메뉴 건너뛰기




Volumn 30, Issue 8, 2003, Pages 456-461

Heterologous production of flavanones in Escherichia coli: Potential for combinatorial biosynthesis of flavonoids in bacteria

Author keywords

4 Coumarate cinnamate:CoA ligase; Chalcone; Combinatorial biosynthesis; Flavonoid Flavanone; Metabolic engineering

Indexed keywords

CHALCONE DERIVATIVE; CHALCONE SYNTHASE; CINNAMIC ACID; FLAVANONE DERIVATIVE; FLAVONOID; ISOMERASE; NARINGENIN; PARA COUMARIC ACID; PHENYLALANINE; PHENYLALANINE AMMONIA LYASE; PINOCEMBRINE; TYROSINE;

EID: 0141594681     PISSN: 13675435     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10295-003-0061-1     Document Type: Conference Paper
Times cited : (71)

References (70)
  • 2
    • 0032810904 scopus 로고    scopus 로고
    • Overexpression of a designed 2.2 kb gene of eukaryotic phenylalanine ammonia-lyase in E. coli
    • Baedeker M, Schulz GE (1999) Overexpression of a designed 2.2 kb gene of eukaryotic phenylalanine ammonia-lyase in E. coli. FEBS Lett 457:57-60
    • (1999) FEBS Lett , vol.457 , pp. 57-60
    • Baedeker, M.1    Schulz, G.E.2
  • 3
    • 0025744288 scopus 로고
    • Structural comparison, modes of expression, and putative cis-acting elements of the two 4-coumarate:CoA ligase genes in potato
    • Becker-André M, Schulze-Lefert P, Hahlbrock K (1991) Structural comparison, modes of expression, and putative cis-acting elements of the two 4-coumarate:CoA ligase genes in potato. J Biol Chem 266:8551-8559
    • (1991) J Biol Chem , vol.266 , pp. 8551-8559
    • Becker-André, M.1    Schulze-Lefert, P.2    Hahlbrock, K.3
  • 4
    • 0025276244 scopus 로고
    • Reactivity and pH dependence of thiol conjugation to N-ethylmaleimide: Detection of a conformational change in chalcone isomerase
    • Bednar RA (1990) Reactivity and pH dependence of thiol conjugation to N-ethylmaleimide: detection of a conformational change in chalcone isomerase. Biochemistry 29:3684-3690
    • (1990) Biochemistry , vol.29 , pp. 3684-3690
    • Bednar, R.A.1
  • 5
    • 0024978434 scopus 로고
    • Chemical modification of chalcone isomerase by mercurials and tetrathionate
    • Bednar RA, Fried WB, Lock YW, Pramanik B (1989) Chemical modification of chalcone isomerase by mercurials and tetrathionate. J Biol Chem 264:14272-14276
    • (1989) J Biol Chem , vol.264 , pp. 14272-14276
    • Bednar, R.A.1    Fried, W.B.2    Lock, Y.W.3    Pramanik, B.4
  • 8
    • 0010396989 scopus 로고    scopus 로고
    • The maize Lc regulatory gene up-regulates the flavonoid biosynthetic pathway of Petunia
    • Bradley JM, Davis KM, Deroles SC, Bloor SJ, Lewis DH (1998) The maize Lc regulatory gene up-regulates the flavonoid biosynthetic pathway of Petunia. Plant J 13:381-392
    • (1998) Plant J , vol.13 , pp. 381-392
    • Bradley, J.M.1    Davis, K.M.2    Deroles, S.C.3    Bloor, S.J.4    Lewis, D.H.5
  • 9
    • 0033521719 scopus 로고    scopus 로고
    • Variation in the ability of the maize Lc regulatory gene to upregulate flavonoid biosynthesis in heterologous systems
    • Bradley JM, Deroles SC, Boase, Bloor S, Swinny E, Davis KM (1999) Variation in the ability of the maize Lc regulatory gene to upregulate flavonoid biosynthesis in heterologous systems. Plant Sci 140:31-39
    • (1999) Plant Sci , vol.140 , pp. 31-39
    • Bradley, J.M.1    Deroles, S.C.2    Boase3    Bloor, S.4    Swinny, E.5    Davis, K.M.6
  • 10
    • 0031721802 scopus 로고    scopus 로고
    • Polyphenols: Chemistry, dietary sources, metabolism, and nutritional significance
    • Bravo L (1998) Polyphenols: chemistry, dietary sources, metabolism, and nutritional significance. Nutr Rev 56:317-333
    • (1998) Nutr Rev , vol.56 , pp. 317-333
    • Bravo, L.1
  • 11
    • 0030174914 scopus 로고    scopus 로고
    • A null mutation in the first enzyme of flavonoid biosynthesis does not affect male fertility in Arabidopsis
