathway for the early steps leading to isopentenyl diphosphate. Biochem. J., 295: 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
    • 0003740095 scopus 로고
    • Terpen-Biosynthese in Ginkgo biloba: Eine überraschende Geschichte
    • Ph.D Thesis Nr 10951, ETH, Zürich, Switzerland
    • Schwarz, M.K., 1994. Terpen-Biosynthese in Ginkgo biloba: eine überraschende Geschichte. Ph.D Thesis Nr 10951, ETH, Zürich, Switzerland.
    • (1994)
    • Schwarz, M.K.1
  • 18
    • 0030696041 scopus 로고    scopus 로고
    • Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol
    • Sprenger, G.A., U. Schörken, T. Wiegert, S. Grolle, A.A.D. Graaf, S.V. Taylor, T.P. Begley, S. Bringer-Meyer and H. Sahm, 1997. Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol. Proc. Natl. Acad. Sci. USA, 94: 12857-12862.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12857-12862
    • Sprenger, G.A.1    Schörken, U.2    Wiegert, T.3    Grolle, S.4    Graaf, A.A.D.5    Taylor, S.V.6    Begley, T.P.7    Bringer-Meyer, S.8    Sahm, H.9
  • 19
    • 0035933854 scopus 로고    scopus 로고
    • 1-deoxy-D-xylulose-5-phosphate synthase, a limiting enzyme for plastidic isoprenoid biosynthesis in plants
    • Juan, M., E.A. Cantero, A. Reindl, S. Reichler and P. León, 2001. 1-deoxy-D-xylulose-5-phosphate synthase, a limiting enzyme for plastidic isoprenoid biosynthesis in plants. J. Biol. Chem., 276: 22901-22909.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22901-22909
    • Juan, M.1    Cantero, E.A.2    Reindl, A.3    Reichler, S.4    León, P.5
  • 20
    • 0032544054 scopus 로고    scopus 로고
    • A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis
    • Takahashi, S., T. Kuzuyama, H. Watanabe and H. Seto, 1998. A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis. Proc. Nat. Acad. Sci. USA, 95: 9879-9884.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 9879-9884
    • Takahashi, S.1    Kuzuyama, T.2    Watanabe, H.3    Seto, H.4
  • 22
    • 0038043258 scopus 로고    scopus 로고
    • Structural basis of fosmidomycin action revealed by the complex with 2-C-methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the catalytic mechanism and anti-malaria drug development
    • Steinbacher, S., J. Kaiser, W. Eisenreich, R. Huber, A. Bacher and F. Rohdich, 2003. Structural basis of fosmidomycin action revealed by the complex with 2-C-methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the catalytic mechanism and anti-malaria drug development. J. Biol. Chem., 278: 18401-18407.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18401-18407
    • Steinbacher, S.1    Kaiser, J.2    Eisenreich, W.3    Huber, R.4    Bacher, A.5    Rohdich, F.6
  • 24
    • 0026887816 scopus 로고
    • Sequence and characterization of the gcpE gene of Escherichia coli
    • Baker, J., D.B. Franklin and J. Parker, 1992. Sequence and characterization of the gcpE gene of Escherichia coli. FEMS Microbiol. Lett., 73: 175-180.
    • (1992) FEMS Microbiol. Lett. , vol.73 , pp. 175-180
    • Baker, J.1    Franklin, D.B.2    Parker, J.3
  • 25
    • 0033813444 scopus 로고    scopus 로고
    • Evidence of a role for LytB in the nonmevalonate pathway of isoprenoid biosynthesis
    • Cunningham, F.X., T.P. Lafond and E. Gantt, 2000. Evidence of a role for LytB in the nonmevalonate pathway of isoprenoid biosynthesis. J. Bacteriol., 182: 5841-5848.
    • (2000) J. Bacteriol. , vol.182 , pp. 5841-5848
    • Cunningham, F.X.1    Lafond, T.P.2    Gantt, E.3
  • 26
    • 0029559203 scopus 로고
    • Isolation and characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl-coenzyme A synthase
    • Montamat, F., M. Guilloton, F. Karst and S. Delrot, 1995. Isolation and characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl-coenzyme A synthase. Gene, 167: 197-201.
