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Volumn 50, Issue , 1999, Pages 473-503

The shikimate pathway

Author keywords

Aromatic amino acids; Chloroplasts; Plant secondary metabolism; Quinate

Indexed keywords

ANIMALIA; CINCHONA PUBESCENS; EMBRYOPHYTA; EUKARYOTA; PROKARYOTA;

EID: 0033506724     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.50.1.473     Document Type: Article
Times cited : (1006)

References (228)
  • 1
    • 0031470150 scopus 로고    scopus 로고
    • Steady-state kinetics and inhibitor binding of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (tryptophan sensitive) from Escherichia coli
    • Akowski JP, Bauerle R. 1997. Steady-state kinetics and inhibitor binding of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (tryptophan sensitive) from Escherichia coli. Biochemistry 36:15817-22
    • (1997) Biochemistry , vol.36 , pp. 15817-15822
    • Akowski, J.P.1    Bauerle, R.2
  • 3
    • 0020570726 scopus 로고
    • Biochemical basis for glyphosate tolerance in a bacterium and a plant tissue culture
    • Amrhein N, Johänning D, Schab J, Schulz A. 1983. Biochemical basis for glyphosate tolerance in a bacterium and a plant tissue culture. FEBS Lett. 157:191-96
    • (1983) FEBS Lett. , vol.157 , pp. 191-196
    • Amrhein, N.1    Johänning, D.2    Schab, J.3    Schulz, A.4
  • 4
    • 0000305142 scopus 로고
    • Kinetic and structural analysis of enzyme intermediates: Lessons from EPSP synthase
    • Anderson KS, Johnson KA. 1990. Kinetic and structural analysis of enzyme intermediates: lessons from EPSP synthase. Chem. Rev. 90:1131-49
    • (1990) Chem. Rev. , vol.90 , pp. 1131-1149
    • Anderson, K.S.1    Johnson, K.A.2
  • 5
    • 0024286625 scopus 로고
    • Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase
    • Anton IA, Coggins JR. 1988. Sequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenase. Biochem. J. 249:319-26
    • (1988) Biochem. J. , vol.249 , pp. 319-326
    • Anton, I.A.1    Coggins, J.R.2
  • 6
    • 13144258781 scopus 로고    scopus 로고
    • Biosynthesis of the ansamycin antibiotic rifamycin: Deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699
    • August PR, Tang L, Yoon YJ, Ning S, Müller R, et al. 1998. Biosynthesis of the ansamycin antibiotic rifamycin: deductions from the molecular analysis of the rif biosynthetic gene cluster of Amyco-latopsis mediterranei S699. Chem. Biol. 5:69-79
    • (1998) Chem. Biol. , vol.5 , pp. 69-79
    • August, P.R.1    Tang, L.2    Yoon, Y.J.3    Ning, S.4    Müller, R.5
  • 7
    • 0024465729 scopus 로고
    • Is the first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (tyrosine sensitive), a copper metalloenzyme?
    • Baasov T, Knowles JR. 1989. Is the first enzyme of the shikimate pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (tyrosine sensitive), a copper metalloenzyme? J. Bacteriol. 171: 6155-60
    • (1989) J. Bacteriol. , vol.171 , pp. 6155-6160
    • Baasov, T.1    Knowles, J.R.2
  • 8
    • 0001547222 scopus 로고
    • Observation of an isotope effect in the chorismate synthase reaction
    • Balasubramanian S, Abell C, Coggins JR. 1990. Observation of an isotope effect in the chorismate synthase reaction. J. Am. Chem. Soc. 112:8581-83
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 8581-8583
    • Balasubramanian, S.1    Abell, C.2    Coggins, J.R.3
  • 10
    • 0028246936 scopus 로고
    • Divergence between the enzymecatalyzed and noncatalyzed synthesis of 3-dehydroquinate
    • Bartlett PA, McLaren KL, Marx MA. 1994. Divergence between the enzymecatalyzed and noncatalyzed synthesis of 3-dehydroquinate. J. Org. Chem. 59: 2082-85
    • (1994) J. Org. Chem. , vol.59 , pp. 2082-2085
    • Bartlett, P.A.1    McLaren, K.L.2    Marx, M.A.3
  • 11
    • 0001650027 scopus 로고
    • Does dehydroquinate synthase synthesize dehydroquinate?
