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Volumn 22, Issue 15, 2015, Pages 1880-1888

Using strictosidine synthase to prepare novel alkaloids

Author keywords

Alkaloids; Application strategies; Protein engineering; Strictosidine synthase; Substrates; X ray complex structures

Indexed keywords

ALKALOID DERIVATIVE; STRICTOSIDINE; STRICTOSIDINE SYNTHASE; UNCLASSIFIED DRUG;

EID: 84931287736     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/0929867322666150408110919     Document Type: Article
Times cited : (20)

References (58)
  • 1
    • 33645377497 scopus 로고    scopus 로고
    • Structure-based development of target-specific compound libraries
    • Orry, A. J. W.; Abagyan, R. A.; Cavasotto, C. N. Structure-based development of target-specific compound libraries. Drug Discov. Today, 2006, 11(5/6), 261-266.
    • (2006) Drug Discov. Today , vol.11 , Issue.5-6 , pp. 261-266
    • Orry, A.J.W.1    Abagyan, R.A.2    Cavasotto, C.N.3
  • 2
    • 79955857749 scopus 로고    scopus 로고
    • Compound acquisition and prioritization algorithm for constructing structurally disverse compound libraries
    • Ma, C.; Lazo, J. S.; Xie, X. Q. Compound acquisition and prioritization algorithm for constructing structurally disverse compound libraries. ACS Comb. Sci., 2011, 13(3), 223-231.
    • (2011) ACS Comb. Sci. , vol.13 , Issue.3 , pp. 223-231
    • Ma, C.1    Lazo, J.S.2    Xie, X.Q.3
  • 3
    • 79955027927 scopus 로고    scopus 로고
    • Global assessment of scaffold hopping potential for current pharmaceutical targets
    • Hu, Y.; Bajorath, J. Global assessment of scaffold hopping potential for current pharmaceutical targets. Med. Chem. Comm., 2010, 1(5), 339-344.
    • (2010) Med. Chem. Comm. , vol.1 , Issue.5 , pp. 339-344
    • Hu, Y.1    Bajorath, J.2
  • 4
    • 84894434782 scopus 로고    scopus 로고
    • Automated modular synthesis of aptamer-drug conjugates for targeted drug delivery. J
    • Wang, R.; Zhu, G.; Mei, L.; Xie, Y.; Ma, H.; Ye, M.; Qing, F.; Tan, W. Automated modular synthesis of aptamer-drug conjugates for targeted drug delivery. J. Am. Chem. Soc., 2014, 136(7), 2731-2734.
    • (2014) Am. Chem. Soc. , vol.136 , Issue.7 , pp. 2731-2734
    • Wang, R.1    Zhu, G.2    Mei, L.3    Xie, Y.4    Ma, H.5    Ye, M.6    Qing, F.7    Tan, W.8
  • 5
    • 84870921311 scopus 로고    scopus 로고
    • The use of enzymes in organic synthesis and the life sciences: Perspectives from the Swiss Industrial Biocatalysis Consortium (SIBC). Catal
    • Meyer, H. P.; Eichhorn, E.; Hanlon, S.; Lutz, S.; Schurmann, M.; Wohlgemuth, R.; Coppolecchia, R. The use of enzymes in organic synthesis and the life sciences: perspectives from the Swiss Industrial Biocatalysis Consortium (SIBC). Catal. Sci. Technol., 2013, 3(1), 29-40.
    • (2013) Sci. Technol. , vol.3 , Issue.1 , pp. 29-40
    • Meyer, H.P.1    Eichhorn, E.2    Hanlon, S.3    Lutz, S.4    Schurmann, M.5    Wohlgemuth, R.6    Coppolecchia, R.7
  • 6
    • 37049108698 scopus 로고
    • Strictosidine (isovincoside): The key intermediate in the biosynthesis of monoterpenoid indole alkaloids. J
    • Stockigt, J.; Zenk, M. H. Strictosidine (isovincoside): The key intermediate in the biosynthesis of monoterpenoid indole alkaloids. J. Chem. Soc. Chem. Commun. 1977, (18), 646-648.
