메뉴 건너뛰기




Volumn 160, Issue 3, 2012, Pages 1267-1280

Cinnamate: CoA ligase initiates the biosynthesis of a benzoate-derived xanthone phytoalexin in hypericum calycinum cell cultures

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84868306586     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.112.204180     Document Type: Article
Times cited : (57)

References (73)
  • 1
    • 0036934797 scopus 로고    scopus 로고
    • Benzoic acid biosynthesis in cell cultures of Hypericum androsaemum
    • Abd El-Mawla AMA, Beerhues L (2002) Benzoic acid biosynthesis in cell cultures of Hypericum androsaemum. Planta 214: 727-733
    • (2002) Planta , vol.214 , pp. 727-733
    • Abd El-Mawla, A.M.A.1    Beerhues, L.2
  • 2
    • 0035125896 scopus 로고    scopus 로고
    • Cinnamic acid is a precursor of benzoic acids in cell cultures of Hypericum androsaemum L but not in cell cultures of Centaurium erythraea RAFN
    • Abd El-Mawla AMA, Schmidt W, Beerhues L (2001) Cinnamic acid is a precursor of benzoic acids in cell cultures of Hypericum androsaemum L. but not in cell cultures of Centaurium erythraea RAFN. Planta 212: 288-293
    • (2001) Planta , vol.212 , pp. 288-293
    • Abd El-Mawla, A.M.A.1    Schmidt, W.2    Beerhues, L.3
  • 3
    • 0030956917 scopus 로고    scopus 로고
    • 3-Hydroxybenzoate:Coenzyme A ligase and 4-coumarate:Coenzyme A ligase from cultured cells of Centaurium erythraea
    • Barillas W, Beerhues L (1997) 3-Hydroxybenzoate:coenzyme A ligase and 4-coumarate:coenzyme A ligase from cultured cells of Centaurium erythraea. Planta 202: 112-116
    • (1997) Planta , vol.202 , pp. 112-116
    • Barillas, W.1    Beerhues, L.2
  • 4
    • 0034095317 scopus 로고    scopus 로고
    • 3-Hydroxybenzoate:Coenzyme A ligase from cell cultures of Centaurium erythraea: Isolation and characterization
    • Barillas W, Beerhues L (2000) 3-Hydroxybenzoate:coenzyme A ligase from cell cultures of Centaurium erythraea: isolation and characterization. Biol Chem 381: 155-160
    • (2000) Biol Chem , vol.381 , pp. 155-160
    • Barillas, W.1    Beerhues, L.2
  • 5
    • 84868332306 scopus 로고    scopus 로고
    • Biosynthesis of the active Hypericum perforatum constituents
    • In MS Odabas, C Cirak, eds, Hypericum Global Science Books, Isleworth, UK
    • Beerhues L (2011) Biosynthesis of the active Hypericum perforatum constituents. In MS Odabas, C Cirak, eds, Medicinal and Aromatic Plant Science and Biotechnology 5 (Special Issue 1): Hypericum. Global Science Books, Isleworth, UK, pp 70-77
    • (2011) Medicinal and Aromatic Plant Science and Biotechnology , vol.5 , Issue.SPEC. ISSUE 1 , pp. 70-77
    • Beerhues, L.1
  • 6
    • 0029187840 scopus 로고
    • Differential accumulation of xanthones in methyl-jasmonate-and yeast extract-treated cell cultures of Centaurium erythraea and Centaurium littorale
    • Beerhues L, Berger U (1995) Differential accumulation of xanthones in methyl-jasmonate-and yeast extract-treated cell cultures of Centaurium erythraea and Centaurium littorale. Planta 197: 608-612
    • (1995) Planta , vol.197 , pp. 608-612
    • Beerhues, L.1    Berger, U.2
  • 7
    • 71049132718 scopus 로고    scopus 로고
    • Biosynthesis of biphenyls and benzophenones: Evolution of benzoic acid-specific type III polyketide synthases in plants