    • Bartlett PA, Satake K. 1988. Does dehydroquinate synthase synthesize dehydroquinate? J. Am. Chem. Soc. 110:1628-30
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1628-1630
    • Bartlett, P.A.1    Satake, K.2
  • 12
    • 0030394616 scopus 로고    scopus 로고
    • Identification of runner bean genotypes (Phaseolus cossineus L.) by isoenzyme analysis
    • Belletti P, Lotito S. 1996. Identification of runner bean genotypes (Phaseolus cossineus L.) by isoenzyme analysis. J. Genet. Breed. 50:185-90
    • (1996) J. Genet. Breed. , vol.50 , pp. 185-190
    • Belletti, P.1    Lotito, S.2
  • 13
    • 0024974067 scopus 로고
    • Dehydroquinate synthase: The role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis
    • Bender SL, Mehdi S, Knowles JR. 1989. Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry 28:7555-60
    • (1989) Biochemistry , vol.28 , pp. 7555-7560
    • Bender, S.L.1    Mehdi, S.2    Knowles, J.R.3
  • 14
    • 0024974063 scopus 로고
    • Dehydroquinate synthase: The use of substrate analogues to probe the early steps of the catalyzed reaction
    • Bender SL, Widlanski T, Knowles JR. 1989. Dehydroquinate synthase: the use of substrate analogues to probe the early steps of the catalyzed reaction. Biochemistry 28:7560-72
    • (1989) Biochemistry , vol.28 , pp. 7560-7572
    • Bender, S.L.1    Widlanski, T.2    Knowles, J.R.3
  • 15
    • 0000975821 scopus 로고
    • Sequence requirements of the 5-enolpyruvylshikimate 3-phosphate synthase 5′-upstream region for tissue-specific expression in flowers and seedlings
    • Benfey PN, Takatsuji H, Ren L, Shah DM, Chua NH. 1990. Sequence requirements of the 5-enolpyruvylshikimate 3-phosphate synthase 5′-upstream region for tissue-specific expression in flowers and seedlings. Plant Cell 2:849-56
    • (1990) Plant Cell , vol.2 , pp. 849-856
    • Benfey, P.N.1    Takatsuji, H.2    Ren, L.3    Shah, D.M.4    Chua, N.H.5
  • 16
    • 0025581736 scopus 로고
    • The shikimate pathway - A metabolic tree with many branches
    • Bentley R. 1990. The shikimate pathway - a metabolic tree with many branches. CRC Crit. Rev. Biochem. Mol. Biol. 25:307-84
    • (1990) CRC Crit. Rev. Biochem. Mol. Biol. , vol.25 , pp. 307-384
    • Bentley, R.1
  • 17
    • 0030130404 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding a 3-dehydroquinate synthase from a higher plant, and analysis of the organ-specific and elicitor-induced expression of the corresponding gene
    • Bischoff M, Rösler J, Raesecke HR, Görlach J, Amrhein N, Schmid J. 1996. Cloning of a cDNA encoding a 3-dehydroquinate synthase from a higher plant, and analysis of the organ-specific and elicitor-induced expression of the corresponding gene. Plant Mol. Biol. 31:69-76
    • (1996) Plant Mol. Biol. , vol.31 , pp. 69-76
    • Bischoff, M.1    Rösler, J.2    Raesecke, H.R.3    Görlach, J.4    Amrhein, N.5    Schmid, J.6
  • 19
    • 0031047708 scopus 로고    scopus 로고
    • Evidence that the active site in type II dehydroquinase from Streptomyces coelicolor is near the single tryptophan
    • Boam DJ, Price NC, Kelly SM, Krell T, Coggins JR. 1997. Evidence that the active site in type II dehydroquinase from Streptomyces coelicolor is near the single tryptophan. Biochem. Soc. Trans. 25: S93
    • (1997) Biochem. Soc. Trans. , vol.25
    • Boam, D.J.1    Price, N.C.2    Kelly, S.M.3    Krell, T.4    Coggins, J.R.5
  • 20
    • 0027965624 scopus 로고
    • Cloning of cDNA encoding the bifunctional dehydroqinase shikimate dehydrogenase of aromatic amino acid biosynthesis in Nicotiana tabacum
    • Bonner CA, Jensen RA. 1994. Cloning of cDNA encoding the bifunctional dehydroqinase shikimate dehydrogenase of aromatic amino acid biosynthesis in M-cotiana tabacum. Biochem. J. 302:11-14
    • (1994) Biochem. J. , vol.302 , pp. 11-14
    • Bonner, C.A.1    Jensen, R.A.2
  • 21
    • 0029743937 scopus 로고    scopus 로고
    • The transient kinetics of Escherichia coli chorismate synthase: Substrate consumption, phosphate dissociation, and characterization of a flavin intermediate
    • Bornemann S, Lowe DJ, Thorneley RNF. 1996. The transient kinetics of Escherichia coli chorismate synthase: substrate consumption, phosphate dissociation, and characterization of a flavin intermediate. Biochemistry 35:9907-16
    • (1996) Biochemistry , vol.35 , pp. 9907-9916
    • Bornemann, S.1    Lowe, D.J.2    Thorneley, R.N.F.3
  • 22
    • 0029833135 scopus 로고    scopus 로고
    • Cloning, sequencing, expression, purification and preliminary characterization of a type II dehydroquinase from Helicobacter pylori
    • Bottomley JR, Clayton CL, Chalk PA, Kleanthous C. 1996. Cloning, sequencing, expression, purification and preliminary characterization of a type II dehydroquinase from Helicobacter pylori. Biochem. J. 319:559-65
    • (1996) Biochem. J. , vol.319 , pp. 559-565
    • Bottomley, J.R.1    Clayton, C.L.2    Chalk, P.A.3    Kleanthous, C.4
  • 24
    • 0029845997 scopus 로고    scopus 로고
    • Enzymatic properties of chorismate synthase isoenzymes of tomato (Lycopersicon esculentum Mill.)