    • (1977) Chem. Soc. Chem. Commun. , Issue.18 , pp. 646-648
    • Stockigt, J.1    Zenk, M.H.2
  • 7
    • 0017380542 scopus 로고
    • Strictosidine (isovincoside): The key intermediate in the enzymatic formation of indole alkaloids
    • Stockigt, J.; Zenk, M. H. Strictosidine (isovincoside): The key intermediate in the enzymatic formation of indole alkaloids. FEBS Lett. 1977, 79(2), 233-237.
    • (1977) FEBS Lett. , vol.79 , Issue.2 , pp. 233-237
    • Stockigt, J.1    Zenk, M.H.2
  • 8
    • 37049104714 scopus 로고
    • The biosynthesis of monoterpenoid indole alkaloids from strictosidine
    • Nagakura, N.; Rueffer, M.; Zenk, M. H. The biosynthesis of monoterpenoid indole alkaloids from strictosidine. J. Chem. Soc. Perkin Trans. 1, 1979, 2308-2312.
    • (1979) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 2308-2312
    • Nagakura, N.1    Rueffer, M.2    Zenk, M.H.3
  • 9
    • 0025316477 scopus 로고
    • Brain uptake and anticancer activities of vincristine and vinblastine are restricted by their low cerebrovascular permeability and binding to plasma constituents in rat
    • Greig, N. H.; Soncrant, T. T.; Shetty, H. U.; Momma, S.; Smith, Q. R.; Rapoprt, S. I. Brain uptake and anticancer activities of vincristine and vinblastine are restricted by their low cerebrovascular permeability and binding to plasma constituents in rat. Cancer Chemother. Pharmacol., 1990, 26(4), 263-268.
    • (1990) Cancer Chemother. Pharmacol. , vol.26 , Issue.4 , pp. 263-268
    • Greig, N.H.1    Soncrant, T.T.2    Shetty, H.U.3    Momma, S.4    Smith, Q.R.5    Rapoprt, S.I.6
  • 10
    • 0000868239 scopus 로고
    • Homogeneous strictosidine synthase from cell suspension cultures of Rauwolfia serpentina
    • Hampp, N.; Zenk, M. H. Homogeneous strictosidine synthase from cell suspension cultures of Rauwolfia serpentina. Phytochemistry 1988, 27(12), 3811-3815.
    • (1988) Phytochemistry , vol.27 , Issue.12 , pp. 3811-3815
    • Hampp, N.1    Zenk, M.H.2
  • 11
    • 0003040198 scopus 로고
    • Purification and characterization of strictosidine synthase from a suspension culture of Cinchona robusta
    • Stevens, L. H.; Giroud, C.; Pennings, E. J. M.; Verpoorte, R. Purification and characterization of strictosidine synthase from a suspension culture of Cinchona robusta. Phytochemistry. 1993, 33(1), 99-106.
    • (1993) Phytochemistry. , vol.33 , Issue.1 , pp. 99-106
    • Stevens, L.H.1    Giroud, C.2    Pennings, E.J.M.3    Verpoorte, R.4
  • 13
    • 0037657891 scopus 로고    scopus 로고
    • Camptothecin biosynthetic genes in hairy roots of Ophiorrhiza pumila: Cloning, characterization and differential expression in tissues and by stress compounds
    • Yamazaki, Y.; Sudo, H.; Yamazaki, M.; Aimi, N.; Saito, K. Camptothecin biosynthetic genes in hairy roots of Ophiorrhiza pumila: cloning, characterization and differential expression in tissues and by stress compounds. Plant Cell Physiol. 2003, 44(4), 395-403.
    • (2003) Plant Cell Physiol. , vol.44 , Issue.4 , pp. 395-403
    • Yamazaki, Y.1    Sudo, H.2    Yamazaki, M.3    Aimi, N.4    Saito, K.5
  • 14
    • 68149157985 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of a new cDNA encoding strictosidine synthase from Ophiorrhiza japonica
    • Lu, Y.; Wang, H.; Wang, W.; Qian, Z.; Li, L.; Wang, J.; Zhou, G.; Kai, G. Molecular characterization and expression analysis of a new cDNA encoding strictosidine synthase from Ophiorrhiza japonica. Mol. Biol. Rep. 2009, 36(7), 1845-1852.