    • (1995) Gene , vol.167 , pp. 197-201
    • Montamat, F.1    Guilloton, M.2    Karst, F.3    Delrot, S.4
  • 27
    • 0030220457 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding cytosolic acetoacetyl-coenzyme a thiolase from radish by functional expression in Saccharomyces cerevisiae
    • Vollack, K.U. and T.J. Bach, 1996. Cloning of a cDNA encoding cytosolic acetoacetyl-coenzyme a thiolase from radish by functional expression in Saccharomyces cerevisiae. Plant Physiol., 111: 1097-1107.
    • (1996) Plant Physiol. , vol.111 , pp. 1097-1107
    • Vollack, K.U.1    Bach, T.J.2
  • 28
    • 0027932251 scopus 로고
    • Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme-A synthase-expression, purification, and characterization of recombinant wild-type and Cys(129) mutant enzymes
    • Rokosz, L.L., D.A. Boulton, E.A. Butkiewicz, G. Sanyal, M.A. Cueto, P.A. Lachance and J.D. Hermes, 1994. Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme-A synthase-expression, purification, and characterization of recombinant wild-type and Cys(129) mutant enzymes. Arch. Biochem. Biophys., 312: 1-13.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 1-13
    • Rokosz, L.L.1    Boulton, D.A.2    Butkiewicz, E.A.3    Sanyal, G.4    Cueto, M.A.5    Lachance, P.A.6    Hermes, J.D.7
  • 29
    • 0034124423 scopus 로고    scopus 로고
    • Expression of Brassica juncea 3-hydroxy-3-methylglutaryl CoA synthase is developmentally regulated and stress-responsive
    • Alex, D., T.J. Bach and M.L. Chye, 2000. Expression of Brassica juncea 3-hydroxy-3-methylglutaryl CoA synthase is developmentally regulated and stress-responsive. Plant J., 22: 415-426.
    • (2000) Plant J. , vol.22 , pp. 415-426
    • Alex, D.1    Bach, T.J.2    Chye, M.L.3
  • 30
    • 0031588983 scopus 로고    scopus 로고
    • Molecular cloning of ozone-inducible protein from Pinus sylvestris L. with high sequence similarity to vertebrate 3-hydroxy-3-methylglutaryl-CoA-synthase
    • Wegener, A., W. Gimbel, T. Werner, J. Hani, D. Ernst and H.J. Sandermann, 1997. Molecular cloning of ozone-inducible protein from Pinus sylvestris L. with high sequence similarity to vertebrate 3-hydroxy-3-methylglutaryl-CoA-synthase. Biochem. Biophys. Acta, 1350: 247-252.
    • (1997) Biochem. Biophys. Acta , vol.1350 , pp. 247-252
    • Wegener, A.1    Gimbel, W.2    Werner, T.3    Hani, J.4    Ernst, D.5    Sandermann, H.J.6
  • 31
    • 1242322438 scopus 로고    scopus 로고
    • Regulation of the expression of 3-hydroxy-3-methylglutaryl-CoA synthase gene in Hevea brasiliensis (BHK) Mull
    • Suwanmanee, P., N. Sirinupong and W. Suvachittanont, 2004. Regulation of the expression of 3-hydroxy-3-methylglutaryl-CoA synthase gene in Hevea brasiliensis (BHK) Mull. Arg. Plant Sci., 166: 531-537.
    • (2004) Arg. Plant Sci. , vol.166 , pp. 531-537
    • Suwanmanee, P.1    Sirinupong, N.2    Suvachittanont, W.3
  • 32
    • 0024869502 scopus 로고
    • Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Caelles, C., A. Ferrer, L. Balcells, F.G. Hegardt and A. Boronat, 1989. Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl coenzyme A reductase. Plant Mol. Biol., 13: 627-638.
    • (1989) Plant Mol. Biol. , vol.13 , pp. 627-638
    • Caelles, C.1    Ferrer, A.2    Balcells, L.3    Hegardt, F.G.4    Boronat, A.5
  • 33
    • 0034672685 scopus 로고    scopus 로고
    • The structure of the catalytic portion of human HMG-CoA reductase
    • Istvan, E.S. and J. Deisenhofer, 2000. The structure of the catalytic portion of human HMG-CoA reductase. Biochem. Biophys. Acta, 1529: 9-18.
