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Volumn 2011, Issue 7, 2011, Pages 41-53

Evolutionary implications and physicochemical analyses of selected proteins of type iii polyketide synthase family

Author keywords

Chalcone synthase; CHS; Molecular phylogeny; Non CHS; PKS; Type III polyketide synthase

Indexed keywords

POLYKETIDE SYNTHASE; TYPE III POLYKETIDE SYNTHASE; UNCLASSIFIED DRUG;

EID: 79958825490     PISSN: None     EISSN: 11769343     Source Type: Journal    
DOI: 10.4137/EBO.S6854     Document Type: Article
Times cited : (17)

References (57)
  • 1
    • 34250743243 scopus 로고    scopus 로고
    • A comprehensive and engaging overview of the type III family of polyketide synthases
    • Watanabe K, Praseuth AP, Wang CCC. A comprehensive and engaging overview of the type III family of polyketide synthases. Curr Opin Chem Biol. 2007;11(3):279-86.
    • (2007) Curr Opin Chem Biol , vol.11 , Issue.3 , pp. 279-286
    • Watanabe, K.1    Praseuth, A.P.2    Wang, C.C.C.3
  • 2
    • 0034979805 scopus 로고    scopus 로고
    • Flavonoid biosynthesis. A colorful model for genetics, biochemistry, cell biology, and biotechnology
    • Winkel-Shirley B. Flavonoid biosynthesis. A colorful model for genetics, biochemistry, cell biology, and biotechnology. Plant Physiol. 2001;126:485-93.
    • (2001) Plant Physiol , vol.126 , pp. 485-493
    • Winkel-Shirley, B.1
  • 3
    • 0037319699 scopus 로고    scopus 로고
    • The chalcone synthase superfamily of type III polyketide synthases
    • Austin MB, Noel JP. The chalcone synthase superfamily of type III polyketide synthases. Nat Prod Rep. 2003;20:79-110.
    • (2003) Nat Prod Rep , vol.20 , pp. 79-110
    • Austin, M.B.1    Noel, J.P.2
  • 4
    • 34250105014 scopus 로고
    • The chalcone synthase multigene family of Petunia hybrida (V30) Sequence homology, chromosomal location and evolutionary aspects
    • Koes RE, Spelt CE, Mol JNM, Geratas AGM. The chalcone synthase multigene family of Petunia hybrida (V30) Sequence homology, chromosomal location and evolutionary aspects. Plant Mol Biol. 1987;10:375-85.
    • (1987) Plant Mol Biol , vol.10 , pp. 375-385
    • Koes, R.E.1    Spelt, C.E.2    Mol, J.N.M.3    Geratas, A.G.M.4
  • 5
    • 0023505583 scopus 로고
    • Organisation and differential activation of a gene family encoding the plant defense enzyme CHS in Phaseolus vulgaris
    • Ryder TB, Hedrick SA, Bell JN, Liang X, Clouse SD, Lamb CJ. Organisation and differential activation of a gene family encoding the plant defense enzyme CHS in Phaseolus vulgaris. Mol Gen Genet. 1987;210:219-33.
    • (1987) Mol Gen Genet , vol.210 , pp. 219-233
    • Ryder, T.B.1    Hedrick, S.A.2    Bell, J.N.3    Liang, X.4    Clouse, S.D.5    Lamb, C.J.6
  • 6
    • 75649150453 scopus 로고    scopus 로고
    • Molecular Characterization of Novel form of Type III Polyketide Synthase from Zingiber Officinale Rosc. and its Analysis using Bioinformatics Method
    • Radhakrishnan EK, Sivakumar KC, Soniya EV. Molecular Characterization of Novel form of Type III Polyketide Synthase from Zingiber Officinale Rosc. and its Analysis using Bioinformatics Method. J Proteomics Bioinform. 2009;2:310-5.
    • (2009) J Proteomics Bioinform , vol.2 , pp. 310-315
    • Radhakrishnan, E.K.1    Sivakumar, K.C.2    Soniya, E.V.3
  • 7
    • 0031561513 scopus 로고    scopus 로고
    • Cancer chemopreventive activity of resveratrol, a natural product derived from grapes
    • Jang M, Cai L, Udeani GO, et al. Cancer chemopreventive activity of resveratrol, a natural product derived from grapes. Science. 1997;275(5297):218-20.
