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Volumn 71, Issue 6, 2005, Pages 2962-2969

Metabolic engineering of the phenylpropanoid pathway in saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; ENZYMES; FLUXES; GENES; METABOLISM;

EID: 20444422841     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.6.2962-2969.2005     Document Type: Article
Times cited : (192)

References (39)
  • 1
    • 0011881212 scopus 로고
    • Crystallization and properties of L-phenylalanine ammonia-lyase from Rhodosporidium toruloides
    • Adachi, O., K. Matsushita, E. Shinagawa, and M. Ameyama. 1990. Crystallization and properties of L-phenylalanine ammonia-lyase from Rhodosporidium toruloides. Agric. Biol. Chem. 54:2839-2843.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 2839-2843
    • Adachi, O.1    Matsushita, K.2    Shinagawa, E.3    Ameyama, M.4
  • 2
    • 0001544701 scopus 로고    scopus 로고
    • p-coumaroyltriacetic acid synthase, a new homologue of chalcone synthase, from Hydrangea macrophylla var. thunbergii
    • Akiyama, T., M. Shibuya, H. M. Liu, and Y. Ebizuka. 1999. p-Coumaroyltriacetic acid synthase, a new homologue of chalcone synthase, from Hydrangea macrophylla var. thunbergii. Eur. J. Biochem. 263:834-839.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 834-839
    • Akiyama, T.1    Shibuya, M.2    Liu, H.M.3    Ebizuka, Y.4
  • 4
    • 0034807826 scopus 로고    scopus 로고
    • Dietary agents in cancer prevention: Flavonoids and isoflavonoids
    • Birt, D. F., S. Hendrich, and W. Q. Wang. 2001. Dietary agents in cancer prevention: flavonoids and isoflavonoids. Pharmacol. Ther. 90:157-177.
    • (2001) Pharmacol. Ther. , vol.90 , pp. 157-177
    • Birt, D.F.1    Hendrich, S.2    Wang, W.Q.3
  • 5
    • 0028226498 scopus 로고
    • Pad1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae
    • Clausen, M., C. J. Lamb, R. Megnet, and P. W. Doerner. 1994. Pad1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae. Gene 142:107-112.
    • (1994) Gene , vol.142 , pp. 107-112
    • Clausen, M.1    Lamb, C.J.2    Megnet, R.3    Doerner, P.W.4
  • 6
    • 0004580398 scopus 로고    scopus 로고
    • Flavonoids: Old and new aspects of a class of natural therapeutic drugs
    • Di Carlo, G. D., N. Mascolo, A. A. Izzo, and F. Capasso. 1999. Flavonoids: old and new aspects of a class of natural therapeutic drugs. Life Sci. 65:337-353.
    • (1999) Life Sci. , vol.65 , pp. 337-353
    • Di Carlo, G.D.1    Mascolo, N.2    Izzo, A.A.3    Capasso, F.4
  • 7
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionary divergent classes in angiosperms
    • Ehlting, J., D. Buttner, Q. Wang, C. J. Douglas, I. E. Somssich, and E. Kombrink. 1999. Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionary divergent classes in angiosperms. Plant J. 19:9-20.
    • (1999) Plant J. , vol.19 , pp. 9-20
    • Ehlting, J.1    Buttner, D.2    Wang, Q.3    Douglas, C.J.4    Somssich, I.E.5    Kombrink, E.6
  • 9
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Gietz, R. D., and R. A. Woods. 2002. Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350:87-96.
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 10
    • 0020466394 scopus 로고
    • Genetic and biochemical analysis of the ability of Saccharomyces cerevisiae to decarboxyiate cinnamic acids
    • Goodey, A. R., and R. S. Tubb. 1982. Genetic and biochemical analysis of the ability of Saccharomyces cerevisiae to decarboxyiate cinnamic acids. J. Gen. Microbiol. 128:2615-2620.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 2615-2620
    • Goodey, A.R.1    Tubb, R.S.2
  • 11
    • 0036950350 scopus 로고    scopus 로고
    • Chemoprevention of skin cancer: Current status and future prospects
    • Gupta, S., and H. Mukhtar. 2002. Chemoprevention of skin cancer: current status and future prospects. Cancer Metastasis Rev. 21:363-380.
