메뉴 건너뛰기




Volumn 6, Issue , 2006, Pages

Biosynthesis of plant-specific stilbene polyketides in metabolically engineered Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CAFFEIC ACID; FERULIC ACID; PHENYLPROPANOIDS; PLANT-SPECIFIC STILBENE POLYKETIDES; TYROSINE KINASES;

EID: 33645779318     PISSN: 14726750     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-6-22     Document Type: Article
Times cited : (179)

References (43)
  • 1
    • 0034349180 scopus 로고    scopus 로고
    • Flavonoids of leguminous plants: Structure, biological activity, and biosynthesis
    • Aoki T, Akashi T, Ayabe S: Flavonoids of leguminous plants: Structure, biological activity, and biosynthesis. J Plant Res 2000, 113(1112):475-488.
    • (2000) J Plant Res , vol.113 , Issue.1112 , pp. 475-488
    • Aoki, T.1    Akashi, T.2    Ayabe, S.3
  • 2
    • 0037899020 scopus 로고    scopus 로고
    • Recent advances in the biosynthesis and accumulation of anthocyanins
    • Springob K, Nakajima J, Yamazaki M, Saito K: Recent advances in the biosynthesis and accumulation of anthocyanins. Nat Prod Rep 2003, 20(3):288-303.
    • (2003) Nat Prod Rep , vol.20 , Issue.3 , pp. 288-303
    • Springob, K.1    Nakajima, J.2    Yamazaki, M.3    Saito, K.4
  • 3
    • 0034736046 scopus 로고    scopus 로고
    • Advances in flavonoid research since 1992
    • Harborne JB, Williams CA: Advances in flavonoid research since 1992. Phytochemistry 2000, 55(6):481-504.
    • (2000) Phytochemistry , vol.55 , Issue.6 , pp. 481-504
    • Harborne, J.B.1    Williams, C.A.2
  • 5
    • 0036820498 scopus 로고    scopus 로고
    • Biological activities of resveratrol and its analogs
    • Wolter F, Stein J: Biological activities of resveratrol and its analogs. Drugs Future 2002, 27(10):949-959.
    • (2002) Drugs Future , vol.27 , Issue.10 , pp. 949-959
    • Wolter, F.1    Stein, J.2
  • 6
    • 0030963473 scopus 로고    scopus 로고
    • Resveratrol: A molecule whose time has come? And gone?
    • Soleas GJ, Diamandis EP, Goldberg DM: Resveratrol: A molecule whose time has come? And gone? Clin Biochem 1997, 30(2):91-113.
    • (1997) Clin Biochem , vol.30 , Issue.2 , pp. 91-113
    • Soleas, G.J.1    Diamandis, E.P.2    Goldberg, D.M.3
  • 10
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT I activation by resveratrol
    • Borra MT, Smith BC, Denu JM: Mechanism of human SIRT I activation by resveratrol. J Biol Chem 2005, 280(17):17187-17195.
    • (2005) J Biol Chem , vol.280 , Issue.17 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 11
    • 0028072499 scopus 로고
    • Inhibition of mast cell Fc epsilon RI-mediated signaling and effector function by the Syk-selective inhibitor, piceatannol
    • Oliver JM, Burg DL, Wilson BS, McLaughlin JL, Geahlen RL: Inhibition of mast cell Fc epsilon RI-mediated signaling and effector function by the Syk-selective inhibitor, piceatannol. J Biol Chem 1994, 269(47):29697-29703.
    • (1994) J Biol Chem , vol.269 , Issue.47 , pp. 29697-29703
    • Oliver, J.M.1    Burg, D.L.2    Wilson, B.S.3    McLaughlin, J.L.4    Geahlen, R.L.5
  • 12
    • 0037072486 scopus 로고    scopus 로고
    • Transcription factors controlling plant secondary metabolism: What regulates the regulators?
    • Vorn Endt D, Kijne JW, Memelink J: Transcription factors controlling plant secondary metabolism: what regulates the regulators? Phytochemistry 2002, 61(2):107-114.
    • (2002) Phytochemistry , vol.61 , Issue.2 , pp. 107-114
    • Vorn Endt, D.1    Kijne, J.W.2    Memelink, J.3
  • 13
    • 0026814012 scopus 로고
    • Molecular analysis of chalcone and dihydropinosylvin synthase from Scots pine (Pinus sylvestris), and differential regulation of these and related enzyme activities in stressed plants
    • Fliegmann J, Schroder G, Schanz S, Britsch L, Schroder J: Molecular analysis of chalcone and dihydropinosylvin synthase from Scots pine (Pinus sylvestris), and differential regulation of these and related enzyme activities in stressed plants. Plant Mol Biol 1992, 18(3):489-503.