    • Beerhues L, Liu B (2009) Biosynthesis of biphenyls and benzophenones: evolution of benzoic acid-specific type III polyketide synthases in plants. Phytochemistry 70: 1719-1727
    • (2009) Phytochemistry , vol.70 , pp. 1719-1727
    • Beerhues, L.1    Liu, B.2
  • 8
    • 0033133572 scopus 로고    scopus 로고
    • The Rx gene from potato controls separate virus resistance and cell death responses
    • Bendahmane A, Kanyuka K, Baulcombe DC (1999) The Rx gene from potato controls separate virus resistance and cell death responses. Plant Cell 11: 781-792
    • (1999) Plant Cell , vol.11 , pp. 781-792
    • Bendahmane, A.1    Kanyuka, K.2    Baulcombe, D.C.3
  • 9
    • 0037086137 scopus 로고    scopus 로고
    • Enzymatic synthesis and purification of aromatic coenzyme A esters
    • Beuerle T, Pichersky E (2002a) Enzymatic synthesis and purification of aromatic coenzyme A esters. Anal Biochem 302: 305-312
    • (2002) Anal Biochem , vol.302 , pp. 305-312
    • Beuerle, T.1    Pichersky, E.2
  • 10
    • 0037092062 scopus 로고    scopus 로고
    • Purification and characterization of benzoate: Coenzyme A ligase from Clarkia breweri
    • Beuerle T, Pichersky E (2002b) Purification and characterization of benzoate: coenzyme A ligase from Clarkia breweri. Arch Biochem Biophys 400: 258-264
    • (2002) Arch Biochem Biophys , vol.400 , pp. 258-264
    • Beuerle, T.1    Pichersky, E.2
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 39149109593 scopus 로고    scopus 로고
    • Salicylic acid production in response to biotic and abiotic stress depends on isochorismate in Nicotiana benthamiana
    • Catinot J, Buchala A, Abou-Mansour E, Métraux JP (2008) Salicylic acid production in response to biotic and abiotic stress depends on isochorismate in Nicotiana benthamiana. FEBS Lett 582: 473-478
    • (2008) FEBS Lett , vol.582 , pp. 473-478
    • Catinot, J.1    Buchala, A.2    Abou-Mansour, E.3    Métraux, J.P.4
  • 16
    • 80051916818 scopus 로고    scopus 로고
    • Taxonomy and chemotaxonomy of the genus Hypericum
    • In MS Odabas, C Cirak, eds, Hypericum Global Science Books, Isleworth, UK
    • Crockett SL, Robson NKB (2011) Taxonomy and chemotaxonomy of the genus Hypericum. In MS Odabas, C Cirak, eds, Medicinal and Aromatic Plant Science and Biotechnology 5 (Special Issue 1): Hypericum. Global Science Books, Isleworth, UK, pp 1-13
    • (2011) Medicinal and Aromatic Plant Science and Biotechnology , vol.5 , Issue.SPEC. ISSUE 1 , pp. 1-13
    • Crockett, S.L.1    Robson, N.K.B.2
  • 18
    • 42249097421 scopus 로고    scopus 로고
    • Metabolic engineering of plant volatiles
    • Dudareva N, Pichersky E (2008) Metabolic engineering of plant volatiles. Curr Opin Biotechnol 19: 181-189
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 181-189
    • Dudareva, N.1    Pichersky, E.2
  • 19
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate:Coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
    • Ehlting J, Büttner D, Wang Q, Douglas CJ, Somssich IE, Kombrink E (1999) Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms. Plant J 19: 9-20
    • (1999) Plant J , vol.19 , pp. 9-20
    • Ehlting, J.1    Büttner, D.2    Wang, Q.3    Douglas, C.J.4    Somssich, I.E.5    Kombrink, E.6
  • 20
    • 84863225155 scopus 로고    scopus 로고
    • Xanthone biosynthesis in Hypericum perforatum cells provides antioxidant and antimicrobial protection upon biotic stress