    • (2009) Mol. Biol. Rep. , vol.36 , Issue.7 , pp. 1845-1852
    • Lu, Y.1    Wang, H.2    Wang, W.3    Qian, Z.4    Li, L.5    Wang, J.6    Zhou, G.7    Kai, G.8
  • 15
    • 40849134104 scopus 로고    scopus 로고
    • 3D-Structure and function of strictosidine synthase-The key enzyme of monoterpenoid indole alkaloid biosynthesis
    • Stockigt, J.; Barleben, L.; Panjikar, S.; Loris, E. A. 3D-Structure and function of strictosidine synthase-the key enzyme of monoterpenoid indole alkaloid biosynthesis. Plant Physiol. Biochem., 2008, 46(3), 340-355.
    • (2008) Plant Physiol. Biochem. , vol.46 , Issue.3 , pp. 340-355
    • Stockigt, J.1    Barleben, L.2    Panjikar, S.3    Loris, E.A.4
  • 16
    • 0024285106 scopus 로고
    • The cDNA clone for strictosidine synthase from Rauvolfia serpentina
    • Kutchan, T. M.; Hampp, N.; Lottspeich, F.; Beyreuther, K.; Zenk, M. H. The cDNA clone for strictosidine synthase from Rauvolfia serpentina. FEBS Lett. 1988, 237(1/2), 40-44.
    • (1988) FEBS Lett. , vol.237 , Issue.1-2 , pp. 40-44
    • Kutchan, T.M.1    Hampp, N.2    Lottspeich, F.3    Beyreuther, K.4    Zenk, M.H.5
  • 17
    • 0024977242 scopus 로고
    • Expression of enzymatically active cloned strictosidine synthase from the higher plant Rauvolfia serpentina in Escherichia coli
    • Kutchan, T. M. Expression of enzymatically active cloned strictosidine synthase from the higher plant Rauvolfia serpentina in Escherichia coli. FEBS Lett. 1989, 257(1), 127-130.
    • (1989) FEBS Lett. , vol.257 , Issue.1 , pp. 127-130
    • Kutchan, T.M.1
  • 18
    • 0010426474 scopus 로고
    • Isolation and immobilization of strictosidine synthase
    • Pfitzner, U.; Zenk, M. H. Isolation and immobilization of strictosidine synthase. Methods Enzymol., 1987, 136, 342-350.
    • (1987) Methods Enzymol. , vol.136 , pp. 342-350
    • Pfitzner, U.1    Zenk, M.H.2
  • 20
    • 0025878733 scopus 로고
    • Enzymology and molecular biology of alkaloid biosynthesis
    • Kutchan, T. M.; Dittrich, H.; Bracher, D. Enzymology and molecular biology of alkaloid biosynthesis. Tetrahedron., 1991, 47(31), 5945-5954.
    • (1991) Tetrahedron. , vol.47 , Issue.31 , pp. 5945-5954
    • Kutchan, T.M.1    Dittrich, H.2    Bracher, D.3
  • 21
    • 33746520558 scopus 로고    scopus 로고
    • Chemistry and biology of monoterpene indole alkaloid biosynthesis
    • O'Connor, S. E.; Maresh, J. J. Chemistry and biology of monoterpene indole alkaloid biosynthesis. Nat. Prod. Rep. 2006, 23(4), 532-547.
    • (2006) Nat. Prod. Rep. , vol.23 , Issue.4 , pp. 532-547
    • O'connor, S.E.1    Maresh, J.J.2
  • 22
    • 36548999354 scopus 로고    scopus 로고
    • Evolution and current status of the phytochemistry of nitrogenous compounds
    • Zenk, M. H.; Juenger, M. Evolution and current status of the phytochemistry of nitrogenous compounds. Phytochemistry. 2007, 68(22/24), 2757-2772.