    • (2000) Biochem. Biophys. Acta , vol.1529 , pp. 9-18
    • Istvan, E.S.1    Deisenhofer, J.2
  • 35
    • 10744224664 scopus 로고    scopus 로고
    • Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG1) in Arabidopsis leads to dwarfing, early senescence and male sterility and reduced sterol levels
    • Suzuki, M., Y. Kamide, N. Nagata, H. Seki, K. Ohyama, H. Kato, K. Masuda, S. Sato, T. Kato, S. Tabata, S. Yoshida and T. Muranaka, 2004. Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG1) in Arabidopsis leads to dwarfing, early senescence and male sterility and reduced sterol levels. Plant J., 37: 750.
    • (2004) Plant J. , vol.37 , pp. 750
    • Suzuki, M.1    Kamide, Y.2    Nagata, N.3    Seki, H.4    Ohyama, K.5    Kato, H.6    Masuda, K.7    Sato, S.8    Kato, T.9    Tabata, S.10    Yoshida, S.11    Marunaka, T.12
  • 36
    • 0031193658 scopus 로고    scopus 로고
    • Molecular characterization of three differentially expressed members of the Camptotheca acuminata 3-hydroxy-3-methylglutaryl CoA reductase (HMGR) gene family
    • Maldonado-Mendoza, I.E., R.M. Vincent and C.L. Nessler, 1997. Molecular characterization of three differentially expressed members of the Camptotheca acuminata 3-hydroxy-3-methylglutaryl CoA reductase (HMGR) gene family. Plant Mol. Biol., 34: 781-790.
    • (1997) Plant Mol. Biol. , vol.34 , pp. 781-790
    • Maldonado-Mendoza, I.E.1    Vincent, R.M.2    Nessler, C.L.3
  • 37
    • 0000998082 scopus 로고
    • Nucleotide sequence of a cDNA encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase from Catharanthus roseus
    • Maldenado-Mendoza, I.E., R.J. Burnett and C.L. Nessler, 1992. Nucleotide sequence of a cDNA encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase from Catharanthus roseus. Plant Physiol., 100: 1613-1614.
    • (1992) Plant Physiol. , vol.100 , pp. 1613-1614
    • Maldenado-Mendoza, I.E.1    Burnett, R.J.2    Nessler, C.L.3
  • 38
    • 0035094242 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase in melon (Cucumis melo L. reticulatus)
    • Kato-Emori, S., K. Higashi, K. Hosoya, T. Kobayashi and H. Ezura, 2001. Cloning and characterization of the gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase in melon (Cucumis melo L. reticulatus). Mol. Genet. Gen., 265: 135-142.
    • (2001) Mol. Genet. Gen. , vol.265 , pp. 135-142
    • Kato-Emori, S.1    Higashi, K.2    Hosoya, K.3    Kobayashi, T.4    Ezura, H.5
  • 39
    • 0026929907 scopus 로고
    • Structure and nucleotide sequence of tomato HMG2 encoding 3-hydroxy-3-methyl-glutaryl coenzyme A reductase
    • Park, H., C.J. Denbow and C.L. Cramer, 1992. Structure and nucleotide sequence of tomato HMG2 encoding 3-hydroxy-3-methyl-glutaryl coenzyme A reductase. Plant Mol. Biol., 20: 327-331.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 327-331
    • Park, H.1    Denbow, C.J.2    Cramer, C.L.3
  • 40
    • 0024650719 scopus 로고
    • 3-Hydroxy-3-methylglutaryl-coenzyme A reductase from Arabidopsis thaliana is structurally distinct from the yeast and animal enzymes
    • Learned, R.M. and G.R. Fink, 1989. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase from Arabidopsis thaliana is structurally distinct from the yeast and animal enzymes. Proc. Nat. Acad. Sci. USA, 86: 2779-2783.