    • Braun M, Henstrand JM, Görlach J, Amrhein N, Schmid J. 1996. Enzymatic properties of chorismate synthase isoenzymes of tomato (Lycopersicon esculentum Mill.). Planta 200:64-70
    • (1996) Planta , vol.200 , pp. 64-70
    • Braun, M.1    Henstrand, J.M.2    Görlach, J.3    Amrhein, N.4    Schmid, J.5
  • 25
    • 0025353911 scopus 로고
    • Hydroaromatic metabolism in Rhodococcus rhodochrous: Purification and characterization of its NAD-dependent quinate dehydrogenase
    • Bruce NC, Cain RB. 1990. Hydroaromatic metabolism in Rhodococcus rhodochrous: purification and characterization of its NAD-dependent quinate dehydrogenase. Arch. Microbiol. 154:179-96
    • (1990) Arch. Microbiol. , vol.154 , pp. 179-196
    • Bruce, N.C.1    Cain, R.B.2
  • 26
    • 0025878005 scopus 로고
    • An amino acid sequence motif observed amongst enzymes of the shikimate pathway
    • Bugg TDH, Alefounder PR, Abell C. 1991. An amino acid sequence motif observed amongst enzymes of the shikimate pathway. Biochem. J. 276:841-43
    • (1991) Biochem. J. , vol.276 , pp. 841-843
    • Bugg, T.D.H.1    Alefounder, P.R.2    Abell, C.3
  • 27
    • 84985595085 scopus 로고
    • The genetic control of seven isoenzymic loci in Vicia faba L. Identification of lines and estimates of outcrossing rates between plants pollinated by bumblebees
    • Carre S, Tasei JN, Guen JL, Mesquida J, Morin G. 1993. The genetic control of seven isoenzymic loci in Vicia faba L. Identification of lines and estimates of outcrossing rates between plants pollinated by bumblebees. Ann. Appl. Biol. 122:555-68
    • (1993) Ann. Appl. Biol. , vol.122 , pp. 555-568
    • Carre, S.1    Tasei, J.N.2    Guen, J.L.3    Mesquida, J.4    Morin, G.5
  • 28
    • 0004706456 scopus 로고
    • Biosynthesis of ansatrienin. Nonincorporation of shikimic acid into the mC7N unit and stereochemistry of its conversion to the cyclohexanecarboxylic acid moiety
    • Casati R, Beale JM, Floss HG. 1987. Biosynthesis of ansatrienin. Nonincorporation of shikimic acid into the mC7N unit and stereochemistry of its conversion to the cyclohexanecarboxylic acid moiety. J. Am. Chem. Soc. 109:8102-4
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 8102-8104
    • Casati, R.1    Beale, J.M.2    Floss, H.G.3
  • 29
    • 0022644082 scopus 로고
    • The isolation and nucleotide sequence of the complex AROM locus of Aspergillus nidulans
    • Charles IG, Keyte JW, Brammar WJ, Smith M, Hawkins AR. 1986. The isolation and nucleotide sequence of the complex AROM locus of Aspergillus nidulans. Nucleic Acids Res. 14:2201-13
    • (1986) Nucleic Acids Res. , vol.14 , pp. 2201-2213
    • Charles, I.G.1    Keyte, J.W.2    Brammar, W.J.3    Smith, M.4    Hawkins, A.R.5
  • 30
    • 0025877807 scopus 로고
    • Identification of the active-site lysine residue of two biosynthetic 3-dehydroquinases
    • Chaudhuri S, Duncan K, Graham LD, Coggins JR. 1991. Identification of the active-site lysine residue of two biosynthetic 3-dehydroquinases. Biochem. J. 275:1-6
    • (1991) Biochem. J. , vol.275 , pp. 1-6
    • Chaudhuri, S.1    Duncan, K.2    Graham, L.D.3    Coggins, J.R.4
  • 31
    • 0028017302 scopus 로고
    • The characterization of the shikimate pathway enzyme dehydroquinase from Pisum sativum
    • Deka RK, Anton IA, Dunbar B, Coggins JR. 1994. The characterization of the shikimate pathway enzyme dehydroquinase from Pisum sativum. FEBS Lett. 349:397-402
    • (1994) FEBS Lett. , vol.349 , pp. 397-402
    • Deka, R.K.1    Anton, I.A.2    Dunbar, B.3    Coggins, J.R.4
  • 32
    • 0026592053 scopus 로고
    • Identification of the essential histidine residue at the active site of Escherichia coli dehdroquinase
    • Deka RK, Kleanthous C, Coggins JR. 1992. Identification of the essential histidine residue at the active site of Escherichia coli dehdroquinase. J. Biol. Chem. 267:22237-42
    • (1992) J. Biol. Chem. , vol.267 , pp. 22237-22242
    • Deka, R.K.1    Kleanthous, C.2    Coggins, J.R.3
  • 33
    • 0022535128 scopus 로고
    • Translocation of the precursor of 5-enolpyruvylshikimate 3-phosphate synthase into chloroplasts of higher plants in vitro