    • (2007) Phytochemistry. , vol.68 , Issue.22-24 , pp. 2757-2772
    • Zenk, M.H.1    Juenger, M.2
  • 24
    • 84866478822 scopus 로고    scopus 로고
    • Discovery and functional analysis of monoterpenoid indole alkaloid pathways in plants
    • De Luca, V.; Salim, V.; Levac, D.; Atsumi, S. M.; Yu, F. Discovery and functional analysis of monoterpenoid indole alkaloid pathways in plants. Methods Enzymol. 2012, 515, 207-229.
    • (2012) Methods Enzymol. , vol.515 , pp. 207-229
    • De Luca, V.1    Salim, V.2    Levac, D.3    Atsumi, S.M.4    Yu, F.5
  • 25
    • 4644304290 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: The first example of a novel enzyme family
    • Ma, X.; Koepke, J.; Fritzsch, G.; Diem, R.; Kutchan, T. M.; Michel, H.; Stockigt, J. Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: The first example of a novel enzyme family. Biochim. Biophys. Acta., 2004, 1702(1), 121-124.
    • (2004) Biochim. Biophys. Acta. , vol.1702 , Issue.1 , pp. 121-124
    • Ma, X.1    Koepke, J.2    Fritzsch, G.3    Diem, R.4    Kutchan, T.M.5    Michel, H.6    Stockigt, J.7
  • 26
    • 33745473834 scopus 로고    scopus 로고
    • The structure of Rauvolfia serpentina strictosidine synthase is a novel six-bladed beta-propeller fold in plant proteins
    • Ma, X.; Panjikar, S.; Koepke, J.; Loris, E; Stockigt, J. The structure of Rauvolfia serpentina strictosidine synthase is a novel six-bladed beta-propeller fold in plant proteins. Plant Cell, 2006, 18(4), 907-920.
    • (2006) Plant Cell , vol.18 , Issue.4 , pp. 907-920
    • Ma, X.1    Panjikar, S.2    Koepke, J.3    Loris, E.4    Stockigt, J.5
  • 27
    • 34548694786 scopus 로고    scopus 로고
    • Structure-based engineering of strictosidine synthase: Auxiliary for alkaloid libraries
    • Loris, E.; Panjikar, S.; Ruppert, M.; Barleben, L.; Unger, M.; Schuebel, H.; Stockigt, J. Structure-based engineering of strictosidine synthase: Auxiliary for alkaloid libraries. Chem. Biol., 2007, 14(9), 979-985.
    • (2007) Chem. Biol. , vol.14 , Issue.9 , pp. 979-985
    • Loris, E.1    Panjikar, S.2    Ruppert, M.3    Barleben, L.4    Unger, M.5    Schuebel, H.6    Stockigt, J.7
  • 28
    • 0018536719 scopus 로고
    • Purification and properties of strictosidine synthase, the key enzyme in indole alkaloid formation
    • Treimer, J. F.; Zenk M. H. Purification and properties of strictosidine synthase, the key enzyme in indole alkaloid formation. Eur. J. Biochem. 1979, 101(1), 225-233.
    • (1979) Eur. J. Biochem. , vol.101 , Issue.1 , pp. 225-233
    • Treimer, J.F.1    Zenk, M.H.2
  • 29
    • 33644990230 scopus 로고    scopus 로고
    • Substrate specificity of strictosidine synthase
    • McCoy, E.; Galan, M. C.; O'Connor, S. E. Substrate specificity of strictosidine synthase. Bioorg. Med. Chem. Lett. 2006, 16(9), 2475-2478.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , Issue.9 , pp. 2475-2478
    • McCoy, E.1    Galan, M.C.2    O'connor, S.E.3
  • 30
    • 84863011696 scopus 로고    scopus 로고
    • Scaffold tailoring by a newly detected pictet-spenglerase activity of strictosidine synthase: From the common tryptoline skeleton to the rare piperazino-indole framework
    • Wu, F.; Zhu, H.; Sun, L.; Rajendran, C.; Wang, M.; Ren, X. Panjikar, S.; Cherkasov, A.; Zou, H.; Stockigt, J. Scaffold tailoring by a newly detected pictet-spenglerase activity of strictosidine synthase: from the common tryptoline skeleton to the rare piperazino-indole framework. J. Am. Chem. Soc., 2012, 134(3), 1498-1500.