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 2779-2783
    • Learned, R.M.1    Fink, G.R.2
  • 42
    • 0026871155 scopus 로고
    • Three genes encode 3-hydroxy-3-methylglutaryl-coenzyme A reductase in Hevea brasiliensis: hmg1 and hmg3 are differentially expressed
    • Chye M.L., C.T. Tan and H.H. Chua, 1992. Three genes encode 3-hydroxy-3-methylglutaryl-coenzyme A reductase in Hevea brasiliensis: hmg1 and hmg3 are differentially expressed. Plant Mol. Biol., 19: 473-484.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 473-484
    • Chye, M.L.1    Tan, C.T.2    Chua, H.H.3
  • 43
    • 0028906885 scopus 로고
    • Some new aspects of isoprenoid biosynthesis in plants-a review
    • Bach, T.J., 1995. Some new aspects of isoprenoid biosynthesis in plants-a review. Lipids, 30: 191-202.
    • (1995) Lipids , vol.30 , pp. 191-202
    • Bach, T.J.1
  • 44
    • 0033485305 scopus 로고    scopus 로고
    • Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene
    • Lee, M. and T. Leustek, 1999. Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene. Arch. Biochem. Biophys., 372: 135-142.
    • (1999) Arch. Biochem. Biophys. , vol.372 , pp. 135-142
    • Lee, M.1    Leustek, T.2
  • 45
    • 0033103924 scopus 로고    scopus 로고
    • Heterologous expression in Saccharomyces cerevisiae of an Arabidopsis thaliana cDNA encoding mevalonate diphosphate decarboxylase
    • Cordier, H., F. Karst and T. Berges, 1999. Heterologous expression in Saccharomyces cerevisiae of an Arabidopsis thaliana cDNA encoding mevalonate diphosphate decarboxylase. Plant Mol. Biol., 39: 953-967.
    • (1999) Plant Mol. Biol. , vol.39 , pp. 953-967
    • Cordier, H.1    Karst, F.2    Berges, T.3
  • 46
    • 0033963451 scopus 로고    scopus 로고
    • Identification of multi-gene families encoding isopentenyl diphosphate isomerase in plants by heterologous complementation in Escherichia coli
    • Cunningham, F.X.J. and E. Gantt, 2000. Identification of multi-gene families encoding isopentenyl diphosphate isomerase in plants by heterologous complementation in Escherichia coli. Plant Cell. Physiol., 41: 119-123.
    • (2000) Plant Cell. Physiol. , vol.41 , pp. 119-123
    • Cunningham, F.X.J.1    Gantt, E.2
  • 48
    • 0031434083 scopus 로고    scopus 로고
    • Isopentenyl diphosphate isomerase: A core enzyme in isoprenoid biosynthesis. A review of its biochemistry and function
    • Ramos-Valdivia, A.C., R. Van der Heijden and R. Verpoorte, 1997. Isopentenyl diphosphate isomerase: a core enzyme in isoprenoid biosynthesis. A review of its biochemistry and function. Natl. Prod. Rep., 14: 591-603.
    • (1997) Natl. Prod. Rep. , vol.14 , pp. 591-603
    • Ramos-Valdivia, A.C.1    Van der Heijden, R.2    Verpoorte, R.3
  • 49
    • 0342505289 scopus 로고    scopus 로고
    • Carotenoid biosynthesis during tomato fruit development: Regulatory role of 1-deoxy-D-xylulose 5-phosphate synthase
    • Lois, L.M., M. Rodriguez-Concepcion, F. Gallego, N. Campos and A. Boronat, 2000. Carotenoid biosynthesis during tomato fruit development: regulatory role of 1-deoxy-D-xylulose 5-phosphate synthase. Plant J., 22: 503-513.
    • (2000) Plant J. , vol.22 , pp. 503-513
    • Lois, L.M.1    Rodriguez-Concepcion, M.2    Gallego, F.3    Campos, N.4    Boronat, A.5
  • 50
    • 0032132839 scopus 로고    scopus 로고
    • Dedicated roles of plastid transketolases during the early onset of isoprenoid biogenesis in pepper fruits
    • Bouvier, F., A.D. Harlingue, C. Suire, R.A. Backhaus and B. Camara, 1998. Dedicated roles of plastid transketolases during the early onset of isoprenoid biogenesis in pepper fruits. Plant Physiol., 117: 1423-1431.