    • (1992) Plant Mol Biol , vol.18 , Issue.3 , pp. 489-503
    • Fliegmann, J.1    Schroder, G.2    Schanz, S.3    Britsch, L.4    Schroder, J.5
  • 14
    • 0033791642 scopus 로고    scopus 로고
    • Gene induction of stilbene biosynthesis in Scots pine in response to ozone treatment, wounding, and fungal infection
    • Chiron H, Drouet A, Lieutier F, Payer HD, Ernst D, Sandermann HJ: Gene induction of stilbene biosynthesis in Scots pine in response to ozone treatment, wounding, and fungal infection. Plant Physiol 2000, 124(2):865-872.
    • (2000) Plant Physiol , vol.124 , Issue.2 , pp. 865-872
    • Chiron, H.1    Drouet, A.2    Lieutier, F.3    Payer, H.D.4    Ernst, D.5    Sandermann, H.J.6
  • 15
    • 3242737570 scopus 로고    scopus 로고
    • Exploring recombinant flavonoid biosynthesis in metabolically engineered Escherichia coli
    • Watts KT, Lee PC, Schmidt-Dannert C: Exploring recombinant flavonoid biosynthesis in metabolically engineered Escherichia coli. Chembiochem 2004,5(4):500-507.
    • (2004) Chembiochem , vol.5 , Issue.4 , pp. 500-507
    • Watts, K.T.1    Lee, P.C.2    Schmidt-Dannert, C.3
  • 17
    • 4644270018 scopus 로고    scopus 로고
    • An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketide synthases
    • Austin MB, Bowman ME, Ferrer JL, Schroder J, Noel JP. An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketide synthases. Chem Biol 2004, 11(9):1179-1194.
    • (2004) Chem Biol , vol.11 , Issue.9 , pp. 1179-1194
    • Austin, M.B.1    Bowman, M.E.2    Ferrer, J.L.3    Schroder, J.4    Noel, J.P.5
  • 18
    • 4644250460 scopus 로고    scopus 로고
    • Enzymatic formation of long-chain polyketide pyrones by plant type III polyketide synthases
    • Abe I, Watanabe T, Noguchi H: Enzymatic formation of long-chain polyketide pyrones by plant type III polyketide synthases. Phytochemistry 2004, 65(17):2447-2453.
    • (2004) Phytochemistry , vol.65 , Issue.17 , pp. 2447-2453
    • Abe, I.1    Watanabe, T.2    Noguchi, H.3
  • 19
    • 0034819358 scopus 로고    scopus 로고
    • Novel polyketides synthesized with a higher plant stilbene synthase
    • Morita H, Noguchi H, Schroder J, Abe I: Novel polyketides synthesized with a higher plant stilbene synthase. Eur J Biochem 2001, 268(13):3759-3766.
    • (2001) Eur J Biochem , vol.268 , Issue.13 , pp. 3759-3766
    • Morita, H.1    Noguchi, H.2    Schroder, J.3    Abe, I.4
  • 20
    • 0033941389 scopus 로고    scopus 로고
    • Molecular breeding of carotenoid biosynthetic pathways
    • Schmidt-Dannert C, Umeno D, Arnold FH: Molecular breeding of carotenoid biosynthetic pathways. Nat Biotechnol 2000, 18(7):750-753.
    • (2000) Nat Biotechnol , vol.18 , Issue.7 , pp. 750-753
    • Schmidt-Dannert, C.1    Umeno, D.2    Arnold, F.H.3
  • 21
    • 0024286787 scopus 로고
    • Molecular analysis of resveratrol synthase. cDNA, genomic clones and relationship with chalcone synthase
    • Schroder G, Brown JW, Schroder J: Molecular analysis of resveratrol synthase. cDNA, genomic clones and relationship with chalcone synthase. Eur J Biochem 1988, 172(1):161-169.