    • Franklin G, Conceição LFR, Kombrink E, Dias ACP (2009) Xanthone biosynthesis in Hypericum perforatum cells provides antioxidant and antimicrobial protection upon biotic stress. Phytochemistry 70: 60-68
    • (2009) Phytochemistry , vol.70 , pp. 60-68
    • Franklin, G.1    Conceição, L.F.R.2    Kombrink, E.3    Dias, A.C.P.4
  • 21
    • 0001391235 scopus 로고
    • Conversion of p-coumaric acid to p-hydroxybenzoic acid by cell free extracts of potato tubers and Polysporus hispidus
    • French CJ, Vance CP, Towers GHN (1976) Conversion of p-coumaric acid to p-hydroxybenzoic acid by cell free extracts of potato tubers and Polysporus hispidus. Phytochemistry 15: 564-566
    • (1976) Phytochemistry , vol.15 , pp. 564-566
    • French, C.J.1    Vance, C.P.2    Towers, G.H.N.3
  • 22
    • 0028054686 scopus 로고
    • The fadD gene of Escherichia coli K12 is located close to rnd at 396 min of the chromosomal map and is a new member of the AMP-binding protein family
    • Fulda M, Heinz E, Wolter FP (1994) The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family. Mol Gen Genet 242: 241-249
    • (1994) Mol Gen Genet , vol.242 , pp. 241-249
    • Fulda, M.1    Heinz, E.2    Wolter, F.P.3
  • 23
    • 79955119721 scopus 로고    scopus 로고
    • 4-Coumarate:CoA ligase family members from elicitor-treated Sorbus aucuparia cell cultures
    • Gaid MM, Scharnhop H, Ramadan H, Beuerle T, Beerhues L (2011) 4-Coumarate:CoA ligase family members from elicitor-treated Sorbus aucuparia cell cultures. J Plant Physiol 168: 944-951
    • (2011) J Plant Physiol , vol.168 , pp. 944-951
    • Gaid, M.M.1    Scharnhop, H.2    Ramadan, H.3    Beuerle, T.4    Beerhues, L.5
  • 24
    • 67651204737 scopus 로고    scopus 로고
    • Benzaldehyde dehydrogenase from chitosan-treated Sorbus aucuparia cell cultures
    • Gaid MM, Sircar D, Beuerle T, Mitra A, Beerhues L (2009) Benzaldehyde dehydrogenase from chitosan-treated Sorbus aucuparia cell cultures. J Plant Physiol 166: 1343-1349
    • (2009) J Plant Physiol , vol.166 , pp. 1343-1349
    • Gaid, M.M.1    Sircar, D.2    Beuerle, T.3    Mitra, A.4    Beerhues, L.5
  • 25
    • 0041094210 scopus 로고    scopus 로고
    • Introducing StuI sites improves vectors for the expression of fusion proteins with factor Xa cleavage sites
    • Görlach J, Schmid J (1996) Introducing StuI sites improves vectors for the expression of fusion proteins with factor Xa cleavage sites. Gene 170: 145-146
    • (1996) Gene , vol.170 , pp. 145-146
    • Görlach, J.1    Schmid, J.2
  • 26
    • 0003169904 scopus 로고
    • Darstellung und Eigenschaften von Coenzym A-Thioestern substituierter Zimtsäuren
    • Gross GG, Zenk MH (1966) Darstellung und Eigenschaften von Coenzym A-Thioestern substituierter Zimtsäuren. Z Naturforsch B 21b: 683-690
    • (1966) Z Naturforsch B , vol.21 b , pp. 683-690
    • Gross, G.G.1    Zenk, M.H.2
  • 27
    • 0001353401 scopus 로고
    • In PK Stumpf, EE Conn, eds, The Biochemistry of Plants, Academic Press, London
    • Hanson KR, Havir EA (1981) Phenylalanine ammonia-lyase. In PK Stumpf, EE Conn, eds, The Biochemistry of Plants, Vol 7. Academic Press, London, pp 577-625
    • (1981) Phenylalanine ammonia-lyase , vol.7 , pp. 577-625
    • Hanson, K.R.1    Havir, E.A.2
  • 28
    • 66149144283 scopus 로고    scopus 로고