    • (1998) Plant Physiol. , vol.117 , pp. 1423-1431
    • Bouvier, F.1    Harlingue, A.D.2    Suire, C.3    Backhaus, R.A.4    Camara, B.5
  • 51
    • 0036872868 scopus 로고    scopus 로고
    • The mevalonate-independent pathway is expressed in transformed roots of artemisia annua and regulated by light and culture age
    • Souret, F.D.F., P.J. Weathers and K.K. Wobbe, 2002. The mevalonate-independent pathway is expressed in transformed roots of artemisia annua and regulated by light and culture age. In vitro Cell. Dev. Biol. Plant, 38: 581-588.
    • (2002) In Vitro Cell. Dev. Biol. Plant , vol.38 , pp. 581-588
    • Souret, F.D.F.1    Weathers, P.J.2    Wobbe, K.K.3
  • 52
    • 0019252768 scopus 로고
    • Studies on new phosphonic acid antibiotics III. Isolation and characterization of FR-31564, FR-32863 and FR-33289, So DXR is the new target protein for developing new herbicides
    • Okuhara, M., Y. Kuroda, T. Goto, M. Okamoto, H. Terano, M. Kohsaka, H. Aoki and H. Imanaka, 1980. Studies on new phosphonic acid antibiotics III. Isolation and characterization of FR-31564, FR-32863 and FR-33289, So DXR is the new target protein for developing new herbicides. J. Antibiot., 33: 24-28.
    • (1980) J. Antibiot. , vol.33 , pp. 24-28
    • Okuhara, M.1    Kuroda, Y.2    Goto, T.3    Okamoto, M.4    Terano, H.5    Kohsaka, M.6    Aoki, H.7    Imanaka, H.8
  • 53
    • 0034830836 scopus 로고    scopus 로고
    • Metabolite profiling of peppermint oil gland secretary cells and application to herbicide target analysis
    • B
    • Markus L., B., E.B. Raymond, L. Ketchum and R.B. Croteau, 2001. Metabolite profiling of peppermint oil gland secretary cells and application to herbicide target analysis. Plant Physiol., 127: 305-314.
    • (2001) Plant Physiol. , vol.127 , pp. 305-314
    • Markus, L.1    Raymond, E.B.2    Ketchum, L.3    Croteau, R.B.4
  • 54
    • 0034700150 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis: The evolution of two ancient and distinct pathways across genomes
    • B
    • Markus L., B., T. Rujan, W. Martin and R. Croteau, 2000. Isoprenoid biosynthesis: The evolution of two ancient and distinct pathways across genomes. Proc. Nat. Acad. Sci. USA, 97: 13172-13177.
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 13172-13177
    • Markus, L.1    Rujan, T.2    Martin, W.3    Croteau, R.4
  • 55
    • 0037008188 scopus 로고    scopus 로고
    • Expression and molecular analysis of the Arabidopsis DXR gene encoding 1-deoxy-D-xylulose 5-phosphate reductoisomerase, the first committed enzyme of the 2-C-methyl-D-erythritol 4-phosphate pathway
    • Carretero-Paulet, L., I. Ahumada, N. Cunillera, M. Rodriguez-Concepcion, A. Ferrer, A. Boronat and N. Campos, 2002. Expression and molecular analysis of the Arabidopsis DXR gene encoding 1-deoxy-D-xylulose 5-phosphate reductoisomerase, the first committed enzyme of the 2-C-methyl-D-erythritol 4-phosphate pathway. Plant Physiol., 129: 1581-1591.
    • (2002) Plant Physiol. , vol.129 , pp. 1581-1591
    • Carretero-Paulet, L.1    Ahumada, I.2    Cunillera, N.3    Rodriguez-Concepcion, M.4    Ferrer, A.5    Boronat, A.6    Campos, N.7
  • 59
    • 0035088792 scopus 로고    scopus 로고
    • GcpE is involved in the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli
    • Altincicek, B., A.K. Kollas, S. Sanderbrand, J. Wiesner, M. Hintz, E. Beck and H. Jomaa, 2001. GcpE is involved in the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli. J. Bacteriol., 183: 2411-2416.