    • Burbulis I, Iacobucci M, B Shirley (1996) A null mutation in the first enzyme of flavonoid biosynthesis does not affect male fertility in Arabidopsis. Plant Cell 8:1013-1025
    • (1996) Plant Cell , vol.8 , pp. 1013-1025
    • Burbulis, I.1    Iacobucci, M.2    Shirley, B.3
  • 12
    • 0028856746 scopus 로고
    • Biological effects of isoflavones in young women: Importance of the chemical composition of soybean products
    • Cassidy A, Bingham S (1995) Biological effects of isoflavones in young women: importance of the chemical composition of soybean products. Brit J Nutr 74:587-601
    • (1995) Brit J Nutr , vol.74 , pp. 587-601
    • Cassidy, A.1    Bingham, S.2
  • 13
    • 0031929267 scopus 로고    scopus 로고
    • Production of yellow colour in flowers: Redirection of flavonoid biosynthesis in Petunia
    • Davies K, Bloor S, Spiller G (1998) Production of yellow colour in flowers: redirection of flavonoid biosynthesis in Petunia. Plant J 13:259-266
    • (1998) Plant J , vol.13 , pp. 259-266
    • Davies, K.1    Bloor, S.2    Spiller, G.3
  • 14
    • 0034666431 scopus 로고    scopus 로고
    • Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli
    • Davis MS, Solbiati J, Cronan, Jr JE (2000) Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli. J Biol Chem 275:28593-28598
    • (2000) J Biol Chem , vol.275 , pp. 28593-28598
    • Davis, M.S.1    Solbiati, J.2    Cronan J.E., Jr.3
  • 16
    • 0033214408 scopus 로고    scopus 로고
    • Flavonoids and isoflavonoids - A gold mine for metabolic engineering
    • Dixon RA, Steele CL (1999) Flavonoids and isoflavonoids - a gold mine for metabolic engineering. Trends Plant Sci 4:394-400
    • (1999) Trends Plant Sci , vol.4 , pp. 394-400
    • Dixon, R.A.1    Steele, C.L.2
  • 17
    • 0032805888 scopus 로고    scopus 로고
    • Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis
    • Ferret JL, Jez JM, Bowman ME, Dixon RA, Noel JP (1999) Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis. Nat Struct Biol 6:775-784
    • (1999) Nat Struct Biol , vol.6 , pp. 775-784
    • Ferret, J.L.1    Jez, J.M.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 19
    • 0030935381 scopus 로고    scopus 로고
    • Stilbene synthase gene expression causes changes in flower colour and male sterility in tobacco
    • Fischer R, Budde I, Hain R (1997) Stilbene synthase gene expression causes changes in flower colour and male sterility in tobacco. Plant J 11:489-498
    • (1997) Plant J , vol.11 , pp. 489-498
    • Fischer, R.1    Budde, I.2    Hain, R.3
  • 20
    • 0035313503 scopus 로고    scopus 로고
    • Metabolic engineering and applications of flavonoids
    • Forkmann G, Martens S (2001) Metabolic engineering and applications of flavonoids. Curr Opin Biotechnol 12:155-160
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 155-160
    • Forkmann, G.1    Martens, S.2
  • 21
    • 0032437643 scopus 로고    scopus 로고
    • Dietary genistein: Prenatal mammary cancer prevention, bioavailability and toxicity testing in rat
    • Frits WA, Coward L, Wang J, CA Lamartiniere (1998) Dietary genistein: prenatal mammary cancer prevention, bioavailability and toxicity testing in rat. Carcinogenesis 19:2152-2158
    • (1998) Carcinogenesis , vol.19 , pp. 2152-2158
    • Frits, W.A.1    Coward, L.2    Wang, J.3    Lamartiniere, C.A.4
  • 22
    • 0028054686 scopus 로고
    • The fadD gene of Escherichia coli K-12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family
    • Fulda M, Heinz E, FP Wolter. (1994) The fadD gene of Escherichia coli K-12 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
  • 24
    • 0028112288 scopus 로고
    • A survey of antifungal compounds from higher plants, 1982-1993
    • Grayer RJ, Harborne JB (1994) A survey of antifungal compounds from higher plants, 1982-1993. Phytochemistry 37:19-42