    • An aldehyde oxidase in developing seeds of Arabidopsis converts benzaldehyde to benzoic acid
    • Ibdah M, Chen YT, Wilkerson CG, Pichersky E (2009) An aldehyde oxidase in developing seeds of Arabidopsis converts benzaldehyde to benzoic acid. Plant Physiol 150: 416-423
    • (2009) Plant Physiol , vol.150 , pp. 416-423
    • Ibdah, M.1    Chen, Y.T.2    Wilkerson, C.G.3    Pichersky, E.4
  • 29
    • 66149151099 scopus 로고    scopus 로고
    • Arabidopsis Chy1 null mutants are deficient in benzoic acid-containing glucosinolates in the seeds
    • IbdahM, Pichersky E (2009) Arabidopsis Chy1 null mutants are deficient in benzoic acid-containing glucosinolates in the seeds. Plant Biol (Stuttg) 11: 574-581
    • (2009) Plant Biol (Stuttg) , vol.11 , pp. 574-581
    • Ibdah, M.1    Pichersky, E.2
  • 30
    • 0034480179 scopus 로고    scopus 로고
    • 3-Hydroxy-3-phenylpropanoic acid is an intermediate in the biosynthesis of benzoic acid and salicylic acid but benzaldehyde is not
    • Jarvis AP, Schaaf O, Oldham NJ (2000) 3-Hydroxy-3-phenylpropanoic acid is an intermediate in the biosynthesis of benzoic acid and salicylic acid but benzaldehyde is not. Planta 212: 119-126
    • (2000) Planta , vol.212 , pp. 119-126
    • Jarvis, A.P.1    Schaaf, O.2    Oldham, N.J.3
  • 31
    • 0037216584 scopus 로고    scopus 로고
    • Cinnamate:Coenzyme A ligase from the filamentous bacterium Streptomyces coelicolor A3(2)
    • Kaneko M, Ohnishi Y, Horinouchi S (2003) Cinnamate:coenzyme A ligase from the filamentous bacterium Streptomyces coelicolor A3(2). J Bacteriol 185: 20-27
    • (2003) J Bacteriol , vol.185 , pp. 20-27
    • Kaneko, M.1    Ohnishi, Y.2    Horinouchi, S.3
  • 33
    • 0028725406 scopus 로고
    • The salicylic acid signal in plants
    • Klessig DF, Malamy J (1994) The salicylic acid signal in plants. Plant Mol Biol 26: 1439-1458
    • (1994) Plant Mol Biol , vol.26 , pp. 1439-1458
    • Klessig, D.F.1    Malamy, J.2
  • 36
    • 0034760621 scopus 로고    scopus 로고
    • Regulation of circadian methyl benzoate emission in diurnally and nocturnally emitting plants
    • Kolosova N, Gorenstein N, Kish CM, Dudareva N (2001) Regulation of circadian methyl benzoate emission in diurnally and nocturnally emitting plants. Plant Cell 13: 2333-2347
    • (2001) Plant Cell , vol.13 , pp. 2333-2347
    • Kolosova, N.1    Gorenstein, N.2    Kish, C.M.3    Dudareva, N.4
  • 37
    • 0037318708 scopus 로고    scopus 로고
    • 4-Coumarate:CoA ligase family in Rubus idaeus: CDNA structure, evolution, and expression
    • Kumar A, Ellis BE (2003) 4-Coumarate:CoA ligase family in Rubus idaeus: cDNA structure, evolution, and expression. Plant Mol Biol 31: 327-340
    • (2003) Plant Mol Biol , vol.31 , pp. 327-340
    • Kumar, A.1    Ellis, B.E.2
  • 38
    • 0030250380 scopus 로고    scopus 로고
    • Two divergent members of a tobacco 4-coumarate: Coenzyme A ligase (4CL) gene family: CDNA structure, gene inheritance and expression, and properties of recombinant proteins
    • Lee D, Douglas CJ (1996) Two divergent members of a tobacco 4-coumarate: coenzyme A ligase (4CL) gene family: cDNA structure, gene inheritance and expression, and properties of recombinant proteins. Plant Physiol 112: 193-205
    • (1996) Plant Physiol , vol.112 , pp. 193-205
    • Lee, D.1    Douglas, C.J.2
  • 40
    • 84982378007 scopus 로고