    • (1988) Eur J Biochem , vol.172 , Issue.1 , pp. 161-169
    • Schroder, G.1    Brown, J.W.2    Schroder, J.3
  • 23
    • 0030272553 scopus 로고    scopus 로고
    • Optimization of heterologous protein production in Escherichia coli
    • Weickert MJ, Doherty DH, Best EA, Olins PO: Optimization of heterologous protein production in Escherichia coli. Curr Opin Biotech 1996, 7(5):494-499.
    • (1996) Curr Opin Biotech , vol.7 , Issue.5 , pp. 494-499
    • Weickert, M.J.1    Doherty, D.H.2    Best, E.A.3    Olins, P.O.4
  • 24
    • 0037545559 scopus 로고    scopus 로고
    • Production of plant-specific flavanones by Escherichia coli containing an artificial gene cluster
    • Hwang EI, Kaneko M, Ohnishi Y, Horinouchi S: Production of plant-specific flavanones by Escherichia coli containing an artificial gene cluster. Appl Environ Microbial 2003, 69(5):2699-2706.
    • (2003) Appl Environ Microbial , vol.69 , Issue.5 , pp. 2699-2706
    • Hwang, E.I.1    Kaneko, M.2    Ohnishi, Y.3    Horinouchi, S.4
  • 25
  • 26
    • 0032463020 scopus 로고    scopus 로고
    • Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12
    • Diaz E, Ferrandez A, Garcia JL: Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J Bacteriol 1998, 180(11):2915-2923.
    • (1998) J Bacteriol , vol.180 , Issue.11 , pp. 2915-2923
    • Diaz, E.1    Ferrandez, A.2    Garcia, J.L.3
  • 28
    • 0028786298 scopus 로고
    • Cinnamate 4-hydroxylase from Catharanthus roseus, and a strategy for the functional expression of plant cytochrome P450 proteins as translational fusions with P450 reductase in Escherichia coli
    • Hotze M, Schroder G, Schroder J: Cinnamate 4-hydroxylase from Catharanthus roseus, and a strategy for the functional expression of plant cytochrome P450 proteins as translational fusions with P450 reductase in Escherichia coli. FEBS Lett 1995, 374(3):345-350.
    • (1995) FEBS Lett , vol.374 , Issue.3 , pp. 345-350
    • Hotze, M.1    Schroder, G.2    Schroder, J.3
  • 29
    • 0030852872 scopus 로고    scopus 로고
    • Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-Cytochrome P450 reductases with P450 CYP73A5
    • Urban P, Mignotte C, Kazmaier M, Delorme F, Pompon D: Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-Cytochrome P450 reductases with P450 CYP73A5. J Biol Chem 1997, 272(31):19176-19186.
    • (1997) J Biol Chem , vol.272 , Issue.31 , pp. 19176-19186
    • Urban, P.1    Mignotte, C.2    Kazmaier, M.3    Delorme, F.4    Pompon, D.5
  • 30
    • 0034089214 scopus 로고    scopus 로고
    • Bacterial expression and purification of the Arabidopsis NADPH-cytochrome P450 reductase ATR2
    • Hull AK, Celenza JL: Bacterial expression and purification of the Arabidopsis NADPH-cytochrome P450 reductase ATR2. Protein Expres Purif 2000, 18(3):310-315.
    • (2000) Protein Expres Purif , vol.18 , Issue.3 , pp. 310-315
    • Hull, A.K.1    Celenza, J.L.2
  • 31
    • 0021759521 scopus 로고
    • Purification and properties of a stilbene synthase from induced cell suspension cultures of peanut
    • Schoppner A, Kindl H: Purification and properties of a stilbene synthase from induced cell suspension cultures of peanut. J Biol Chem 1984, 259(11):6806-6811.
    • (1984) J Biol Chem , vol.259 , Issue.11 , pp. 6806-6811
    • Schoppner, A.1    Kindl, H.2
  • 32
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate: Coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
    • Ehlting J, Buttner D, Wang Q, Douglas CJ, Somssich IE, Kombrink E: Three 4-coumarate: coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms. Plant J 1999, 19(1):9-20.