    • (1994) Phytochemistry , vol.37 , pp. 19-42
    • Grayer, R.J.1    Harborne, J.B.2
  • 26
    • 0000089537 scopus 로고
    • Enzymatic controls in the biosynthesis of lignin and flavonoids
    • Hahlbrock K, Grisebach H (1979) Enzymatic controls in the biosynthesis of lignin and flavonoids. Annu Rev Plant Physiol 30:105-130
    • (1979) Annu Rev Plant Physiol , vol.30 , pp. 105-130
    • Hahlbrock, K.1    Grisebach, H.2
  • 27
    • 0014810955 scopus 로고
    • Stereochemistry of the enzymatic cyclisation of 4,2′,4′ -trihydroxychalcone to 7,4′-dihydroxyflavanone by isomerases from mung bean seedlings
    • Hahlbrock K, Zilg H, Grisebach H (1970) Stereochemistry of the enzymatic cyclisation of 4,2′,4′-trihydroxychalcone to 7,4′ -dihydroxyflavanone by isomerases from mung bean seedlings. Eur J Biochem 15:13-18
    • (1970) Eur J Biochem , vol.15 , pp. 13-18
    • Hahlbrock, K.1    Zilg, H.2    Grisebach, H.3
  • 28
    • 0033151349 scopus 로고    scopus 로고
    • The comparative biochemistry of phytoalexin induction in plants
    • Harborne JB (1999) The comparative biochemistry of phytoalexin induction in plants. Biochem Syst Ecol 27:335-368
    • (1999) Biochem Syst Ecol , vol.27 , pp. 335-368
    • Harborne, J.B.1
  • 29
    • 0030775534 scopus 로고    scopus 로고
    • Absorption, metabolism and health effects of dietary flavonoids in man
    • Hollman PC, Katan MB (1997) Absorption, metabolism and health effects of dietary flavonoids in man. Biomed Pharmacother 51:305-310
    • (1997) Biomed Pharmacother , vol.51 , pp. 305-310
    • Hollman, P.C.1    Katan, M.B.2
  • 30
    • 0028245937 scopus 로고
    • A-factor as a microbial hormone that controls cellular differentiation and secondary metabolism in Streptomyces griseus
    • Horinouchi S, Beppu T (1994) A-factor as a microbial hormone that controls cellular differentiation and secondary metabolism in Streptomyces griseus. Mol Microbiol 12:859-864
    • (1994) Mol Microbiol , vol.12 , pp. 859-864
    • Horinouchi, S.1    Beppu, T.2
  • 31
    • 0028786298 scopus 로고
    • Cinnamate 4-hydroxylase from Cantharanthus roseus, and a strategy for functional expression of plant cytochrome P450 proteins as translational fusions with P450 reductase in E. coli
    • Hotze M, Schröder G, Schröder J (1995) Cinnamate 4-hydroxylase from Cantharanthus roseus, and a strategy for functional expression of plant cytochrome P450 proteins as translational fusions with P450 reductase in E. coli. FEBS Lett 374:345-350
    • (1995) FEBS Lett , vol.374 , pp. 345-350
    • Hotze, M.1    Schröder, G.2    Schröder, J.3
  • 32
    • 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 (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
  • 34
    • 0037059756 scopus 로고    scopus 로고
    • Reaction mechanism of chalcone isomerase
    • Jez JM, Noel JP (2002) Reaction mechanism of chalcone isomerase. J Biol Chem 277:1361-1369
    • (2002) J Biol Chem , vol.277 , pp. 1361-1369
    • Jez, J.M.1    Noel, J.P.2
  • 35
    • 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
  • 36
    • 0016630210 scopus 로고
    • Isoenzymes of p-coumarate:CoA ligase from cell suspension of Glycine max
    • Knobloh KH, Hahlbrock K (1975) Isoenzymes of p-coumarate:CoA ligase from cell suspension of Glycine max. Eur J Biochem 52:311-320
    • (1975) Eur J Biochem , vol.52 , pp. 311-320
    • Knobloh, K.H.1    Hahlbrock, K.2
  • 37
    • 0005604581 scopus 로고    scopus 로고
    • Induction of resistance mechanism against fungal infection of cultivars of Rosa
    • Knott J, Martens S, Forkmann G (2000) Induction of resistance mechanism against fungal infection of cultivars of Rosa. Polyphenols Commun 2:627-628
    • (2000) Polyphenols Commun , vol.2 , pp. 627-628
    • Knott, J.1    Martens, S.2    Forkmann, G.3