    • (1997) Science , vol.275 , Issue.5297 , pp. 218-220
    • Jang, M.1    Cai, L.2    Udeani, G.O.3
  • 8
    • 0345566753 scopus 로고    scopus 로고
    • Chemopreventive Agent Resveratrol, a Natural Product Derived From Grapes, Triggers CD95 Signaling-Dependent Apoptosis in Human Tumor Cells
    • Clement MV, Hirpara JL, Chawdhury SH, Pervaiz S. Chemopreventive Agent Resveratrol, a Natural Product Derived From Grapes, Triggers CD95 Signaling-Dependent Apoptosis in Human Tumor Cells. Blood. 1998;92(3):996-1002.
    • (1998) Blood , vol.92 , Issue.3 , pp. 996-1002
    • Clement, M.V.1    Hirpara, J.L.2    Chawdhury, S.H.3    Pervaiz, S.4
  • 9
    • 0032805888 scopus 로고    scopus 로고
    • Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis
    • Ferrer JL, Jez JM, Bowman ME, Dixon RA, Noel JP. Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis. Nat Struct Biol. 1999;6:775-84.
    • (1999) Nat Struct Biol , vol.6 , pp. 775-784
    • Ferrer, J.L.1    Jez, J.M.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 10
    • 7244239181 scopus 로고    scopus 로고
    • Crystal Structure of a Bacterial Type III Polyketide Synthase and Enzymatic Control of Reactive Polyketide Intermediates
    • Austin MB, Izumikawa M, Bowman ME, et al. Crystal Structure of a Bacterial Type III Polyketide Synthase and Enzymatic Control of Reactive Polyketide Intermediates. J Biol Chem. 2004;279:45162-74.
    • (2004) J Biol Chem , vol.279 , pp. 45162-45174
    • Austin, M.B.1    Izumikawa, M.2    Bowman, M.E.3
  • 11
    • 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 U S A. 2002;99:5319-24.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 5319-5324
    • Jez, J.M.1    Bowman, M.E.2    Noel, J.P.3
  • 12
    • 0036775842 scopus 로고    scopus 로고
    • Rock CO. The Claisen condensation in biology
    • Heath RJ, Rock CO. The Claisen condensation in biology. Nat Prod Rep. 2002;19(5):581-96.
    • (2002) Nat Prod Rep , vol.19 , Issue.5 , pp. 581-596
    • Heath, R.J.1
  • 13
    • 0040241878 scopus 로고    scopus 로고
    • A family of plant-specific polyketide synthases: Facts and predictions
    • Schroder J. A family of plant-specific polyketide synthases: facts and predictions. Trends in Plant Science. 1997;2:373-8.
    • (1997) Trends in Plant Science , vol.2 , pp. 373-378
    • Schroder, J.1
  • 15
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997;25: 4876-82.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 17
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol. 2007;24:1596-9.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 18
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M. The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol Biol Evol. 1987;4:406-25.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 20
    • 0026660413 scopus 로고
    • A simple method for estimating and testing minimum evolution trees
    • Rzhetsky A, Nei M. A simple method for estimating and testing minimum evolution trees. Mol Biol Evol. 1992;9:945-67.
    • (1992) Mol Biol Evol , vol.9 , pp. 945-967
    • Rzhetsky, A.1    Nei, M.2
  • 21
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J. Confidence limits on phylogenies: An approach using the bootstrap. Evolution. 1985;39:783-91.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 22
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas J, Ouyang Z, Tseng J, Binkowski A, Turpaz Y, Liang J. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 2006;34:W116-8.
    • (2006) Nucleic Acids Res , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 24
    • 0034843744 scopus 로고    scopus 로고
    • Support vector machine approach for protein subcellular localization prediction
    • Hua S, Sun Z. Support vector machine approach for protein subcellular localization prediction. Bioinformatics. 2001;17(8):721-8.
    • (2001) Bioinformatics , vol.17 , Issue.8 , pp. 721-728
    • Hua, S.1    Sun, Z.2
  • 25
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, Heijne GV. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol. 2000;300:1005-16.
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Heijne, G.V.4
  • 26
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v.2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy JL, Laird MR, Chen F, et al. PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics. 2005;21(5);617-23.
    • (2005) Bioinformatics , vol.21 , Issue.5 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3
  • 27
    • 75149164436 scopus 로고    scopus 로고
    • PreDisorder: Ab initio sequence-based prediction of protein disordered regions
    • Deng X, Eickholt J, Cheng J. PreDisorder: ab initio sequence-based prediction of protein disordered regions. BMC Bioinformatics. 2009;10:436.