    • Della-Cioppa G, Bauer SC, Klein BK, Shah DM, Fraley RT, Kishore GM. 1986. Translocation of the precursor of 5-enolpyruvylshikimate 3-phosphate synthase into chloroplasts of higher plants in vitro. Proc. Natl Acad. Sci. USA 83: 6873-77
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 6873-6877
    • Della-Cioppa, G.1    Bauer, S.C.2    Klein, B.K.3    Shah, D.M.4    Fraley, R.T.5    Kishore, G.M.6
  • 34
    • 0032007403 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • Dewick PM. 1998. The biosynthesis of shikimate metabolites. Nat. Prod. Rep. 15:17-58
    • (1998) Nat. Prod. Rep. , vol.15 , pp. 17-58
    • Dewick, P.M.1
  • 35
    • 0344043193 scopus 로고    scopus 로고
    • Shikimate dehydrogenase from pepper (Capsicum annum) seedlings. Purification and properties
    • Diaz J, Merino F. 1997. Shikimate dehydrogenase from pepper (Capsicum annum) seedlings. Purification and properties. Physiol. Plant. 100:147-52
    • (1997) Physiol. Plant. , vol.100 , pp. 147-152
    • Diaz, J.1    Merino, F.2
  • 36
    • 0031889288 scopus 로고    scopus 로고
    • Wound-induced shikimate dehydrogenase and peroxidase related to lignification in pepper (Capsicum annum L.)
    • Diaz J, Merino F. 1998. Wound-induced shikimate dehydrogenase and peroxidase related to lignification in pepper (Capsicum annum L.). J. Plant Physiol. 152:51-57
    • (1998) J. Plant Physiol. , vol.152 , pp. 51-57
    • Diaz, J.1    Merino, F.2
  • 37
    • 0001588624 scopus 로고
    • The cytosolic iso-enzyme of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Spinacia oleracea and other higher plants: Extreme substrate ambiguity and other properties
    • Doong RL, Gander JE, Ganson RJ, Jensen RA. 1992. The cytosolic iso-enzyme of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Spinacia oleracea and other higher plants: extreme substrate ambiguity and other properties. Physiol. Plant. 84:351-60
    • (1992) Physiol. Plant. , vol.84 , pp. 351-360
    • Doong, R.L.1    Gander, J.E.2    Ganson, R.J.3    Jensen, R.A.4
  • 38
    • 0022784669 scopus 로고
    • The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase
    • Duncan K, Chaudhuri S, Campbell MS, Coggins JR. 1986. The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase. Biochem. J. 238:475-83
    • (1986) Biochem. J. , vol.238 , pp. 475-483
    • Duncan, K.1    Chaudhuri, S.2    Campbell, M.S.3    Coggins, J.R.4
  • 39
    • 0023414737 scopus 로고
    • The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains
    • Duncan K, Edwards MR, Coggins JR. 1987. The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains. Biochem J. 246:375-86
    • (1987) Biochem J. , vol.246 , pp. 375-386
    • Duncan, K.1    Edwards, M.R.2    Coggins, J.R.3
  • 42
    • 0028125023 scopus 로고
    • The pca-pob supraoperonic cluster of Acinetobacter calcoaceticus contains quiA, the structural gene for quinate-shikimate dehydrogenase
    • Elsemore DA, Ornston LN. 1994. The pca-pob supraoperonic cluster of Acinetobacter calcoaceticus contains quiA, the structural gene for quinate-shikimate dehydrogenase. J. Bacteriol. 176:7659-66
    • (1994) J. Bacteriol. , vol.176 , pp. 7659-7666
    • Elsemore, D.A.1    Ornston, L.N.2
  • 43
    • 0028820070 scopus 로고
    • Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus
    • Elsemore DA, Omston LN. 1995. Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus. J. Bacteriol. 177:5971-78
    • (1995) J. Bacteriol. , vol.177 , pp. 5971-5978
    • Elsemore, D.A.1    Omston, L.N.2
  • 44
    • 0026483810 scopus 로고
    • Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica
    • Euverink GJW, Hessels GI, Vrijbloed JW, Coggins JR, Dijkhuizen L. 1992. Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica. J. Gen. Microbiol. 138:2449-57
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2449-2457
    • Euverink, G.J.W.1    Hessels, G.I.2    Vrijbloed, J.W.3    Coggins, J.R.4    Dijkhuizen, L.5
  • 45
    • 0030948513 scopus 로고    scopus 로고
    • Properties of the 5-enolpyruvyl-shikimate 3-phosphate synthase isoforms isolated from maize cultured cells