  • 38
    • 0016739536 scopus 로고
    • Enzymic synthesis of an aromatic ring from acetate units
    • Kreuzaler F, Hahlbrock K (1975) Enzymic synthesis of an aromatic ring from acetate units. Eur J Biochem 56:205-213
    • (1975) Eur J Biochem , vol.56 , pp. 205-213
    • Kreuzaler, F.1    Hahlbrock, K.2
  • 39
    • 0037070203 scopus 로고    scopus 로고
    • Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein
    • Kyndt JA, Meyer TE, Cusanovich MA, Van Beeumen JJ (2002) Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein. FEBS Lett 512:240-244
    • (2002) FEBS Lett , vol.512 , pp. 240-244
    • Kyndt, J.A.1    Meyer, T.E.2    Cusanovich, M.A.3    Van Beeumen, J.J.4
  • 40
    • 0034086069 scopus 로고    scopus 로고
    • Protection against breast cancer with genistein: A component of soy
    • Lamartiniere CA (2000) Protection against breast cancer with genistein: a component of soy. Am J Clin Nutr 71:1705S-1707S
    • (2000) Am J Clin Nutr , vol.71
    • Lamartiniere, C.A.1
  • 41
    • 0030250380 scopus 로고    scopus 로고
    • Two divergent members of a tobacco 4-coumarate:coenzyme A ligase (4CL) gene family
    • Lee D, Douglas CJ (1996) Two divergent members of a tobacco 4-coumarate:coenzyme A ligase (4CL) gene family. Plant Physiol 112:193-205
    • (1996) Plant Physiol , vol.112 , pp. 193-205
    • Lee, D.1    Douglas, C.J.2
  • 42
    • 0036669812 scopus 로고    scopus 로고
    • Cancer preventive effects of flavonoids - A review
    • Le Marchand 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.1
  • 44
    • 0032839807 scopus 로고    scopus 로고
    • Legumes and soybeans: Overview of their nutritional profiles and health effects
    • Messina MJ (1999) Legumes and soybeans: overview of their nutritional profiles and health effects. Am J Clin Nutr 70:439S-450S
    • (1999) Am J Clin Nutr , vol.70
    • Messina, M.J.1
  • 45
    • 0026654039 scopus 로고
    • Biochemical complementation for chalcone synthase mutants defines a role for flavonols in functional pollen
    • Mo Y, Nagel C, Taylor L (1992) Biochemical complementation for chalcone synthase mutants defines a role for flavonols in functional pollen. Plant Biol 89:7213-7217
    • (1992) Plant Biol , vol.89 , pp. 7213-7217
    • Mo, Y.1    Nagel, C.2    Taylor, L.3
  • 47
    • 0000899360 scopus 로고
    • Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone
    • Mol JNM, Robbins MP, Dixon RA, Veltkamp E (1985) Spontaneous and enzymic rearrangement of naringenin chalcone to flavanone. Phytochemistry 24:2267-2269
    • (1985) Phytochemistry , vol.24 , pp. 2267-2269
    • Mol, J.N.M.1    Robbins, M.P.2    Dixon, R.A.3    Veltkamp, E.4
  • 48
    • 0000355224 scopus 로고
    • Purification and properties of chalcone-flavanone isomerase from soya bean seed
    • Moustafa E, Wong E (1967) Purification and properties of chalcone-flavanone isomerase from soya bean seed. Phytochemistry 6:625-632
    • (1967) Phytochemistry , vol.6 , pp. 625-632
    • Moustafa, E.1    Wong, E.2
  • 49
    • 0035793858 scopus 로고    scopus 로고
    • Biosynthesis of complex polyketides in a metabolically engineered strain of E. coli
    • Pfeifer BA, Admiraal SJ, Gramajo H, Cane DE, Khosla C (2001) Biosynthesis of complex polyketides in a metabolically engineered strain of E. coli. Science 291:1790-1792
    • (2001) Science , vol.291 , pp. 1790-1792
    • Pfeifer, B.A.1    Admiraal, S.J.2    Gramajo, H.3    Cane, D.E.4    Khosla, C.5
  • 50
    • 0035102454 scopus 로고    scopus 로고
    • Biosynthesis of polyketides in heterologous hosts
    • Pfeifer BA, Khosla C (2001) Biosynthesis of polyketides in heterologous hosts. Microbiol Mol Biol Rev 65:106-118
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 106-118
    • Pfeifer, B.A.1    Khosla, C.2
  • 51
    • 0029776005 scopus 로고    scopus 로고