    • Organic growth factor requirements of tobacco tissue cultures
    • Linsmaier EM, Skoog F (1965) Organic growth factor requirements of tobacco tissue cultures. Physiol Plant 18: 100-127
    • (1965) Physiol Plant , vol.18 , pp. 100-127
    • Linsmaier, E.M.1    Skoog, F.2
  • 41
    • 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 (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.1    Falkenstein-Paul, H.2    Schmidt, W.3    Beerhues, L.4
  • 43
    • 0027951993 scopus 로고
    • Biosynthesis of p-hydroxybenzoate from pcoumarate and p-coumaroyl-coenzyme A in cell-free extracts of Lithospermum erythrorhizon cell cultures
    • Löscher R, Heide L (1994) Biosynthesis of p-hydroxybenzoate from pcoumarate and p-coumaroyl-coenzyme A in cell-free extracts of Lithospermum erythrorhizon cell cultures. Plant Physiol 106: 271-279
    • (1994) Plant Physiol , vol.106 , pp. 271-279
    • Löscher, R.1    Heide, L.2
  • 44
    • 0028317609 scopus 로고
    • Elicitor-mediated induction of isochorismate synthase and accumulation of 2,3-dihydroxybenzoic acid in Catharanthus roseus cell suspension and shoot cultures
    • Moreno PRH, van der Heijden R, Verpoorte R (1994) Elicitor-mediated induction of isochorismate synthase and accumulation of 2,3-dihydroxybenzoic acid in Catharanthus roseus cell suspension and shoot cultures. Plant Cell Rep 14: 188-191
    • (1994) Plant Cell Rep , vol.14 , pp. 188-191
    • Moreno, P.R.H.1    van der Heijden, R.2    Verpoorte, R.3
  • 45
    • 0037414447 scopus 로고    scopus 로고
    • Motif refinement of the peroxisomal targeting signal 1 and evaluation of taxon-specific differences
    • Neuberger G, Maurer-Stroh S, Eisenhaber B, Hartig A, Eisenhaber F (2003) Motif refinement of the peroxisomal targeting signal 1 and evaluation of taxon-specific differences. J Mol Biol 328: 567-579
    • (2003) J Mol Biol , vol.328 , pp. 567-579
    • Neuberger, G.1    Maurer-Stroh, S.2    Eisenhaber, B.3    Hartig, A.4    Eisenhaber, F.5
  • 46
    • 1442340104 scopus 로고    scopus 로고
    • Fluorescent proteins in poplar: A useful tool to study promoter function and protein localization
    • Nowak K, Luniak N, Meyer S, Schulze J, Mendel RR, Hänsch R (2004) Fluorescent proteins in poplar: a useful tool to study promoter function and protein localization. Plant Biol (Stuttg) 6: 65-73
    • (2004) Plant Biol (Stuttg) , vol.6 , pp. 65-73
    • Nowak, K.1    Luniak, N.2    Meyer, S.3    Schulze, J.4    Mendel, R.R.5    Hänsch, R.6
  • 48
    • 0036011085 scopus 로고    scopus 로고
    • The formation and function of plant volatiles: Perfumes for pollinator attraction and defense
    • Pichersky E, Gershenzon J (2002) The formation and function of plant volatiles: perfumes for pollinator attraction and defense. Curr Opin Plant Biol 5: 237-243
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 237-243
    • Pichersky, E.1    Gershenzon, J.2
  • 49
    • 0000379525 scopus 로고
    • Salicylic acid: A natural inducer of heat production in Arum lilies
    • Raskin I, Ehmann A, Melander WR, Meeuse BJD (1987) Salicylic acid: a natural inducer of heat production in Arum lilies. Science 237: 1601-1602
    • (1987) Science , vol.237 , pp. 1601-1602
    • Raskin, I.1    Ehmann, A.2    Melander, W.R.3    Meeuse, B.J.D.4
  • 50
    • 0000914490 scopus 로고    scopus 로고
    • Intermediates of salicylic acid biosynthesis in tobacco
