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Volumn , Issue , 2011, Pages 173-196

Microbial Production of Plant-Derived Pharmaceutical Natural Products through Metabolic Engineering: Artemisinin and beyond

Author keywords

Artemisinin and beyond; As the rate limiting pathway enzyme for amorphadiene biosynthesis; Gene copy numbers of titrating pathway enzymes identifying mevalonate kinase (MK); Microbial production of plant derived pharmaceutical natural products through metabolic engineering; Terpene indole alkaloids expanding upon mevalonate pathway

Indexed keywords


EID: 84881543561     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118028308.ch7     Document Type: Chapter
Times cited : (2)

References (66)
  • 1
    • 0000931448 scopus 로고
    • Shanidar IV, a Neanderthal flower burial in northern Iraq
    • Solecki R. Shanidar IV, a Neanderthal flower burial in northern Iraq. Science 1975;190:880-881.
    • (1975) Science , vol.190 , pp. 880-881
    • Solecki, R.1
  • 2
    • 0016820627 scopus 로고
    • The flowers found with Shanidar IV, a Neanderthal burial in Iraq
    • Leroi-Gourhan A. The flowers found with Shanidar IV, a Neanderthal burial in Iraq. Science 1975;190:562-564.
    • (1975) Science , vol.190 , pp. 562-564
    • Leroi-Gourhan, A.1
  • 3
    • 0042844744 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the period 1981-2002
    • Newman J, Cragg G, Snader K. Natural products as sources of new drugs over the period 1981-2002. J Nat Prod 2003;66:1022-1037.
    • (2003) J Nat Prod , vol.66 , pp. 1022-1037
    • Newman, J.1    Cragg, G.2    Snader, K.3
  • 4
    • 39149137869 scopus 로고    scopus 로고
    • Plant-derived compounds in clinical trials
    • Saklani A, Kutty S. Plant-derived compounds in clinical trials. Drug Discov Today 2008;13:161-171.
    • (2008) Drug Discov Today , vol.13 , pp. 161-171
    • Saklani, A.1    Kutty, S.2
  • 6
    • 0028013416 scopus 로고
    • How to make taxol from scratch
    • Horwitz SB. How to make taxol from scratch. Nature 1994;367:593-594.
    • (1994) Nature , vol.367 , pp. 593-594
    • Horwitz, S.B.1
  • 7
    • 0034789998 scopus 로고    scopus 로고
    • Taxol: biosynthesis, molecular genetics, and biotechnological applications
    • Jennewein S, Croteau R. Taxol: biosynthesis, molecular genetics, and biotechnological applications. Appl Microbiol Biotechnol 2001;57:13-19.
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 13-19
    • Jennewein, S.1    Croteau, R.2
  • 8
    • 0025641040 scopus 로고
    • The discovery of the vinca alkaloids-chemotherapeutic agents against cancer
    • Noble R. The discovery of the vinca alkaloids-chemotherapeutic agents against cancer. Biochem Cell Biol 1990;68:1344-1351.
    • (1990) Biochem Cell Biol , vol.68 , pp. 1344-1351
    • Noble, R.1
  • 9
    • 0037436563 scopus 로고    scopus 로고
    • Dispelling the myths-biocatalysis in industrial synthesis
    • Schoemaker HE, Mink D, Wubbolts MG. Dispelling the myths-biocatalysis in industrial synthesis. Science 2003;299:1694-1697.
    • (2003) Science , vol.299 , pp. 1694-1697
    • Schoemaker, H.E.1    Mink, D.2    Wubbolts, M.G.3
  • 13
    • 0034967907 scopus 로고    scopus 로고
    • The economic burden of malaria
    • Gallup J, Sachs J. The economic burden of malaria. Am J Trop Med Hyg 2001;64:85-96.
    • (2001) Am J Trop Med Hyg , vol.64 , pp. 85-96
    • Gallup, J.1    Sachs, J.2
  • 14
    • 1242344209 scopus 로고    scopus 로고
    • Climate change and malaria: analysis of the SRES climate and socio-economic scenarios
    • van Lieshout M, Kovats RS, Livermore MTJ, Martens P. Climate change and malaria: analysis of the SRES climate and socio-economic scenarios. Glob Environ Change 2004;14:87-99.