    • Forlani G. 1997. Properties of the 5-enolpyruvyl-shikimate 3-phosphate synthase isoforms isolated from maize cultured cells. J. Plant Physiol. 150:369-75
    • (1997) J. Plant Physiol. , vol.150 , pp. 369-375
    • Forlani, G.1
  • 46
    • 0028119605 scopus 로고
    • 5-enol-pyruvyl-shikimate 3-phosphate synthase from Zea mays cultured cells
    • Forlani G, Parisi B, Nielsen E. 1994. 5-enol-pyruvyl-shikimate 3-phosphate synthase from Zea mays cultured cells. Plant Physiol. 105:1107-14
    • (1994) Plant Physiol. , vol.105 , pp. 1107-1114
    • Forlani, G.1    Parisi, B.2    Nielsen, E.3
  • 47
    • 0021760658 scopus 로고
    • Dehydroquinate synthase from Escherichia coli: Purification, cloning, and construction of overproducers of the enzyme
    • Frost JW, Bender JL, Kadonaga JT, Knowles JR. 1984. Dehydroquinate synthase from Escherichia coli: purification, cloning, and construction of overproducers of the enzyme. Biochemistry 23:4470-75
    • (1984) Biochemistry , vol.23 , pp. 4470-4475
    • Frost, J.W.1    Bender, J.L.2    Kadonaga, J.T.3    Knowles, J.R.4
  • 48
    • 0025742991 scopus 로고
    • The Mycobacterium tuberculosis shikimate pathway genes: Evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases
    • Garbe T, Selvos S, Hawkins A, Dimitriadis G, Young D, et al. 1991. The Mycobacterium tuberculosis shikimate pathway genes: evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases. Mol. Gen. Genet. 228: 385-92
    • (1991) Mol. Gen. Genet. , vol.228 , pp. 385-392
    • Garbe, T.1    Selvos, S.2    Hawkins, A.3    Dimitriadis, G.4    Young, D.5
  • 50
    • 0021958412 scopus 로고
    • Operator mutations of the Escherichia coli aroF gene
    • Garner CC, Herrmann KM. 1985. Operator mutations of the Escherichia coli aroF gene. J. Biol. Chem. 260:3820-25
    • (1985) J. Biol. Chem. , vol.260 , pp. 3820-3825
    • Garner, C.C.1    Herrmann, K.M.2
  • 51
    • 0025363625 scopus 로고
    • A Brassica napus gene encoding 5-enolpyruvylshikimate 3-phosphate synthase
    • Gasser CS, Klee HJ. 1990. A Brassica napus gene encoding 5-enolpyruvylshikimate 3-phosphate synthase. Nucleic Acids Res. 18:2821
    • (1990) Nucleic Acids Res. , vol.18 , pp. 2821
    • Gasser, C.S.1    Klee, H.J.2
  • 52
    • 0024296415 scopus 로고
    • Structure, expression, and evolution of the 5-enolpyruvylshikimate 3-phosphate synthase genes of petunia and tomato
    • Gasser CS, Winter JA, Hironaka CM, Shah DM. 1988. Structure, expression, and evolution of the 5-enolpyruvylshikimate 3-phosphate synthase genes of petunia and tomato. J. Biol. Chem. 263: 4280-89
    • (1988) J. Biol. Chem. , vol.263 , pp. 4280-4289
    • Gasser, C.S.1    Winter, J.A.2    Hironaka, C.M.3    Shah, D.M.4
  • 53
    • 0024400630 scopus 로고
    • DNA sequence, organization and regulation of the qa gene cluster of Neurospora crassa
    • Geever RF, Huiet L, Baum JA, Tyler BM, Patel VB, et al. 1989. DNA sequence, organization and regulation of the qa gene cluster of Neurospora crassa. J. Mol. Biol. 207:15-34
    • (1989) J. Mol. Biol. , vol.207 , pp. 15-34
    • Geever, R.F.1    Huiet, L.2    Baum, J.A.3    Tyler, B.M.4    Patel, V.B.5
  • 54
    • 0028171435 scopus 로고
    • A single Ser-180 mutation desensitizes feedback inhibition of the phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthetase in Escherichia coli
    • Ger YM, Chen SL, Chiang HJ, Shiuan D. 1994. A single Ser-180 mutation desensitizes feedback inhibition of the phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthetase in Escherichia coli. J. Biochem. 116:986-90
    • (1994) J. Biochem. , vol.116 , pp. 986-990
    • Ger, Y.M.1    Chen, S.L.2    Chiang, H.J.3    Shiuan, D.4
  • 55
    • 0031938056 scopus 로고    scopus 로고
    • PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter
    • Gerischer U, Segura A, Ornston LN. 1998. PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter. J. Bacteriol. 180:1512-24
    • (1998) J. Bacteriol. , vol.180 , pp. 1512-1524
    • Gerischer, U.1    Segura, A.2    Ornston, L.N.3
  • 56
    • 0021829055 scopus 로고