    • Ribnicky DM, Shulaev V, Raskin I (1998) Intermediates of salicylic acid biosynthesis in tobacco. Plant Physiol 118: 565-572
    • (1998) Plant Physiol , vol.118 , pp. 565-572
    • Ribnicky, D.M.1    Shulaev, V.2    Raskin, I.3
  • 51
    • 3042724871 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals
    • Rottensteiner H, Kramer A, Lorenzen S, Stein K, Landgraf C, Volkmer-Engert R, Erdmann R (2004) Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals. Mol Biol Cell 15: 3406-3417
    • (2004) Mol Biol Cell , vol.15 , pp. 3406-3417
    • Rottensteiner, H.1    Kramer, A.2    Lorenzen, S.3    Stein, K.4    Landgraf, C.5    Volkmer-Engert, R.6    Erdmann, R.7
  • 53
    • 17144416797 scopus 로고    scopus 로고
    • A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis thaliana has the catalytic capacity to activate biosynthetic precursors of jasmonic acid
    • Schneider K, Kienow L, Schmelzer E, Colby T, Bartsch M, Miersch O, Wasternack C, Kombrink E, Stuible HP (2005) A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis thaliana has the catalytic capacity to activate biosynthetic precursors of jasmonic acid. J Biol Chem 280: 13962-13972
    • (2005) J Biol Chem , vol.280 , pp. 13962-13972
    • Schneider, K.1    Kienow, L.2    Schmelzer, E.3    Colby, T.4    Bartsch, M.5    Miersch, O.6    Wasternack, C.7    Kombrink, E.8    Stuible, H.P.9
  • 54
    • 0000862440 scopus 로고
    • Biosynthesis of phydroxybenzoic acid in elicitor-treated carrot cell cultures
    • Schnitzler JP, Madlung J, Rose A, Seitz HU (1992) Biosynthesis of phydroxybenzoic acid in elicitor-treated carrot cell cultures. Planta 188: 594-600
    • (1992) Planta , vol.188 , pp. 594-600
    • Schnitzler, J.P.1    Madlung, J.2    Rose, A.3    Seitz, H.U.4
  • 55
    • 38249011698 scopus 로고
    • o-Succinylbenzoate:Coenzyme A ligase from anthraquinone producing cell suspension cultures of Galium mollugo
    • Sieweke HJ, Leistner E (1992) o-Succinylbenzoate:coenzyme A ligase from anthraquinone producing cell suspension cultures of Galium mollugo. Phytochemistry 31: 2329-2335
    • (1992) Phytochemistry , vol.31 , pp. 2329-2335
    • Sieweke, H.J.1    Leistner, E.2
  • 56
    • 39149115125 scopus 로고    scopus 로고
    • Evidence for p-hydroxybenzoate formation involving enzymatic phenylpropanoid side-chain cleavage in hairy roots of Daucus carota
    • Sircar D, Mitra A (2008) Evidence for p-hydroxybenzoate formation involving enzymatic phenylpropanoid side-chain cleavage in hairy roots of Daucus carota. J Plant Physiol 165: 407-414
    • (2008) J Plant Physiol , vol.165 , pp. 407-414
    • Sircar, D.1    Mitra, A.2
  • 57
    • 0016736883 scopus 로고
    • Chemical syntheses and properties of hydroxycinnamoyl-coenzyme A derivatives
    • Stöckigt J, Zenk MH (1975) Chemical syntheses and properties of hydroxycinnamoyl-coenzyme A derivatives. Z Naturforsch C 30: 352-358
    • (1975) Z Naturforsch C , vol.30 , pp. 352-358
    • Stöckigt, J.1    Zenk, M.H.2
  • 58
    • 0035920183 scopus 로고    scopus 로고
    • Identification of the substrate specificityconferring amino acid residues of 4-coumarate:Coenzyme A ligase allows the rational design of mutant enzymes with new catalytic properties