    • (1999) Plant J , vol.19 , Issue.1 , pp. 9-20
    • Ehlting, J.1    Buttner, D.2    Wang, Q.3    Douglas, C.J.4    Somssich, I.E.5    Kombrink, E.6
  • 33
    • 1242296765 scopus 로고    scopus 로고
    • The 4-coumarate: CoA ligase gene family in Arabidopsis thaliana comprises one rare, sinapateactivating and three commonly occurring isoenzymes
    • Hamberger B, Hahlbrock K: The 4-coumarate:CoA ligase gene family in Arabidopsis thaliana comprises one rare, sinapateactivating and three commonly occurring isoenzymes. Proc Natl Acad Sci U S A 2004, 101(7):2209-2214.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.7 , pp. 2209-2214
    • Hamberger, B.1    Hahlbrock, K.2
  • 34
    • 0037086137 scopus 로고    scopus 로고
    • Enzymatic synthesis and purification of aromatic coenzyme A esters
    • Beuerle T, Pichersky E: Enzymatic synthesis and purification of aromatic coenzyme A esters. Anal Biochem 2002, 302(2):305-312.
    • (2002) Anal Biochem , vol.302 , Issue.2 , pp. 305-312
    • Beuerle, T.1    Pichersky, E.2
  • 35
    • 0037117475 scopus 로고    scopus 로고
    • Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity
    • Jez JM, Bowman ME, Noel JP: Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity. Proc Natl Acad Sci USA 2002, 99(8):5319-5324.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.8 , pp. 5319-5324
    • Jez, J.M.1    Bowman, M.E.2    Noel, J.P.3
  • 38
    • 0035846573 scopus 로고    scopus 로고
    • Structure-guided programming of polyketide chain-length determination in chalcone synthase
    • Jez JM, Bowman ME, Noel JP: Structure-guided programming of polyketide chain-length determination in chalcone synthase. Biochemistry 2001, 40(49):14829-14838.
    • (2001) Biochemistry , vol.40 , Issue.49 , pp. 14829-14838
    • Jez, J.M.1    Bowman, M.E.2    Noel, J.P.3
  • 39
    • 0034526571 scopus 로고    scopus 로고
    • Structural control of polyketide formation in plant-specific polyketide synthases
    • Jez JM, Austin MB, Ferrer JL, Bowman ME, Schroder J, Noel JP: Structural control of polyketide formation in plant-specific polyketide synthases. Chem Biol 2000, 7(12):919-930.
    • (2000) Chem Biol , vol.7 , Issue.12 , pp. 919-930
    • Jez, J.M.1    Austin, M.B.2    Ferrer, J.L.3    Bowman, M.E.4    Schroder, J.5    Noel, J.P.6
  • 40
    • 0035940995 scopus 로고    scopus 로고
    • Transformation of acridone synthase to chalcone synthase
    • Lukacin R, Schreiner S, Matern U: Transformation of acridone synthase to chalcone synthase. FEBS Lett 2001, 508(3):413-417.
    • (2001) FEBS Lett , vol.508 , Issue.3 , pp. 413-417
    • Lukacin, R.1    Schreiner, S.2    Matern, U.3
  • 41
    • 0028321623 scopus 로고
    • Evidence that stilbene synthases have developed from chalcone synthases several times in the course of evolution
    • Tropf S, Lanz T, Rensing SA, Schroder J, Schroder G: Evidence that stilbene synthases have developed from chalcone synthases several times in the course of evolution. J Mol Evol 1994, 38(6):610-618.
    • (1994) J Mol Evol , vol.38 , Issue.6 , pp. 610-618
    • Tropf, S.1    Lanz, T.2    Rensing, S.A.3    Schroder, J.4    Schroder, G.5
  • 42
    • 0004136246 scopus 로고    scopus 로고
    • Three edition. Cold Spring Harbor, NY, Cold Spring Harbor Laboratory Press
    • Sambrook J: Molecular Cloning - A Laboratory Manual. Volume 3. Three edition. Cold Spring Harbor, NY, Cold Spring Harbor Laboratory Press; 2001.
    • (2001) Molecular Cloning - A Laboratory Manual , vol.3
    • Sambrook, J.1
  • 43
    • 0035216867 scopus 로고    scopus 로고
    • Homogeneous expression of the P(BAD) promoter in Escherichia coli by constitutive expression of the low-affinity high-capacity AraE transporter
    • Khlebnikov A, Datsenko KA, Skaug T, Wanner BL, Keasling JD: Homogeneous expression of the P(BAD) promoter in Escherichia coli by constitutive expression of the low-affinity high-capacity AraE transporter. Microbiology 2001, 147(12):3241-3247.
    • (2001) Microbiology , vol.147 , Issue.12 , pp. 3241-3247
    • Khlebnikov, A.1    Datsenko, K.A.2    Skaug, T.3    Wanner, B.L.4    Keasling, J.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.