    • (2009) BMC Bioinformatics , vol.10 , pp. 436
    • Deng, X.1    Eickholt, J.2    Cheng, J.3
  • 28
    • 33644847172 scopus 로고    scopus 로고
    • Prediction of protein stability changes for singlesite mutations using support vector machines
    • Cheng J, Randall A, Baldi P. Prediction of protein stability changes for singlesite mutations using support vector machines. Proteins. 2006;62(4):1125-32.
    • (2006) Proteins , vol.62 , Issue.4 , pp. 1125-1132
    • Cheng, J.1    Randall, A.2    Baldi, P.3
  • 29
    • 18444390875 scopus 로고    scopus 로고
    • Ab initio prediction of human orphan protein function from post-translational modifications and localization features
    • Jensen JL, Gupta R, Blom N, et al. Ab initio prediction of human orphan protein function from post-translational modifications and localization features. J Mol Biol. 2002;319:1257-65.
    • (2002) J Mol Biol , vol.319 , pp. 1257-1265
    • Jensen, J.L.1    Gupta, R.2    Blom, N.3
  • 30
    • 0037460964 scopus 로고    scopus 로고
    • Prediction of human protein function according to gene ontology categories
    • Jensen JL, Sterfeldt HH, Brunak S. Prediction of human protein function according to gene ontology categories. Bioinformatics. 2003;19:635-42.
    • (2003) Bioinformatics , vol.19 , pp. 635-642
    • Jensen, J.L.1    Sterfeldt, H.H.2    Brunak, S.3
  • 31
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European Molecular Biology Open Software Suite
    • Rice P, Longden I, Bleasby A. EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet. 2000;16(6):276-7.
    • (2000) Trends Genet , vol.16 , Issue.6 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 32
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier J, Osguthorpe DJ, Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol. 1978;120(1):97-120.
    • (1978) J Mol Biol , vol.120 , Issue.1 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 33
    • 0034671516 scopus 로고    scopus 로고
    • Mechanism of chalcone synthase. pKa of the catalytic cystein and the role of the conserved histidine in a plant polyketide synthase
    • Jez JM, Noel JP. Mechanism of chalcone synthase. pKa of the catalytic cystein and the role of the conserved histidine in a plant polyketide synthase. J Biol Chem. 2000;275:39640-6.
    • (2000) J Biol Chem , vol.275 , pp. 39640-39646
    • Jez, J.M.1    Noel, J.P.2
  • 34
    • 0025883209 scopus 로고
    • The role of cysteines in polyketide synthases: Site-directed mutagenesis of resveratrol and chalcone synthases, two key enzymes in different plant-specific pathways
    • Lanz T, Tropf S, Marner FJ, Schroder J, Schroder G. The role of cysteines in polyketide synthases: site-directed mutagenesis of resveratrol and chalcone synthases, two key enzymes in different plant-specific pathways. J Biol Chem. 1991;266, 9971-6.
    • (1991) J Biol Chem , vol.266 , pp. 9971-9976
    • Lanz, T.1    Tropf, S.2    Marner, F.J.3    Schroder, J.4    Schroder, G.5
  • 35
    • 0024994799 scopus 로고
    • Stilbene and chalcone synthases: Related enzymes with key functions in plant-specific pathways. Z
    • Schroeder J, Schroeder G. Stilbene and chalcone synthases: related enzymes with key functions in plant-specific pathways. Z. Naturforsch C. 1990;45(1-2):1-8.
    • (1990) Naturforsch C , vol.45 , Issue.1-2 , pp. 1-8
    • Schroeder, J.1    Schroeder, G.2
  • 36
    • 0034663468 scopus 로고    scopus 로고
    • Identification of amino acid residues important in the cyclization reactions of chalcone and stilbene synthases
    • Suh DY, Fukuma K, Kagami J, et al. Identification of amino acid residues important in the cyclization reactions of chalcone and stilbene synthases. Biochem J. 2000;350:229-35.
    • (2000) Biochem J , vol.350 , pp. 229-235
    • Suh, D.Y.1    Fukuma, K.2    Kagami, J.3
  • 37
    • 56549128655 scopus 로고    scopus 로고
    • Divergent evolution of the thiolase superfamily and chalcone synthase family
    • Jiang C, Kim SY, Suh DY. Divergent evolution of the thiolase superfamily and chalcone synthase family. Mol Phylogenet Evol. 2008;49(3): 691-701.
    • (2008) Mol Phylogenet Evol , vol.49 , Issue.3 , pp. 691-701
    • Jiang, C.1    Kim, S.Y.2    Suh, D.Y.3
  • 40
    • 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):14829-38.