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.3 , pp. 1498-1500
    • Wu, F.1    Zhu, H.2    Sun, L.3    Rajendran, C.4    Wang, M.5    Ren Panjikar, X.S.6    Cherkasov, A.7    Zou, H.8    Stockigt, J.9
  • 31
    • 34547927914 scopus 로고    scopus 로고
    • Rapid identification of enzyme variants for reengineered alkaloid biosynthesis in periwinkle
    • Bernhardt, P.; McCoy, E.; O'Connor, S. E. Rapid identification of enzyme variants for reengineered alkaloid biosynthesis in periwinkle. Chem. Biol., 2007, 14(8), 888-897.
    • (2007) Chem. Biol. , vol.14 , Issue.8 , pp. 888-897
    • Bernhardt, P.1    McCoy, E.2    O'connor, S.E.3
  • 32
    • 84893415560 scopus 로고    scopus 로고
    • Halogen bond: Its role beyond drug-target binding affinity for drug discovery and development. J
    • Xu, Z.; Yang Z.; Liu Y.; Lu, Y.; Chen, K.; Zhu, W. Halogen bond: its role beyond drug-target binding affinity for drug discovery and development. J. Chem. Inf. Model., 2014, 54(1), 69-78.
    • (2014) Chem. Inf. Model. , vol.54 , Issue.1 , pp. 69-78
    • Xu, Z.1    Yang, Z.2    Liu, Y.3    Lu, Y.4    Chen, K.5    Zhu, W.6
  • 33
    • 60249093108 scopus 로고    scopus 로고
    • Metabolic reprogramming of periwinkle plant culture
    • Runguphan, W.; O'Connor, S. E. Metabolic reprogramming of periwinkle plant culture. Nat. Chem. Biol., 2009, 5(3), 151-153.
    • (2009) Nat. Chem. Biol. , vol.5 , Issue.3 , pp. 151-153
    • Runguphan, W.1    O'connor, S.E.2
  • 34
    • 69549086898 scopus 로고    scopus 로고
    • Silencing of tryptamine biosynthesis for production of unnatural alkaloids in plant culture
    • Runguphan, W.; Maresh J. J., O'Connor, S. E. Silencing of tryptamine biosynthesis for production of unnatural alkaloids in plant culture. Proc. Natl. Acad. Sci. USA, 2009, 106(33), 13673-13678.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , Issue.33 , pp. 13673-13678
    • Runguphan, W.1    Maresh, J.J.2    O'connor, S.E.3
  • 35
    • 33751009100 scopus 로고    scopus 로고
    • Redesign of a central enzyme in alkaloid biosynthesis
    • Chen, S.; Galan, M. C.; Coltharp, C.; O'Connor, S. E. Redesign of a central enzyme in alkaloid biosynthesis. Chem. Biol., 2006, 13(11), 1137-1141.
    • (2006) Chem. Biol. , vol.13 , Issue.11 , pp. 1137-1141
    • Chen, S.1    Galan, M.C.2    Coltharp, C.3    O'connor, S.E.4
  • 36
    • 0019127129 scopus 로고
    • Enzymatic synthesis of ajmalicine and related indole alkaloids
    • Zenk, M. H. Enzymatic synthesis of ajmalicine and related indole alkaloids. J. Nat. Prod., 1980, 43(4), 438-451.
    • (1980) J. Nat. Prod. , vol.43 , Issue.4 , pp. 438-451
    • Zenk, M.H.1
  • 37
    • 35748962318 scopus 로고    scopus 로고
    • Molecular architecture of strictosidine glucosidase: The gateway to the biosynthesis of the monoterpenoid indole alkaloid family
    • Barleben, L.; Panjikar, S.; Ruppert, M.; Koepke, J.; Stockigt, J. Molecular architecture of strictosidine glucosidase: The gateway to the biosynthesis of the monoterpenoid indole alkaloid family. Plant Cell, 2007, 19(9), 2886-2897.