    • (2004) Glob Environ Change , vol.14 , pp. 87-99
    • van Lieshout, M.1    Kovats, R.S.2    Livermore, M.T.J.3    Martens, P.4
  • 16
    • 0034911341 scopus 로고    scopus 로고
    • Distributive justice and clinical trials in the third world
    • Benatar S. Distributive justice and clinical trials in the third world. Theor Med 2001;22:169-176.
    • (2001) Theor Med , vol.22 , pp. 169-176
    • Benatar, S.1
  • 18
    • 56549084929 scopus 로고    scopus 로고
    • Making artemisinin
    • Covello PS. Making artemisinin. Phytochemistry 2008;69:2881-2885.
    • (2008) Phytochemistry , vol.69 , pp. 2881-2885
    • Covello, P.S.1
  • 19
    • 54249161841 scopus 로고    scopus 로고
    • Predicting Global Fund grant disbursements for procurement of artemisinin-based combination therapies
    • Cohen JM, Singh I, O'Brien ME. Predicting Global Fund grant disbursements for procurement of artemisinin-based combination therapies. Malar J 2008;7: 200.
    • (2008) Malar J , vol.7 , pp. 200
    • Cohen, J.M.1    Singh, I.2    O'Brien, M.E.3
  • 20
    • 40049097594 scopus 로고    scopus 로고
    • Microbially derived artemisinin: a biotechnology solution to the global problem of access to affordable antimalarial drugs
    • Hale V, Keasling JD, Renninger N, Diagana TT. Microbially derived artemisinin: a biotechnology solution to the global problem of access to affordable antimalarial drugs. Am J Trop Med Hyg 2007;77:198-202.
    • (2007) Am J Trop Med Hyg , vol.77 , pp. 198-202
    • Hale, V.1    Keasling, J.D.2    Renninger, N.3    Diagana, T.T.4
  • 22
    • 33845919578 scopus 로고    scopus 로고
    • Comparative assessment of technologies for extraction of artemisinin
    • Lapkin AA, Plucinski PK, Cutler M. Comparative assessment of technologies for extraction of artemisinin. J Nat Prod 2006;69:1653-1664.
    • (2006) J Nat Prod , vol.69 , pp. 1653-1664
    • Lapkin, A.A.1    Plucinski, P.K.2    Cutler, M.3
  • 23
    • 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, Sahm H. Isoprenoid biosynthesis in bacteria: a novel pathway for the early steps leading to isopentenyl diphosphate. Biochem J 1993: 295.
    • (1993) Biochem J
    • Rohmer, M.1    Knani, M.2    Simonin, P.3    Sutter, B.4    Sahm, H.5
  • 25
    • 0029804201 scopus 로고    scopus 로고
    • A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product
    • Ohnuma S, Narita K, Nakazawa T, Ishida C, Takeuchi Y, Ohto C, Nishino T. A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product. J Biol Chem 1996;271:30748-30754.
    • (1996) J Biol Chem , vol.271 , pp. 30748-30754
    • Ohnuma, S.1    Narita, K.2    Nakazawa, T.3    Ishida, C.4    Takeuchi, Y.5    Ohto, C.6    Nishino, T.7
  • 26
    • 13844297445 scopus 로고    scopus 로고
    • Directed evolution of Escherichia coli farnesyl diphosphate synthase (IspA) reveals novel structural determinants of chain length specificity
    • Lee PC, Petri R, Mijts BN, Watts KT, Schmidt-Dannert C. Directed evolution of Escherichia coli farnesyl diphosphate synthase (IspA) reveals novel structural determinants of chain length specificity. Metab Eng 2005;7:18-26.
    • (2005) Metab Eng , vol.7 , pp. 18-26
    • Lee, P.C.1    Petri, R.2    Mijts, B.N.3    Watts, K.T.4    Schmidt-Dannert, C.5
  • 27
    • 0029880618 scopus 로고    scopus 로고
    • Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutagenesis
    • Ohnuma S, Nakazawa T, Hemmi H, Hallberg A, Koyama T, Ogura K, Nishino T. Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutagenesis. J Biol Chem 1996;271:10087-10095.
    • (1996) J Biol Chem , vol.271 , pp. 10087-10095
    • Ohnuma, S.1    Nakazawa, T.2    Hemmi, H.3    Hallberg, A.4    Koyama, T.5    Ogura, K.6    Nishino, T.7
  • 29
    • 0024429567 scopus 로고
    • A simple conversion of artemisinic acid into artemisinin
    • Roth R, Acton N. A simple conversion of artemisinic acid into artemisinin. J Nat Prod 1989;52:1183-1185.