    • (2002) Cancer Metastasis Rev. , vol.21 , pp. 363-380
    • Gupta, S.1    Mukhtar, H.2
  • 12
  • 13
    • 0034736046 scopus 로고    scopus 로고
    • Advances in flavonoid research since 1992
    • Harborne, J. B., and C. A. Williams. 2000. Advances in flavonoid research since 1992. Phytochemistry 55:481-504.
    • (2000) Phytochemistry , vol.55 , pp. 481-504
    • Harborne, J.B.1    Williams, C.A.2
  • 14
    • 33751391670 scopus 로고
    • Optimization of a quantitative HPLC determination of potentially anticarcinogenic flavonoids in vegetables and fruits
    • Hertog, M. G. L., P. C. H. Hollman, and D. P. Venema. 1992. Optimization of a quantitative HPLC determination of potentially anticarcinogenic flavonoids in vegetables and fruits. J. Agric. Food Chem. 40:1591-1598.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 1591-1598
    • Hertog, M.G.L.1    Hollman, P.C.H.2    Venema, D.P.3
  • 15
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R. M., H. D. Hunt, S. N. Ho, J. K. Pullen, and L. R. Pease. 1989. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 16
    • 0033621061 scopus 로고    scopus 로고
    • New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependent mono-oxygenase
    • Humphreys, J. M., M. R. Hemm, and C. Chapple. 1999. New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependent mono-oxygenase. Proc. Natl. Acad. Sci. USA 96:10045-10050.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10045-10050
    • Humphreys, J.M.1    Hemm, M.R.2    Chapple, C.3
  • 17
    • 0037545559 scopus 로고    scopus 로고
    • Production of plant-specific flavanones by Escherichia coli containing an artificial gene cluster
    • Hwang, E. I., M. Kaneko, Y. Ohnishi, and S. Horinouchi. 2003. Production of plant-specific flavanones by Escherichia coli containing an artificial gene cluster. Appl. Environ. Microbiol. 69:2699-2706.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2699-2706
    • Hwang, E.I.1    Kaneko, M.2    Ohnishi, Y.3    Horinouchi, S.4
  • 18
    • 0035846573 scopus 로고    scopus 로고
    • Structure-guided programming of polyketide chain-length determination in chalcone synthase
    • Jez, J. M., M. E. Bowman, and J. P. Noel. 2001. Structure-guided programming of polyketide chain-length determination in chalcone synthase. Biochemistry 40:14829-14838.
    • (2001) Biochemistry , vol.40 , pp. 14829-14838
    • Jez, J.M.1    Bowman, M.E.2    Noel, J.P.3
  • 19
    • 0942297864 scopus 로고    scopus 로고
    • Optimization of an in vivo plant P450 monooxygenase system in Saccharomyces cerevisiae
    • Jiang, H. X., and J. A. Morgan. 2004. Optimization of an in vivo plant P450 monooxygenase system in Saccharomyces cerevisiae. Biotechnol. Bioeng. 85:130-137.
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 130-137
    • Jiang, H.X.1    Morgan, J.A.2
  • 20
    • 0017747551 scopus 로고
    • 4-Coumarate-CoA ligase from cell suspension cultures of Petroselinum hortense Hoffm. Partial purification, substrate specificity, and further properties
    • Knobloch, K. H., and K. Hahlbrock. 1977. 4-Coumarate-CoA ligase from cell suspension cultures of Petroselinum hortense Hoffm. Partial purification, substrate specificity, and further properties. Arch. Biochem. Biophys. 184:237-248.