    • Yeast expression of animal and plant P450s in optimized redox environments
    • Pompon D, Louerat B, Bronine A, Urban P (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
  • 52
    • 0030338680 scopus 로고    scopus 로고
    • The genetics and biochemical basis for nodulation of legumes by rhizobia
    • Pueppke JL (1996) The genetics and biochemical basis for nodulation of legumes by rhizobia. Crit Rev Biotechnol 16:1-51
    • (1996) Crit Rev Biotechnol , vol.16 , pp. 1-51
    • Pueppke, J.L.1
  • 53
    • 0033177873 scopus 로고    scopus 로고
    • Molecular analysis of the anthocyanin 2 gene of petunia and its role in the evolution of flower color
    • Quattrocchio F, Wing J, van der Woude K, Souer E, de Vetten N, Mol J, Koes R (1999) Molecular analysis of the anthocyanin 2 gene of petunia and its role in the evolution of flower color. Plant Cell 11:1433-1444
    • (1999) Plant Cell , vol.11 , pp. 1433-1444
    • Quattrocchio, F.1    Wing, J.2    Van Der Woude, K.3    Souer, E.4    De Vetten, N.5    Mol, J.6    Koes, R.7
  • 54
    • 1842287997 scopus 로고    scopus 로고
    • Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity
    • Rösler J, Krekel F, Amrhein N, Schmid J (1997) Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. Plant Physiol 113:175-179
    • (1997) Plant Physiol , vol.113 , pp. 175-179
    • Rösler, J.1    Krekel, F.2    Amrhein, N.3    Schmid, J.4
  • 55
    • 0040241878 scopus 로고    scopus 로고
    • A family of plant-specific polyketide synthases: Facts and predictions
    • Schröder J (1997) A family of plant-specific polyketide synthases: facts and predictions. Trends Plant Sci 2:373-378
    • (1997) Trends Plant Sci , vol.2 , pp. 373-378
    • Schröder, J.1
  • 56
    • 0028112128 scopus 로고
    • Floral flavonoids and the potential for pelargonidin biosynthesis in commercial Chrysanthemum cultivars
    • Schwinn K, Markham K, Given N (1994) Floral flavonoids and the potential for pelargonidin biosynthesis in commercial Chrysanthemum cultivars. Phytochemistry 35:145-150
    • (1994) Phytochemistry , vol.35 , pp. 145-150
    • Schwinn, K.1    Markham, K.2    Given, N.3
  • 57
    • 0026537109 scopus 로고
    • Identification by high-performance liquid chromatography of tyrosine ammonia-lyase activity in purified fraction of Phaseolus vulgaris phenylalanine ammonia-lyase
    • Scott DA, Hammond PM, Brearly GM, Price CP (1992) Identification by high-performance liquid chromatography of tyrosine ammonia-lyase activity in purified fraction of Phaseolus vulgaris phenylalanine ammonia-lyase. J Chromatog B 573:309-312
    • (1992) J Chromatog B , vol.573 , pp. 309-312
    • Scott, D.A.1    Hammond, P.M.2    Brearly, G.M.3    Price, C.P.4
  • 58
    • 0031741906 scopus 로고    scopus 로고
    • Phytoestrogens: The biochemistry, physiology, and implications for human health of soy isoflavones
    • Setchell KD (1998) Phytoestrogens: the biochemistry, physiology, and implications for human health of soy isoflavones. Am J Clin Nutr 68:1333S-1346S
    • (1998) Am J Clin Nutr , vol.68
    • Setchell, K.D.1
  • 59
    • 0033011895 scopus 로고    scopus 로고
    • Dietary isoflavones: Biological effects and relevance to human health
    • Setchell KD, Cassidy A (1999) Dietary isoflavones: biological effects and relevance to human health. J Nutr 129:758S-767S
    • (1999) J Nutr , vol.129
    • Setchell, K.D.1    Cassidy, A.2
  • 60
    • 17544396621 scopus 로고    scopus 로고
    • Mutational analysis of 4-coumarate:CoA ligase identifies functionally important amino acids and verifies its relationship to other adenylate-forming enzymes
    • Stuible HP, Büttner D, Ehlting J, Hahlbrock K, Kombrink E (2000) Mutational analysis of 4-coumarate:CoA ligase identifies functionally important amino acids and verifies its relationship to other adenylate-forming enzymes. FEBS Lett 467:117-122