    • Gene organization and regulation in the qa (quinic acid) gene cluster of Neurospora crassa
    • Giles NH, Case ME, Baum J, Geever R, Hulet L, et al. 1985. Gene organization and regulation in the qa (quinic acid) gene cluster of Neurospora crassa. Microbiol. Rev. 49:338-58
    • (1985) Microbiol. Rev. , vol.49 , pp. 338-358
    • Giles, N.H.1    Case, M.E.2    Baum, J.3    Geever, R.4    Hulet, L.5
  • 58
    • 0027690077 scopus 로고
    • Differential expression of tomato (Lycopersicon esculentum L.) genes encoding shikimate pathway isoenzymes. I. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
    • Görlach J, Beck A, Henstrand JM, Handa AK, Herrmann KM, et al. 1993. Differential expression of tomato (Lycopersicon esculentum L.) genes encoding shikimate pathway isoenzymes. I. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. Plant Mol. Biol. 23:697-706
    • (1993) Plant Mol. Biol. , vol.23 , pp. 697-706
    • Görlach, J.1    Beck, A.2    Henstrand, J.M.3    Handa, A.K.4    Herrmann, K.M.5
  • 59
    • 0029360656 scopus 로고
    • Organspecific differences in the ratio of alternatively spliced chorismate synthase (LeCS2) transcripts in tomato
    • Görlach J, Raesecke HR, Abel G, Wehli R, Amrhein N, Schmid J. 1995. Organspecific differences in the ratio of alternatively spliced chorismate synthase (LeCS2) transcripts in tomato. Plant J. 8:451-56
    • (1995) Plant J. , vol.8 , pp. 451-456
    • Görlach, J.1    Raesecke, H.R.2    Abel, G.3    Wehli, R.4    Amrhein, N.5    Schmid, J.6
  • 60
    • 0028969717 scopus 로고
    • Temporally distinct accumulation of transcripts encoding enzymes of the prechorismate pathway in elicitor-treated, cultured tomato cells
    • Görlach J, Raesecke HR, Rentsch D, Regenass M, Roy P, et al. 1995. Temporally distinct accumulation of transcripts encoding enzymes of the prechorismate pathway in elicitor-treated, cultured tomato cells. Proc. Natl. Acad. Sci. USA 92:3166-70
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3166-3170
    • Görlach, J.1    Raesecke, H.R.2    Rentsch, D.3    Regenass, M.4    Roy, P.5
  • 61
    • 0027691504 scopus 로고
    • Differential expression of tomato (Lycopersicon esculentum L.) genes encoding shikimate pathway isoenzymes. II. Chorismate synthase
    • Görlach J, Schmid J, Amrhein N. 1993. Differential expression of tomato (Lycopersicon esculentum L.) genes encoding shikimate pathway isoenzymes. II. Chorismate synthase. Plant Mol. Biol 23:707-16
    • (1993) Plant Mol. Biol , vol.23 , pp. 707-716
    • Görlach, J.1    Schmid, J.2    Amrhein, N.3
  • 62
    • 0028080629 scopus 로고
    • Abundance of transcripts specific for genes encoding enzymes of the prechorismate pathway in different organs of tomato (Lycopersicon esculentum L.) plants
    • Görlach J, Schmid J, Amrhein N. 1994. Abundance of transcripts specific for genes encoding enzymes of the prechorismate pathway in different organs of tomato (Lycopersicon esculentum L.) plants. Planta 193:216-23
    • (1994) Planta , vol.193 , pp. 216-223
    • Görlach, J.1    Schmid, J.2    Amrhein, N.3
  • 64
    • 0023958771 scopus 로고
    • Genetic regulation of the quinic acid utilization (qut) gene cluster in Aspergillus nidulans
    • Grant S, Roberts CF, Lamb H, Stout M, Hawkins AR. 1988. Genetic regulation of the quinic acid utilization (qut) gene cluster in Aspergillus nidulans. J. Gen. Microbiol 134:347-58
    • (1988) J. Gen. Microbiol , vol.134 , pp. 347-358
    • Grant, S.1    Roberts, C.F.2    Lamb, H.3    Stout, M.4    Hawkins, A.R.5
  • 65
    • 0021762551 scopus 로고
    • A calcium binding protein is a regulatory subunit of quinate:NAD oxidoreductase from dark-grown carrot cells
    • Graziana A, Dillenschneider M, Ranjeva R. 1984. A calcium binding protein is a regulatory subunit of quinate:NAD oxidoreductase from dark-grown carrot cells. Biochem. Biophys. Res. Commun. 125:774-83
    • (1984) Biochem. Biophys. Res. Commun. , vol.125 , pp. 774-783
    • Graziana, A.1    Dillenschneider, M.2    Ranjeva, R.3
  • 66
    • 0029142129 scopus 로고
    • The gene (aroK) encoding shikimate kinase I from Escherichia coli