    • (1977) Arch. Biochem. Biophys. , vol.184 , pp. 237-248
    • Knobloch, K.H.1    Hahlbrock, K.2
  • 21
    • 0016746473 scopus 로고
    • Enzymatic synthesis of aromatic compounds in higher plants-formation of bis-noryangonin (4-hydroxy-6[4-hydroxystyryl]2-pyrone) from p-coumaroyl-CoA and malonyl-CoA
    • Kreuzaler, F., and K. Hahlbrock. 1975. Enzymatic synthesis of aromatic compounds in higher plants-formation of bis-noryangonin (4-hydroxy-6[4- hydroxystyryl]2-pyrone) from p-coumaroyl-CoA and malonyl-CoA. Arch. Biochem. Biophys. 169:84-90.
    • (1975) Arch. Biochem. Biophys. , vol.169 , pp. 84-90
    • Kreuzaler, F.1    Hahlbrock, K.2
  • 22
    • 0031431501 scopus 로고    scopus 로고
    • Dietary flavonoid and cancer prevention: Evidence and potential mechanism
    • Kuo, S. M. 1997. Dietary flavonoid and cancer prevention: evidence and potential mechanism. Crit. Rev. Oncog. 8:47-69.
    • (1997) Crit. Rev. Oncog. , vol.8 , pp. 47-69
    • Kuo, S.M.1
  • 23
    • 0034784858 scopus 로고    scopus 로고
    • Effect of overexpression of Saccharomyces cerevisiae Pad1p on the resistance to phenylacrylic acids and lignocellulose hydrolysates under aerobic and oxygen-limited conditions
    • Larsson, S., N. O. Nilvebrant, and L. J. Jonsson. 2001. Effect of overexpression of Saccharomyces cerevisiae Pad1p on the resistance to phenylacrylic acids and lignocellulose hydrolysates under aerobic and oxygen-limited conditions. Appl. Microbiol. Biotechnol. 57:167-174.
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 167-174
    • Larsson, S.1    Nilvebrant, N.O.2    Jonsson, L.J.3
  • 24
    • 0036669812 scopus 로고    scopus 로고
    • Cancer preventive effects of flavonoids-a review
    • Le Marchand, L. L. 2002. Cancer preventive effects of flavonoids-a review. Biomed. Pharmacother. 56:296-301.
    • (2002) Biomed. Pharmacother. , vol.56 , pp. 296-301
    • Le Marchand, L.L.1
  • 25
    • 0037742330 scopus 로고    scopus 로고
    • Benzophenone synthase and chalcone synthase from Hypericum androsaemum cell cultures: cDNA cloning, functional expression, and site-directed mutagenesis of two polyketide synthases
    • Liu, B. Y., H. Falkenstein-Paul, W. Schmidt, and L. Beerhues. 2003. Benzophenone synthase and chalcone synthase from Hypericum androsaemum cell cultures: cDNA cloning, functional expression, and site-directed mutagenesis of two polyketide synthases. Plant J. 34:847-855.
    • (2003) Plant J. , vol.34 , pp. 847-855
    • Liu, B.Y.1    Falkenstein-Paul, H.2    Schmidt, W.3    Beerhues, L.4
  • 26
    • 0035001464 scopus 로고    scopus 로고
    • Biological properties of citrus flavonoids pertaining to cancer and inflammation
    • Manthey, J. A., N. Guthrie, and K. Grohmann. 2001. Biological properties of citrus flavonoids pertaining to cancer and inflammation. Curr. Med. Chem. 8:135-153.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 135-153
    • Manthey, J.A.1    Guthrie, N.2    Grohmann, K.3
  • 28
    • 0029776005 scopus 로고    scopus 로고
    • Yeast expression of animal and plant P450s in optimized redox environments
    • Pompon, D., B. Louerat, A. Bronine, and P. Urban. 1996. Yeast expression of animal and plant P450s in optimized redox environments. Methods Enzymol. 272:51-64.