    • (2001) Biochemistry , vol.40 , Issue.49 , pp. 14829-14838
    • Jez, J.M.1    Bowman, M.E.2    Noel, J.P.3
  • 42
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, Heijne GV. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Engineering. 1997;10:1-6.
    • (1997) Protein Engineering , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Heijne, G.V.4
  • 43
    • 0028388172 scopus 로고
    • Isolation of chalcone synthase and chalcone isomerase cDNAs from alfalfa (Medicago sativa L.): Highest transcript levels occur in young roots and root tips
    • McKhann HI, Hirsch AM. Isolation of chalcone synthase and chalcone isomerase cDNAs from alfalfa (Medicago sativa L.): highest transcript levels occur in young roots and root tips. Plant Mol Biol. 1994;24(5):767-77.
    • (1994) Plant Mol Biol , vol.24 , Issue.5 , pp. 767-777
    • McKhann, H.I.1    Hirsch, A.M.2
  • 44
    • 0029278107 scopus 로고
    • Chalcone synthase-like genes active during corolla development are differentially expressed and encode enzymes with different catalytic properties in Gerbera hybrida (Asteraceae)
    • Helariutta Y, Elomaa P, Kotilainen M, Griesbach RJ, Schroder J, Teeri TH. Chalcone synthase-like genes active during corolla development are differentially expressed and encode enzymes with different catalytic properties in Gerbera hybrida (Asteraceae). Plant Mol Biol. 1995;28(1):47-60.
    • (1995) Plant Mol Biol , vol.28 , Issue.1 , pp. 47-60
    • Helariutta, Y.1    Elomaa, P.2    Kotilainen, M.3    Griesbach, R.J.4    Schroder, J.5    Teeri, T.H.6
  • 45
    • 79958798843 scopus 로고    scopus 로고
    • Two bioactive compounds and a novel chalcone synthase like enzyme identified in Gerbera hybrida. Proc. IV IS on In Vitro Cult. & Hort Breeding
    • Koskela S, Elomaa P, Helariutta Y, Soderholm P, Vuorela P. Two bioactive compounds and a novel chalcone synthase like enzyme identified in Gerbera hybrida. Proc. IV IS on In Vitro Cult. & Hort Breeding. ISHS Acta Hort. 2001;560:271-4.
    • (2001) ISHS Acta Hort , vol.560 , pp. 271-274
    • Koskela, S.1    Elomaa, P.2    Helariutta, Y.3    Soderholm, P.4    Vuorela, P.5
  • 46
    • 0033152851 scopus 로고    scopus 로고
    • Phlorisovalerophenone synthase, a novel polyketide synthase from hop (Humulus lupulus L.) cones
    • Paniego NB, Zuurbier KW, Fung SY, et al. Phlorisovalerophenone synthase, a novel polyketide synthase from hop (Humulus lupulus L.) cones. Eur J Biochem. 1999;262(2):612-6.
    • (1999) Eur J Biochem , vol.262 , Issue.2 , pp. 612-616
    • Paniego, N.B.1    Zuurbier, K.W.2    Fung, S.Y.3
  • 47
    • 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, Falkenstein-Paul H, Schmidt W, Beerhues L. Benzophenone synthase and chalcone synthase from Hypericum androsaemum cell cultures:cDNA cloning, functional expression, and site-directed mutagenesis of two polyketide synthases. Plant J. 2003;34:847-55.
    • (2003) Plant J , vol.34 , pp. 847-855
    • Liu, B.1    Falkenstein-Paul, H.2    Schmidt, W.3    Beerhues, L.4
  • 48
    • 33846781472 scopus 로고    scopus 로고
    • An acridone-producing novel multifunctional type III polyketide synthase from Huperzia serrata
    • Wanibuchi K, Zhang P, Abe T, et al. An acridone-producing novel multifunctional type III polyketide synthase from Huperzia serrata. FEBS J. 2007;274(4):1073-82.
    • (2007) FEBS J , vol.274 , Issue.4 , pp. 1073-1082
    • Wanibuchi, K.1    Zhang, P.2    Abe, T.3
  • 49
    • 34247350408 scopus 로고    scopus 로고
    • Biphenyl synthase, a novel type III polyketide synthase
    • Liu B, Raeth T, Beuerle T, Beerhues L. Biphenyl synthase, a novel type III polyketide synthase. Planta. 2007;225(6):1495-503.
    • (2007) Planta , vol.225 , Issue.6 , pp. 1495-1503
    • Liu, B.1    Raeth, T.2    Beuerle, T.3    Beerhues, L.4
  • 50
    • 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):6806-11.