    • Griffin HG, Gasson MJ. 1995. The gene (aroK) encoding shikimate kinase I from Escherichia coli. DNA Sequence 5:195-97
    • (1995) DNA Sequence , vol.5 , pp. 195-197
    • Griffin, H.G.1    Gasson, M.J.2
  • 67
    • 0040395940 scopus 로고
    • Regulation of the aroH operon of Escherichia coli by the tryptophan represser
    • Grove CL, Gunsalus RP. 1987. Regulation of the aroH operon of Escherichia coli by the tryptophan represser. J. Bacterial. 173:3601-4
    • (1987) J. Bacterial. , vol.173 , pp. 3601-3604
    • Grove, C.L.1    Gunsalus, R.P.2
  • 68
    • 0027317964 scopus 로고
    • Steady-state kinetic evaluation of the reverse reaction for Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase
    • Gruys KJ, Marzabadi MR, Pansegrau PD, Sikorski JA. 1993. Steady-state kinetic evaluation of the reverse reaction for Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase. Arch. Biochem. Biophys. 304:345-51
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 345-351
    • Gruys, K.J.1    Marzabadi, M.R.2    Pansegrau, P.D.3    Sikorski, J.A.4
  • 69
    • 0029005482 scopus 로고
    • Evidence for cross-pathway regulation of metabolic gene expression in plants
    • Guyer D, Patton D, Ward E. 1995. Evidence for cross-pathway regulation of metabolic gene expression in plants. Proc. Natl. Acad. Sci. USA 92:4997-5000
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4997-5000
    • Guyer, D.1    Patton, D.2    Ward, E.3
  • 70
    • 0025219764 scopus 로고
    • Study of the biosynthesis of rifamycin-chromophore in Nocardia mediterranei
    • Gygax D, Ghisalba O, Treichler H, Nuesch J. 1990. Study of the biosynthesis of rifamycin-chromophore in Nocardia mediterranei. J. Antibiot. 43:324-26
    • (1990) J. Antibiot. , vol.43 , pp. 324-326
    • Gygax, D.1    Ghisalba, O.2    Treichler, H.3    Nuesch, J.4
  • 71
    • 0030425947 scopus 로고    scopus 로고
    • Use of isoenzyme analysis in breeding of synthetic rapeseed cultivars
    • Hackenberg EM, Kohler W. 1996. Use of isoenzyme analysis in breeding of synthetic rapeseed cultivars. Plant Breed. 115:474-79
    • (1996) Plant Breed. , vol.115 , pp. 474-479
    • Hackenberg, E.M.1    Kohler, W.2
  • 72
    • 0027951452 scopus 로고
    • Effect of gibberellic acid on berberine and tyrosine accumulation in Coptis japonica
    • Hara Y, Laugel T, Morimoto T, Yamada Y. 1994. Effect of gibberellic acid on berberine and tyrosine accumulation in Coptis japonica. Phytochemistry 36:643-46
    • (1994) Phytochemistry , vol.36 , pp. 643-646
    • Hara, Y.1    Laugel, T.2    Morimoto, T.3    Yamada, Y.4
  • 74
    • 0025134148 scopus 로고
    • Chorismate synthase, presteady-state kinetics of phosphate release from 5-enolpyruvylshikimate 3-phosphate
    • Hawkes TR, Lewis T, Coggins JR, Mousedale DM, Lowe DJ, Thorneley RNF. 1990. Chorismate synthase, presteady-state kinetics of phosphate release from 5-enolpyruvylshikimate 3-phosphate. Biochem. J. 265:899-902
    • (1990) Biochem. J. , vol.265 , pp. 899-902
    • Hawkes, T.R.1    Lewis, T.2    Coggins, J.R.3    Mousedale, D.M.4    Lowe, D.J.5    Thorneley, R.N.F.6
  • 75
    • 0027764649 scopus 로고
    • Genesis of eukaryotic transcriptional activator and repressor proteins by splitting a multidomain anabolic enzyme
    • Hawkins AR, Lamb HK, Moore JD, Roberts CF. 1993. Genesis of eukaryotic transcriptional activator and repressor proteins by splitting a multidomain anabolic enzyme. Gene 136:49-54
    • (1993) Gene , vol.136 , pp. 49-54
    • Hawkins, A.R.1    Lamb, H.K.2    Moore, J.D.3    Roberts, C.F.4
  • 76
    • 0026515476 scopus 로고
    • Structure of the Aspergillus nidulans qut repressor-encoding gene: Implications for the regulation of transcription initiation
    • Hawkins AR, Lamb HK, Roberts CE 1992. Structure of the Aspergillus nidulans qut repressor-encoding gene: implications for the regulation of transcription initiation. Gene 110:109-14
    • (1992) Gene , vol.110 , pp. 109-114
    • Hawkins, A.R.1    Lamb, H.K.2    Roberts, C.E.3
  • 77
    • 0026023427 scopus 로고
    • Domain structure and interaction within the pentafunctional arom polypeptide