    • (1996) Methods Enzymol. , vol.272 , pp. 51-64
    • Pompon, D.1    Louerat, B.2    Bronine, A.3    Urban, P.4
  • 30
    • 1642576078 scopus 로고    scopus 로고
    • Reconstitution of the entry point of plant phenylpropanoid metabolism in yeast (Saccharomyces cerevisiae)-implications for control of metabolic flux into the phenylpropanoid pathway
    • Ro, D. K., and C. J. Douglas. 2004. Reconstitution of the entry point of plant phenylpropanoid metabolism in yeast (Saccharomyces cerevisiae)- implications for control of metabolic flux into the phenylpropanoid pathway. J. Biol. Chem. 279:2600-2607.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2600-2607
    • Ro, D.K.1    Douglas, C.J.2
  • 31
    • 1842287997 scopus 로고    scopus 로고
    • Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity
    • Rosier, J., F. Krekel, N. Amrhein, and J. Schmid. 1997. Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. Plant Physiol. 113:175-179.
    • (1997) Plant Physiol. , vol.113 , pp. 175-179
    • Rosier, J.1    Krekel, F.2    Amrhein, N.3    Schmid, J.4
  • 32
    • 0036834321 scopus 로고    scopus 로고
    • Molecular characterization of root-specific chalcone synthases from Cassia alata
    • Samappito, S., J. Page, J. Schmidt, W. De-Eknamkul, and T. M. Kutchan. 2002. Molecular characterization of root-specific chalcone synthases from Cassia alata. Planta 216:64-71.
    • (2002) Planta , vol.216 , pp. 64-71
    • Samappito, S.1    Page, J.2    Schmidt, J.3    De-Eknamkul, W.4    Kutchan, T.M.5
  • 33
    • 0035965253 scopus 로고    scopus 로고
    • CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway
    • Schoch, G., S. Goepfert, M. Morant, A. Hehn, D. Meyer, P. Ullmann, and D. Werck-Reichhart. 2001. CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J. Biol. Chem. 276:36566-36574.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36566-36574
    • Schoch, G.1    Goepfert, S.2    Morant, M.3    Hehn, A.4    Meyer, D.5    Ullmann, P.6    Werck-Reichhart, D.7
  • 34
    • 0021099645 scopus 로고
    • Substrate specificity of chalcone synthase from Petroselinum hortense-formation of phloroglucinol derivatives from aliphatic substrates
    • Schuz, R., W. Heller, and K. Hahlbrock. 1983. Substrate specificity of chalcone synthase from Petroselinum hortense-formation of phloroglucinol derivatives from aliphatic substrates. J. Biol. Chem. 258:6730-6734.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6730-6734
    • Schuz, R.1    Heller, W.2    Hahlbrock, K.3
  • 35
    • 0016736883 scopus 로고
    • Chemical syntheses and properties of hydroxycinnamoyl-coenzyme A derivatives
    • Stockigt, J., and M. H. Zenk. 1975. Chemical syntheses and properties of hydroxycinnamoyl-coenzyme A derivatives. Z. Naturforsch. Sect. C 30:352-358.
    • (1975) Z. Naturforsch. Sect. C , vol.30 , pp. 352-358
    • Stockigt, J.1    Zenk, M.H.2
  • 37
    • 3242737570 scopus 로고    scopus 로고
    • Exploring recombinant flavonoid biosynthesis in metabolically engineered Escherichia coli
    • Watts, K. T., P. C. Lee, and C. Schmidt-Dannert. 2004. Exploring recombinant flavonoid biosynthesis in metabolically engineered Escherichia coli. Chembiochem 5:500-507.
    • (2004) Chembiochem , vol.5 , pp. 500-507
    • Watts, K.T.1    Lee, P.C.2    Schmidt-Dannert, C.3
  • 39
    • 0031040101 scopus 로고    scopus 로고
    • Molecular cloning of 4-coumarate: Coenzyme A ligase in loblolly pine and the roles of this enzyme in the biosynthesis of lignin in compression wood
    • Zhang, X. H., and V. L. Chiang. 1997. Molecular cloning of 4-coumarate: coenzyme A ligase in loblolly pine and the roles of this enzyme in the biosynthesis of lignin in compression wood. Plant Physiol. 113:65-74.
    • (1997) Plant Physiol. , vol.113 , pp. 65-74
    • Zhang, X.H.1    Chiang, V.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.