    • (1984) J Biol Chem , vol.259 , Issue.11 , pp. 6806-6811
    • Schoppner, A.1    Kindl, H.2
  • 51
    • 13444282087 scopus 로고    scopus 로고
    • A Plant Type III Polyketide Synthase that Produces Pentaketide Chromone
    • Abe I, Utsumi Y, Oguro S, Morita H, Sano Y, Noguchi H. A Plant Type III Polyketide Synthase that Produces Pentaketide Chromone. J Am Chem Soc. 2005;127:1362-3.
    • (2005) J Am Chem Soc , vol.127 , pp. 1362-1363
    • Abe, I.1    Utsumi, Y.2    Oguro, S.3    Morita, H.4    Sano, Y.5    Noguchi, H.A.6
  • 52
    • 24744454823 scopus 로고    scopus 로고
    • Engineered biosynthesis of plant polyketides: Chain length control in an octaketide-producing plant type III polyketide synthase
    • Abe I, Oguro S, Utsumi Y, Sano Y, Noguchi H. Engineered biosynthesis of plant polyketides: chain length control in an octaketide-producing plant type III polyketide synthase. J Am Chem Soc. 2005;127(36):12709-16.
    • (2005) J Am Chem Soc , vol.127 , Issue.36 , pp. 12709-12716
    • Abe, I.1    Oguro, S.2    Utsumi, Y.3    Sano, Y.4    Noguchi, H.5
  • 53
    • 0034845768 scopus 로고    scopus 로고
    • Benzalacetone synthase. A novel polyketide synthase that plays a crucial role in the biosynthesis of phenylbutanones in Rheum palmatum
    • Abe I, Takahashi Y, Morita H, Noguchi H. Benzalacetone synthase. A novel polyketide synthase that plays a crucial role in the biosynthesis of phenylbutanones in Rheum palmatum. Eur J Biochem. 2001;268(11):3354-9.
    • (2001) Eur J Biochem , vol.268 , Issue.11 , pp. 3354-3359
    • Abe, I.1    Takahashi, Y.2    Morita, H.3    Noguchi, H.4
  • 54
    • 1642299704 scopus 로고    scopus 로고
    • The first plant type III polyketide synthase that catalyzes formation of aromatic heptaketide
    • Abe I, Utsumi Y, Oguro S, Noguchi H. The first plant type III polyketide synthase that catalyzes formation of aromatic heptaketide. FEBS Lett. 2004; 562(1-3):171-6.
    • (2004) FEBS Lett , vol.562 , Issue.1-3 , pp. 171-176
    • Abe, I.1    Utsumi, Y.2    Oguro, S.3    Noguchi, H.4
  • 55
    • 0028919709 scopus 로고
    • The inducible 9, 10-dihydrophenanthrene pathway: Characterization and expression of bibenzyl synthase and S-adenosylhomocysteine hydrolase
    • Preisig-Muller R, Gnau P, Kindl H. The inducible 9, 10-dihydrophenanthrene pathway: characterization and expression of bibenzyl synthase and S-adenosylhomocysteine hydrolase. Arch Biochem Biophys. 1995;317(1):201-7.
    • (1995) Arch Biochem Biophys , vol.317 , Issue.1 , pp. 201-207
    • Preisig-Muller, R.1    Gnau, P.2    Kindl, H.3
  • 56
    • 0001544701 scopus 로고    scopus 로고
    • P-Coumaroyltriacetic acid synthase, a new homologue of chalcone synthase, from Hydrangea macrophylla var. thunbergii
    • Akiyama T, Shibuya M, Liu HM, Ebizuka Y. P-Coumaroyltriacetic acid synthase, a new homologue of chalcone synthase, from Hydrangea macrophylla var. thunbergii. Eur J Biochem. 1999;263(3):834-9.
    • (1999) Eur J Biochem , vol.263 , Issue.3 , pp. 834-839
    • Akiyama, T.1    Shibuya, M.2    Liu, H.M.3    Ebizuka, Y.4
  • 57
    • 0037308046 scopus 로고    scopus 로고
    • Stilbenecarboxylate biosynthesis: A new function in the family of chalcone synthase-related proteins
    • Eckermann C, Schroder G, Eckermann S, et al. Stilbenecarboxylate biosynthesis: a new function in the family of chalcone synthase-related proteins. Phytochemistry. 2003;62(3):271-86.
    • (2003) Phytochemistry , vol.62 , Issue.3 , pp. 271-286
    • Eckermann, C.1    Schroder, G.2    Eckermann, S.3


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