    • (2000) FEBS Lett , vol.467 , pp. 117-122
    • Stuible, H.P.1    Büttner, D.2    Ehlting, J.3    Hahlbrock, K.4    Kombrink, E.5
  • 61
    • 0024065387 scopus 로고
    • Changes in the intracellular concentration of acetyl-CoA and malonyl-CoA in relation to the carbon and energy metabolism of Escherichia coli K12
    • Takamura Y, Nomura. G (1988) Changes in the intracellular concentration of acetyl-CoA and malonyl-CoA in relation to the carbon and energy metabolism of Escherichia coli K12. J Gen Microbiol 134:2249-2253
    • (1988) J Gen Microbiol , vol.134 , pp. 2249-2253
    • Takamura, Y.1    Nomura, G.2
  • 62
    • 0027055662 scopus 로고
    • Conditional male fertility in chalcone synthase-deficient Petunia
    • Taylor LP, Jorgensen R (1992) Conditional male fertility in chalcone synthase-deficient Petunia. J Hered 83:11-17
    • (1992) J Hered , vol.83 , pp. 11-17
    • Taylor, L.P.1    Jorgensen, R.2
  • 64
    • 0026826809 scopus 로고
    • Antisense inhibition of flavonoid biosynthesis in Petunia anthers results in male sterility
    • van der Meer I, Stam M, van Tunen A, Mol J, Stuitje R (1992) Antisense inhibition of flavonoid biosynthesis in Petunia anthers results in male sterility. Plant Cell 4:253-262
    • (1992) Plant Cell , vol.4 , pp. 253-262
    • Van Der Meer, I.1    Stam, M.2    Van Tunen, A.3    Mol, J.4    Stuitje, R.5
  • 65
    • 0028001912 scopus 로고
    • A vesicular arbuscular mycorrhizal fungus (Glomus intraradix) induces a defense response in alfalfa roots
    • Volpin H, Elkind Y, Okon Y, Kapulnik Y (1994) A vesicular arbuscular mycorrhizal fungus (Glomus intraradix) induces a defense response in alfalfa roots. Plant Physiol 104:683-689
    • (1994) Plant Physiol , vol.104 , pp. 683-689
    • Volpin, H.1    Elkind, Y.2    Okon, Y.3    Kapulnik, Y.4
  • 66
    • 0031688155 scopus 로고    scopus 로고
    • Recent advances in the discovery and development of flavonoids and their analogues as antitumor and anti-HIV agents
    • Wang HK, Xia Y, Yang ZY, Natschke SL, Lee KH (1998) Recent advances in the discovery and development of flavonoids and their analogues as antitumor and anti-HIV agents. Adv Exp Med Biol 439:191-225
    • (1998) Adv Exp Med Biol , vol.439 , pp. 191-225
    • Wang, H.K.1    Xia, Y.2    Yang, Z.Y.3    Natschke, S.L.4    Lee, K.H.5
  • 67
    • 0032082930 scopus 로고    scopus 로고
    • Phenylpropanoid biosynthesis and its regulation
    • Weisshaar B, Jenkins GI (1998) Phenylpropanoid biosynthesis and its regulation. Curr Opin Plant Biol 1:251-257
    • (1998) Curr Opin Plant Biol , vol.1 , pp. 251-257
    • Weisshaar, B.1    Jenkins, G.I.2
  • 68
    • 0026081978 scopus 로고
    • Induced plant responses to pathogen attack: Analysis and heterologous expression of the key enzyme in the biosynthesis of phytoalexins in soybean (Glycine max L. Merr. cv. Harosoy 63)
    • Welle R, Schröder G, Schilts E, Grisbach H, Schröder J (1991) Induced plant responses to pathogen attack: analysis and heterologous expression of the key enzyme in the biosynthesis of phytoalexins in soybean (Glycine max L. Merr. cv. Harosoy 63). Eur J Biochem 196:423-430
    • (1991) Eur J Biochem , vol.196 , pp. 423-430
    • Welle, R.1    Schröder, G.2    Schilts, E.3    Grisbach, H.4    Schröder, J.5
  • 70
    • 0033200340 scopus 로고    scopus 로고
    • Heterologous expression, purification, reconstitution and kinetic analysis of an extended type II polyketide synthase
    • Zawada RJX, Khosla C (1999) Heterologous expression, purification, reconstitution and kinetic analysis of an extended type II polyketide synthase. Chem Biol 6:607-615
    • (1999) Chem Biol , vol.6 , pp. 607-615
    • Zawada, R.J.X.1    Khosla, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.