    • Stuible HP, Kombrink E (2001) Identification of the substrate specificityconferring amino acid residues of 4-coumarate:coenzyme A ligase allows the rational design of mutant enzymes with new catalytic properties. J Biol Chem 276: 26893-26897
    • (2001) J Biol Chem , vol.276 , pp. 26893-26897
    • Stuible, H.P.1    Kombrink, E.2
  • 59
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 61
    • 0242560352 scopus 로고
    • Biosynthesis of ubiquinone: A search for polyprenyl phenol and quinone precursors
    • Threlfall DR, Whistance GR (1970) Biosynthesis of ubiquinone: a search for polyprenyl phenol and quinone precursors. Phytochemistry 9: 355-359
    • (1970) Phytochemistry , vol.9 , pp. 355-359
    • Threlfall, D.R.1    Whistance, G.R.2
  • 62
  • 63
    • 0032539524 scopus 로고    scopus 로고
    • Characterization of the monovalent and divalent cation requirements for the xenobiotic carboxylic acid:CoA ligases of bovine liver mitochondria
    • Vessey DA, Kelley M (1998) Characterization of the monovalent and divalent cation requirements for the xenobiotic carboxylic acid:CoA ligases of bovine liver mitochondria. Biochim Biophys Acta 1382: 243-248
    • (1998) Biochim Biophys Acta , vol.1382 , pp. 243-248
    • Vessey, D.A.1    Kelley, M.2
  • 64
    • 0033631957 scopus 로고    scopus 로고
    • Monovalent cation effects on the activity of the xenobiotic/medium-chain fatty acid:CoA ligases are substrate specific
    • Vessey DA, Kelley M, Lau E, Zhang SZ (2000) Monovalent cation effects on the activity of the xenobiotic/medium-chain fatty acid:CoA ligases are substrate specific. J Biochem Mol Toxicol 14: 162-168
    • (2000) J Biochem Mol Toxicol , vol.14 , pp. 162-168
    • Vessey, D.A.1    Kelley, M.2    Lau, E.3    Zhang, S.Z.4
  • 65
    • 76549093442 scopus 로고    scopus 로고
    • Phenylpropanoid biosynthesis
    • Vogt T (2010) Phenylpropanoid biosynthesis. Mol Plant 3: 2-20
    • (2010) Mol Plant , vol.3 , pp. 2-20
    • Vogt, T.1
  • 66
    • 0037342553 scopus 로고    scopus 로고
    • An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus
    • Voinnet O, Rivas S, Mestre P, Baulcombe D (2003) An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus. Plant J 33: 949-956
    • (2003) Plant J , vol.33 , pp. 949-956
    • Voinnet, O.1    Rivas, S.2    Mestre, P.3    Baulcombe, D.4
  • 69
    • 0030764890 scopus 로고    scopus 로고
    • 13C-labeled glucose: Formation of gallic acid in plants and fungi
    • 13C-labeled glucose: formation of gallic acid in plants and fungi. J Biol Chem 272: 25474-25482
    • (1997) J Biol Chem , vol.272 , pp. 25474-25482
    • Werner, I.1    Bacher, A.2    Eisenreich, W.3
  • 70
    • 33646121742 scopus 로고    scopus 로고
    • Variations on a theme: Synthesis and modification of plant benzoic acids
    • Wildermuth MC (2006) Variations on a theme: synthesis and modification of plant benzoic acids. Curr Opin Plant Biol 9: 288-296
    • (2006) Curr Opin Plant Biol , vol.9 , pp. 288-296
    • Wildermuth, M.C.1
  • 71
    • 0035969499 scopus 로고    scopus 로고
    • Isochorismate synthase is required to synthesize salicylic acid for plant defence
    • Wildermuth MC, Dewdney J, Wu G, Ausubel FM (2001) Isochorismate synthase is required to synthesize salicylic acid for plant defence. Nature 414: 562-565
    • (2001) Nature , vol.414 , pp. 562-565
    • Wildermuth, M.C.1    Dewdney, J.2    Wu, G.3    Ausubel, F.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.