    • (1989) J Nat Prod , vol.52 , pp. 1183-1185
    • Roth, R.1    Acton, N.2
  • 32
    • 70349964350 scopus 로고    scopus 로고
    • Automated design of synthetic ribosome binding sites to control protein expression
    • Salis HM, Mirsky EA, Voigt CA. Automated design of synthetic ribosome binding sites to control protein expression. Nat Biotechnol 2009;27:946-950.
    • (2009) Nat Biotechnol , vol.27 , pp. 946-950
    • Salis, H.M.1    Mirsky, E.A.2    Voigt, C.A.3
  • 33
    • 55549116661 scopus 로고    scopus 로고
    • Optimization of the mevalonate-based isoprenoid biosynthetic pathway in Escherichia coli for production of the anti-malarial drug precursor amorpha-4,11-diene
    • Anthony JR, Anthony LC, Nowroozi F, Kwon G, Newman JD, Keasling JD. Optimization of the mevalonate-based isoprenoid biosynthetic pathway in Escherichia coli for production of the anti-malarial drug precursor amorpha-4,11-diene. Metab Eng 2009;11:13-19.
    • (2009) Metab Eng , vol.11 , pp. 13-19
    • Anthony, J.R.1    Anthony, L.C.2    Nowroozi, F.3    Kwon, G.4    Newman, J.D.5    Keasling, J.D.6
  • 34
    • 33747078696 scopus 로고    scopus 로고
    • Combinatorial engineering of intergenic regions in operons tunes expression of multiple genes
    • Pfleger BF, Pitera DJ, Smolke CD, Keasling JD. Combinatorial engineering of intergenic regions in operons tunes expression of multiple genes. Nat Biotechnol 2006;24:1027-1032.
    • (2006) Nat Biotechnol , vol.24 , pp. 1027-1032
    • Pfleger, B.F.1    Pitera, D.J.2    Smolke, C.D.3    Keasling, J.D.4
  • 36
    • 0141794487 scopus 로고    scopus 로고
    • Monoterpene biosynthesis pathway construction in Escherichia coli
    • Carter OA, Peters RJ, Croteau R. Monoterpene biosynthesis pathway construction in Escherichia coli . Phytochemistry 2003;64:425-433.
    • (2003) Phytochemistry , vol.64 , pp. 425-433
    • Carter, O.A.1    Peters, R.J.2    Croteau, R.3
  • 37
    • 34247182988 scopus 로고    scopus 로고
    • Engineering Escherichia coli for production of functionalized terpenoids using plant P450s
    • Chang MCY, Eachus RA, Trieu W, Ro D-K, Keasling JD. Engineering Escherichia coli for production of functionalized terpenoids using plant P450s. Nat Chem Biol 2007;3:274-277.
    • (2007) Nat Chem Biol , vol.3 , pp. 274-277
    • Chang, M.C.Y.1    Eachus, R.A.2    Trieu, W.3    Ro, D.-K.4    Keasling, J.D.5
  • 39
    • 33847378479 scopus 로고    scopus 로고
    • Engineering of the pyruvate dehydrogenase bypass in Saccharomyces cerevisiae for high-level production of isoprenoids
    • Shiba Y, Paradise EM, Kirby J, Ro D, Keasling JD. Engineering of the pyruvate dehydrogenase bypass in Saccharomyces cerevisiae for high-level production of isoprenoids. Metab Eng 2007;9:160-168.
    • (2007) Metab Eng , vol.9 , pp. 160-168
    • Shiba, Y.1    Paradise, E.M.2    Kirby, J.3    Ro, D.4    Keasling, J.D.5
  • 40
    • 57049089897 scopus 로고    scopus 로고
    • Induction of multiple pleiotropic drug resistance genes in yeast engineered to produce an increased level of anti-malarial drug precursor, artemisinic acid
    • Ro D, Ouellet M, Paradise EM, Burd H, Eng D, Paddon CJ, Newman JD, Keasling JD. Induction of multiple pleiotropic drug resistance genes in yeast engineered to produce an increased level of anti-malarial drug precursor, artemisinic acid. BMC Biotechnol 2008;8:83.