    • (2001) J. Bacteriol. , vol.183 , pp. 2411-2416
    • Altincicek, B.1    Kollas, A.K.2    Sanderbrand, S.3    Wiesner, J.4    Hintz, M.5    Beck, E.6    Jomaa, H.7
  • 60
    • 0037070556 scopus 로고    scopus 로고
    • Functional analysis of the Arabidopsis thaliana GCPE protein involved in plastid isoprenoid biosynthesis
    • Querol, J., N. Campos, S. Imperial, A. Boronat and M. Rodriguez-Concepcion, 2002. Functional analysis of the Arabidopsis thaliana GCPE protein involved in plastid isoprenoid biosynthesis. FEBS Lett., 514: 343-346.
    • (2002) FEBS Lett. , vol.514 , pp. 343-346
    • Querol, J.1    Campos, N.2    Imperial, S.3    Boronat, A.4    Rodriguez-Concepcion, M.5
  • 61
    • 0042209700 scopus 로고    scopus 로고
    • Bioinformatic and molecular analysis of hydroxymethylbutenyl diphosphate synthase (GCPE) gene expression during carotenoid accumulation in ripening tomato fruit
    • Rodriguez-Concepeion, M., J. Querol, L.M. Lois, S. Imperial and A. Boronat, 2003. Bioinformatic and molecular analysis of hydroxymethylbutenyl diphosphate synthase (GCPE) gene expression during carotenoid accumulation in ripening tomato fruit. Planta, 217: 476-482.
    • (2003) Planta , vol.217 , pp. 476-482
    • Rodriguez-Concepeion, M.1    Querol, J.2    Lois, L.M.3    Imperial, S.4    Boronat, A.5
  • 63
    • 1942533683 scopus 로고    scopus 로고
    • Functional analysis of the final steps of the 1-Deoxy-D-xylulose 5-phosphate (DXP) pathway to isoprenoids in plants using virus-induced gene silencing
    • Page, J.E., G. Hause, M. Raschke, W.Y. Gao, J. Schmidt, M.H. Zenk and T.M. Kutchan, 2004. Functional analysis of the final steps of the 1-Deoxy-D-xylulose 5-phosphate (DXP) pathway to isoprenoids in plants using virus-induced gene silencing. Plant Physiol., 134: 1401-1413.
    • (2004) Plant Physiol. , vol.134 , pp. 1401-1413
    • Page, J.E.1    Hause, G.2    Raschke, M.3    Gao, W.Y.4    Schmidt, J.5    Zenk, M.H.6    Kutchan, T.M.7
  • 64
    • 0031798616 scopus 로고    scopus 로고
    • Biosynthesis of the isoprene units of chamomile sesquiterpenes
    • Adam, K.P. and J. Zapp, 1998. Biosynthesis of the isoprene units of chamomile sesquiterpenes. Phytochemistry, 48: 953-959.
    • (1998) Phytochemistry , vol.48 , pp. 953-959
    • Adam, K.P.1    Zapp, J.2
  • 65
    • 0037327989 scopus 로고    scopus 로고
    • Inhibitor studies of isopentenyl pyrophosphate biosynthesis in suspension cultures of the new Taxus chinensis var. mairei
    • Wang, Y.D., Y.J. Yuan, M. Lu, J.C. Wu and J.L. Jiang, 2003. Inhibitor studies of isopentenyl pyrophosphate biosynthesis in suspension cultures of the new Taxus chinensis var. mairei. Biotechnol. Applied Biochem., 37: 39-43.
    • (2003) Biotechnol. Applied Biochem. , vol.37 , pp. 39-43
    • Wang, Y.D.1    Yuan, Y.J.2    Lu, M.3    Wu, J.C.4    Jiang, J.L.5
  • 67
    • 0033983338 scopus 로고    scopus 로고
    • Engineering provitamin A (β-carotene) biosynthetic pathway into (caroteneoidfree) rice endosperm
    • Ye, X.D., S. Al-Babili, A. Klöti, J. Zhang, P. Lucca, P. Beyer and I. Potrykus, 2000. Engineering provitamin A (β-carotene) biosynthetic pathway into (caroteneoidfree) rice endosperm. Science, 287: 303-305.