    • (2007) Plant Cell , vol.19 , Issue.9 , pp. 2886-2897
    • Barleben, L.1    Panjikar, S.2    Ruppert, M.3    Koepke, J.4    Stockigt, J.5
  • 38
    • 78349231666 scopus 로고    scopus 로고
    • A facile chemoenzymatic approach: One-step syntheses of monoterpenoid indole alkaloids
    • Zou. H.; Zhu, H.; Zhang, L.; Yang, L.; Yu, Y.; Stockigt, J. A facile chemoenzymatic approach: one-step syntheses of monoterpenoid indole alkaloids. Chem. Asian. J., 2010, 5(11), 2400-2404.
    • (2010) Chem. Asian. J. , vol.5 , Issue.11 , pp. 2400-2404
    • Zou, H.1    Zhu, H.2    Zhang, L.3    Yang, L.4    Yu, Y.5    Stockigt, J.6
  • 39
    • 0001370591 scopus 로고
    • Enzymatic formation of intermediates in the biosynthesis of ajmaline: Strictosidine and cathenamine
    • Stockigt, J. Enzymatic formation of intermediates in the biosynthesis of ajmaline: Strictosidine and cathenamine. Phytochemistry, 1979, 18, 965-971.
    • (1979) Phytochemistry , vol.18 , pp. 965-971
    • Stockigt, J.1
  • 40
    • 0032726417 scopus 로고    scopus 로고
    • Configurative correlation and conformational analysis of strictosidine and vincoside derivatives. J
    • Patthy-Lukats, A.; Kocsis, A.; Szabo, L. F.; Podanyi, B. Configurative correlation and conformational analysis of strictosidine and vincoside derivatives. J. Nat. Prod., 1999, 62(11), 1492-1499.
    • (1999) Nat. Prod. , vol.62 , Issue.11 , pp. 1492-1499
    • Patthy-Lukats, A.1    Kocsis, A.2    Szabo, L.F.3    Podanyi, B.4
  • 41
  • 42
    • 0023747588 scopus 로고
    • A concise strategy for the syntheses of indole alkaloids of the heteroyohimboid and corynantheioid families. Total syntheses of (. .)-tetrahydroalstonine, (. .)-cathenamine and (. .)-geissoschizine
    • Martin, S. F.; Benage, B.; Hunter, J. E. A concise strategy for the syntheses of indole alkaloids of the heteroyohimboid and corynantheioid families. Total syntheses of (. .)-tetrahydroalstonine, (. .)-cathenamine and (. .)-geissoschizine. J. Am. Chem. Soc., 1988, 110(17), 5925-5927.
    • (1988) J. Am. Chem. Soc. , vol.110 , Issue.17 , pp. 5925-5927
    • Martin, S.F.1    Benage, B.2    Hunter, J.E.3
  • 43
    • 80052483777 scopus 로고    scopus 로고
    • The pictetspengler reaction in nature and in organic chemistry
    • Stockigt. J.; Antonchick, A. P.; Wu, F.; Waldmann, H. The pictetspengler reaction in nature and in organic chemistry. Angew. Chem. Int. Ed., 2011, 50(37), 8538-8546.
    • (2011) Angew. Chem. Int. Ed. , vol.50 , Issue.37 , pp. 8538-8546
    • Stockigt, J.1    Antonchick, A.P.2    Wu, F.3    Waldmann, H.4
  • 46
    • 49949088247 scopus 로고    scopus 로고
    • Production of benzylisoquinoline alkaloids in Sacharomyces cerevisiae
    • Hawkins, K. M.; Smolke, C. D. Production of benzylisoquinoline alkaloids in Sacharomyces cerevisiae. Nat. Chem. Biol., 2008, 4(9), 564-573.
    • (2008) Nat. Chem. Biol. , vol.4 , Issue.9 , pp. 564-573
    • Hawkins, K.M.1    Smolke, C.D.2
  • 47
    • 84857048835 scopus 로고    scopus 로고
    • Advancing secondary metabolite biosynthesis in yeast with synthetic biology tools
    • Siddiqui, M. S.; Thodey, K.; Trenchard, I.; Smolke, C. D. Advancing secondary metabolite biosynthesis in yeast with synthetic biology tools. FEMS Yeast Res, 2012, 12(2), 144-170.