    • (2008) BMC Biotechnol , vol.8 , pp. 83
    • Ro, D.1    Ouellet, M.2    Paradise, E.M.3    Burd, H.4    Eng, D.5    Paddon, C.J.6    Newman, J.D.7    Keasling, J.D.8
  • 42
    • 0032403252 scopus 로고    scopus 로고
    • Solvent-tolerant bacteria in biocatalysis
    • de Bont J. Solvent-tolerant bacteria in biocatalysis. Trends Biotechnol 1998;16:493-499.
    • (1998) Trends Biotechnol , vol.16 , pp. 493-499
    • de Bont, J.1
  • 43
    • 68049135724 scopus 로고    scopus 로고
    • Engineering alternative butanol production platforms in heterologous bacteria
    • Nielsen DR, Leonard E, Yoon S, Tseng H, Yuan C, Prather KLJ. Engineering alternative butanol production platforms in heterologous bacteria. Metab Eng 2009;11:262-273.
    • (2009) Metab Eng , vol.11 , pp. 262-273
    • Nielsen, D.R.1    Leonard, E.2    Yoon, S.3    Tseng, H.4    Yuan, C.5    Prather, K.L.J.6
  • 44
    • 33845781663 scopus 로고    scopus 로고
    • Levulinic acid production from wheat straw
    • Chang C, Cen P, Ma X. Levulinic acid production from wheat straw. Bioresour Technol 2007;98:1448-1453.
    • (2007) Bioresour Technol , vol.98 , pp. 1448-1453
    • Chang, C.1    Cen, P.2    Ma, X.3
  • 45
    • 57349161210 scopus 로고    scopus 로고
    • High-titer production of monomeric hydroxyvalerates from levulinic acid in Pseudomonas putida
    • Martin CH, Prather KLJ. High-titer production of monomeric hydroxyvalerates from levulinic acid in Pseudomonas putida. J Biotechnol 2009;139:61-67.
    • (2009) J Biotechnol , vol.139 , pp. 61-67
    • Martin, C.H.1    Prather, K.L.J.2
  • 46
    • 33746520558 scopus 로고    scopus 로고
    • Chemistry and biology of monoterpene indole alkaloid biosynthesis
    • O'Connor SE, Maresh JJ. Chemistry and biology of monoterpene indole alkaloid biosynthesis. Nat Prod Rep 2006;23:532-547.
    • (2006) Nat Prod Rep , vol.23 , pp. 532-547
    • O'Connor, S.E.1    Maresh, J.J.2
  • 48
    • 0028912058 scopus 로고
    • Strictosidine synthase from Catharanthus roseus: purification and characterization of multiple forms
    • deWaal A, Meijer AH, Verpoorte R. Strictosidine synthase from Catharanthus roseus: purification and characterization of multiple forms. Biochem J 1995;306:571-580.
    • (1995) Biochem J , vol.306 , pp. 571-580
    • deWaal, A.1    Meijer, A.H.2    Verpoorte, R.3
  • 49
    • 0024653312 scopus 로고
    • Molecular cloning and analysis of cDNA encoding a plant tryptophan decarboxylase: comparison with animal dopa decarboxylases
    • de Luca V, Marineau C, Brisson N. Molecular cloning and analysis of cDNA encoding a plant tryptophan decarboxylase: comparison with animal dopa decarboxylases. Proc Natl Acad Sci USA 1989;86:2582-2586.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2582-2586
    • de Luca, V.1    Marineau, C.2    Brisson, N.3
  • 50
    • 34547435219 scopus 로고    scopus 로고
    • From scratch to value: engineering Escherichia coli wild type cells to the production of L-phenylalanine and other fine chemicals derived from chorismate
    • Sprenger GA. From scratch to value: engineering Escherichia coli wild type cells to the production of L-phenylalanine and other fine chemicals derived from chorismate. Appl Microbiol Biotechnol 2007;75:739-749.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 739-749
    • Sprenger, G.A.1
  • 51
    • 31144476958 scopus 로고    scopus 로고
    • Towards bacterial strains overproducing L-tryptophan and other aromatics by metabolic engineering
    • Ikeda M. Towards bacterial strains overproducing L-tryptophan and other aromatics by metabolic engineering. Appl Microbiol Biotechnol 2006;69:615-626.