    • (2000) Science , vol.287 , pp. 303-305
    • Ye, X.D.1    Al-Babili, S.2    Klöti, A.3    Zhang, J.4    Lucca, P.5    Beyer, P.6    Potrykus, I.7
  • 69
    • 0033898414 scopus 로고    scopus 로고
    • Metabolic engineering of astaxanthin production in tobacco flowers
    • Mann, V., M. Harker, I. Pecker and J. Hirschberg, 2000. Metabolic engineering of astaxanthin production in tobacco flowers. Natl. Biotechnol., 18: 888-892.
    • (2000) Natl. Biotechnol. , vol.18 , pp. 888-892
    • Mann, V.1    Harker, M.2    Pecker, I.3    Hirschberg, J.4
  • 70
    • 0033941389 scopus 로고    scopus 로고
    • Molecular breeding of carotenoid biosynthetic pathways
    • Schmidt-Dannert, C., D. Umeno and F.H. Arnold, 2000. Molecular breeding of carotenoid biosynthetic pathways. Natl. Biotechnol., 18: 750-753.
    • (2000) Natl. Biotechnol. , vol.18 , pp. 750-753
    • Schmidt-Dannert, C.1    Umeno, D.2    Arnold, F.H.3
  • 71
    • 0033119714 scopus 로고    scopus 로고
    • Genetic engineering of essential oil production in mint
    • Lange, B.M. and R. Croteau, 1999. Genetic engineering of essential oil production in mint. Curr. Opin. Plant Biol., 2: 139-144.
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 139-144
    • Lange, B.M.1    Croteau, R.2
  • 72
    • 0038391517 scopus 로고    scopus 로고
    • Engineering a mevalonate pathway in Escherichia coli for production of terpenoids
    • Martin, V.J.J., D.J. Pitera, S.T. Withers, J.D. Newman and J.D. Keasling, 2003. Engineering a mevalonate pathway in Escherichia coli for production of terpenoids. Nat. Biotech., 21: 796-802.
    • (2003) Nat. Biotech. , vol.21 , pp. 796-802
    • Martin, V.J.J.1    Pitera, D.J.2    Withers, S.T.3    Newman, J.D.4    Keasling, J.D.5
  • 73
    • 0034647914 scopus 로고    scopus 로고
    • ORCA3, a jasmonate-responsive transcriptional regulator of plant primary and secondary metabolism
    • Fits, L.V.D. and J. Memelink, 2000. ORCA3, a jasmonate-responsive transcriptional regulator of plant primary and secondary metabolism. Science, 289: 295-297.
    • (2000) Science , vol.289 , pp. 295-297
    • Fits, L.V.D.1    Memelink, J.2
  • 74
    • 0034830836 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis: Metabolite profiling of peppermint oil gland secretary cells and application to herbicide target analysis
    • Lange, B.M., R.E.B. Ketchum and R. Croteau, 2001. Isoprenoid biosynthesis: Metabolite profiling of peppermint oil gland secretary cells and application to herbicide target analysis. Plant Physiol., 127: 305-314.
    • (2001) Plant Physiol. , vol.127 , pp. 305-314
    • Lange, B.M.1    Ketchum, R.E.B.2    Croteau, R.3
  • 76
    • 0033940216 scopus 로고    scopus 로고
    • Increased gibberellin biosynthesis in transgenic trees promotes growth, biomass production and xylem fiber length
    • Eriksson, M.E., M. Israelsson, O. Olsson and T. Moritz, 2000. Increased gibberellin biosynthesis in transgenic trees promotes growth, biomass production and xylem fiber length. Natl. Biotechnol., 18: 784-788.
    • (2000) Natl. Biotechnol. , vol.18 , pp. 784-788
    • Eriksson, M.E.1    Israelsson, M.2    Olsson, O.3    Moritz, T.4
  • 78
    • 0034105938 scopus 로고    scopus 로고
    • Metabolic engineering of carotenoid accumulation in E. coli by modulation of the isoprenoid precursor pool with expression of deoxyxylulose phosphate synthase
    • Matthews, P.D. and E.T. Wurtzel, 2000. Metabolic engineering of carotenoid accumulation in E. coli by modulation of the isoprenoid precursor pool with expression of deoxyxylulose phosphate synthase. Applied Microbiol. Biotechnol., 53: 396-400.
    • (2000) Applied Microbiol. Biotechnol. , vol.53 , pp. 396-400
    • Matthews, P.D.1    Wurtzel, E.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.