    • (2012) FEMS Yeast Res , vol.12 , Issue.2 , pp. 144-170
    • Siddiqui, M.S.1    Thodey, K.2    Trenchard, I.3    Smolke, C.D.4
  • 48
    • 84922067763 scopus 로고    scopus 로고
    • A microbial biomanufacturing platform for natural and semisynthetic opioids
    • Thodey, K.; Galanie, S.; Smolke, C. D. A microbial biomanufacturing platform for natural and semisynthetic opioids. Nat. Chem. Biol., 2014, 10(10), 837-844.
    • (2014) Nat. Chem. Biol. , vol.10 , Issue.10 , pp. 837-844
    • Thodey, K.1    Galanie, S.2    Smolke, C.D.3
  • 49
    • 84949177207 scopus 로고    scopus 로고
    • Metabolic engineering and synthetic biology for the production of isoquinoline alkaloids
    • Chandra, S.; Lata, H.; Varma, A. Eds. Springer: Berlin, Heidelberg
    • Chow, Y.-L.;Sato, F. Metabolic engineering and synthetic biology for the production of isoquinoline alkaloids. In: Chandra, S.; Lata, H.; Varma, A. Eds. Biotechnology for Medicinal Plants. Springer: Berlin, Heidelberg, 2013, pp. 327-343.
    • (2013) Biotechnology for Medicinal Plants , pp. 327-343
    • Chow, Y.-L.1    Sato, F.2
  • 50
    • 6444243887 scopus 로고    scopus 로고
    • Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis
    • Samanani, N.; Liscombe, D. K.; Facchini, P. J. Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis. Plant J. 2004, 40(2), 302-313.
    • (2004) Plant J. , vol.40 , Issue.2 , pp. 302-313
    • Samanani, N.1    Liscombe, D.K.2    Facchini, P.J.3
  • 51
    • 0028874083 scopus 로고
    • Alkaloid biosynthesis-The basis for metabolic engineering of medicinal plants
    • Kutchan, T. M. Alkaloid biosynthesis-the basis for metabolic engineering of medicinal plants. Plant Cell. 1995, 7(7), 1059-1070.
    • (1995) Plant Cell. , vol.7 , Issue.7 , pp. 1059-1070
    • Kutchan, T.M.1
  • 52
    • 84866489051 scopus 로고    scopus 로고
    • Strategies for engineering plant natural products: The iridoid-derived monoterpene indole alkaloids of Catharanthus roseus
    • O'Connor, S. E. Strategies for engineering plant natural products: The iridoid-derived monoterpene indole alkaloids of Catharanthus roseus. Methods Enzymol. 2012, 515, 189-206.
    • (2012) Methods Enzymol. , vol.515 , pp. 189-206
    • O'Connor, S.E.1
  • 53
    • 84874992963 scopus 로고    scopus 로고
    • Recent progress in the metabolic engineering of alkaloids in plant systems
    • Glenn, W. S.; Runguphan, W.; O'Connor, S. E. Recent progress in the metabolic engineering of alkaloids in plant systems. Curr. Opin. Biotechnol., 2013, 24(2), 354-365.
    • (2013) Curr. Opin. Biotechnol. , vol.24 , Issue.2 , pp. 354-365
    • Glenn, W.S.1    Runguphan, W.2    O'Connor, S.E.3
  • 55
    • 78549294465 scopus 로고    scopus 로고
    • Integrating carbonhalogen bond formation into medicinal plant metabolism
    • Runguphan, W.; Qu, X.; O'Connor, S. E. Integrating carbonhalogen bond formation into medicinal plant metabolism. Nature. 2010, 468(7322), 461-464.
    • (2010) Nature. , vol.468 , Issue.7322 , pp. 461-464
    • Runguphan, W.1    Qu, X.2    O'connor, S.E.3


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