    • (2006) Appl Microbiol Biotechnol , vol.69 , pp. 615-626
    • Ikeda, M.1
  • 53
    • 0034951945 scopus 로고    scopus 로고
    • A metabolic node in action: chorismate-utilizing enzymes in microorganisms
    • Dosselaere F, Vanderleyden J. A metabolic node in action: chorismate-utilizing enzymes in microorganisms. Crit Rev Microbiol 2001;27:75-131.
    • (2001) Crit Rev Microbiol , vol.27 , pp. 75-131
    • Dosselaere, F.1    Vanderleyden, J.2
  • 55
    • 35848961026 scopus 로고    scopus 로고
    • Development of a combined biological and chemical process for production of industrial aromatics from renewable resources
    • Sariaslani FS. Development of a combined biological and chemical process for production of industrial aromatics from renewable resources. Annu Rev Microbiol 2007;61:51-69.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 51-69
    • Sariaslani, F.S.1
  • 56
    • 0011023559 scopus 로고
    • Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor
    • Gunsalus R, Yanofsky C. Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor. Proc Natl Acad Sci USA 1980;77:7117-7121.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7117-7121
    • Gunsalus, R.1    Yanofsky, C.2
  • 58
    • 4344573757 scopus 로고    scopus 로고
    • Metabolic engineering and protein directed evolution increase the yield of Lphenylalanine synthesized from glucose in Escherichia coli
    • Báez-Viveros JL, Osuna J, Hernández-Chávez G, Soberón X, Bolívar F, Gosset G. Metabolic engineering and protein directed evolution increase the yield of Lphenylalanine synthesized from glucose in Escherichia coli . Biotechnol Bioeng 2004;87:516-524.
    • (2004) Biotechnol Bioeng , vol.87 , pp. 516-524
    • Báez-Viveros, J.L.1    Osuna, J.2    Hernández-Chávez, G.3    Soberón, X.4    Bolívar, F.5    Gosset, G.6
  • 59
    • 0030201057 scopus 로고    scopus 로고
    • Improving production of aromatic compounds in Escherichia coli by metabolic engineering
    • Berry A. Improving production of aromatic compounds in Escherichia coli by metabolic engineering. Trends Biotechnol 1996;14:250-256.
    • (1996) Trends Biotechnol , vol.14 , pp. 250-256
    • Berry, A.1
  • 60
    • 33845254128 scopus 로고    scopus 로고
    • Transcriptome analysis in Catharanthus roseus leaves and roots for comparative terpenoid indole alkaloid profiles
    • Shukla AK, Shasany AK, Gupta MM, Khanuja SPS. Transcriptome analysis in Catharanthus roseus leaves and roots for comparative terpenoid indole alkaloid profiles. J Exp Bot 2006;57:3921-3932.
    • (2006) J Exp Bot , vol.57 , pp. 3921-3932
    • Shukla, A.K.1    Shasany, A.K.2    Gupta, M.M.3    Khanuja, S.P.S.4
  • 61
    • 33746339948 scopus 로고    scopus 로고
    • Expressed sequence tags from Madagascar periwinkle (Catharanthus roseus)
    • Murata J, Bienzle D, Brandle JE, Sensen CW, Luca VD. Expressed sequence tags from Madagascar periwinkle (Catharanthus roseus). FEBS Lett 2006;580: 4501-4507.
    • (2006) FEBS Lett , vol.580 , pp. 4501-4507
    • Murata, J.1    Bienzle, D.2    Brandle, J.E.3    Sensen, C.W.4    Luca, V.D.5
  • 63
    • 34548313705 scopus 로고    scopus 로고
    • Metabolic engineering in isoquinoline alkaloid biosynthesis
    • Sato F, Inui T, Takemura T. Metabolic engineering in isoquinoline alkaloid biosynthesis. Curr Pharm Biotechnol 2007;8:211-218.
    • (2007) Curr Pharm Biotechnol , vol.8 , pp. 211-218
    • Sato, F.1    Inui, T.2    Takemura, T.3
  • 65
    • 49949088247 scopus 로고    scopus 로고
    • Production of benzylisoquinoline alkaloids in Saccharomyces cerevisiae
    • Hawkins KM, Smolke CD. Production of benzylisoquinoline alkaloids in Saccharomyces cerevisiae. Nat Chem Biol 2008;4:564-573.
    • (2008) Nat Chem Biol , vol.4 , pp. 564-573
    • Hawkins, K.M.1    Smolke, C.D.2


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