    • Hawkins AR, Smith M. 1991. Domain structure and interaction within the pentafunctional arom polypeptide. Eur. J. Biochem. 196:717-24
    • (1991) Eur. J. Biochem. , vol.196 , pp. 717-724
    • Hawkins, A.R.1    Smith, M.2
  • 78
    • 0026525555 scopus 로고
    • Synergism between the trp repressor and tyr represser in repression of the aroL promoter of Escherichia coli K-12
    • Heatwole VM, Somerville RL. 1992. Synergism between the trp repressor and tyr represser in repression of the aroL promoter of Escherichia coli K-12. J. Bacterial. 174:331-35
    • (1992) J. Bacterial. , vol.174 , pp. 331-335
    • Heatwole, V.M.1    Somerville, R.L.2
  • 79
    • 0024240284 scopus 로고
    • 3-deoxy-D-manno-octulosonate 8-phosphate synthase catalyzes the C-O bond cleavage of phosphoenolpyruvate
    • Hedstrom L, Abeles R. 1988. 3-deoxy-D-manno-octulosonate 8-phosphate synthase catalyzes the C-O bond cleavage of phosphoenolpyruvate. Biochem. Biophys. Res. Commun. 157:816-20
    • (1988) Biochem. Biophys. Res. Commun. , vol.157 , pp. 816-820
    • Hedstrom, L.1    Abeles, R.2
  • 80
    • 0029157798 scopus 로고
    • Cloning and characterization of a heterologously expressed bifunctional chorismate synthase/flavin reductase from Neurospora crassa
    • Henstrand JM, Amrhein N, Schmid J. 1995. Cloning and characterization of a heterologously expressed bifunctional chorismate synthase/flavin reductase from Neurospora crassa. J. Biol. Chem. 270:20447-52
    • (1995) J. Biol. Chem. , vol.270 , pp. 20447-20452
    • Henstrand, J.M.1    Amrhein, N.2    Schmid, J.3
  • 81
    • 0001490638 scopus 로고
    • Light and fungal elicitor induce 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase mRNA in suspension cultured cells of parsley (Petroselinum crispum L.)
    • Henstrand JM, McCue KF, Brink K, Handa AK, Herrmann KM, Conn EE. 1992. Light and fungal elicitor induce 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase mRNA in suspension cultured cells of parsley (Petroselinum crispum L.). Plant Physiol. 98:761-63
    • (1992) Plant Physiol. , vol.98 , pp. 761-763
    • Henstrand, J.M.1    McCue, K.F.2    Brink, K.3    Handa, A.K.4    Herrmann, K.M.5    Conn, E.E.6
  • 82
    • 0028796502 scopus 로고
    • Only the mature form of the plastidic chorismate synthase is enzymatically active
    • Henstrand JM, Schmid J, Amrhein N. 1995. Only the mature form of the plastidic chorismate synthase is enzymatically active. Plant Physiol. 108:1127-32
    • (1995) Plant Physiol. , vol.108 , pp. 1127-1132
    • Henstrand, J.M.1    Schmid, J.2    Amrhein, N.3
  • 83
    • 0011946506 scopus 로고
    • The common aromatic biosynthetic pathway
    • ed. KM Herrmann, RL Somerville, London: Addison-Wesley. 453 pp
    • Herrmann KM. 1983. The common aromatic biosynthetic pathway. In Amino Acids: Biosynthesis and Genetic Regulation, ed. KM Herrmann, RL Somerville, 17:301-22. London: Addison-Wesley. 453 pp.
    • (1983) Amino Acids: Biosynthesis and Genetic Regulation , vol.17 , pp. 301-322
    • Herrmann, K.M.1
  • 84
    • 0029104066 scopus 로고
    • The shikimate pathway as an entry to aromatic secondary metabolism
    • Herrmann KM. 1995. The shikimate pathway as an entry to aromatic secondary metabolism. Plant Physiol. 107:7-12
    • (1995) Plant Physiol. , vol.107 , pp. 7-12
    • Herrmann, K.M.1
  • 85
    • 0028857259 scopus 로고
    • The shikimate pathway: Early steps in the biosynthesis of aromatic compounds
    • Herrmann KM. 1995. The shikimate pathway: early steps in the biosynthesis of aromatic compounds. Plant Cell 7:907-19
    • (1995) Plant Cell , vol.7 , pp. 907-919
    • Herrmann, K.M.1
  • 86
    • 0025285187 scopus 로고
    • Induced expression of the Aspergillus nidulans QUTE gene introduced by transformation into Neurospora crassa
    • Hiett KL, Case ME. 1990. Induced expression of the Aspergillus nidulans QUTE gene introduced by transformation into Neurospora crassa. Mol. Gen. Genet. 222:201-5
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 201-205
    • Hiett, K.L.1    Case, M.E.2
  • 87
    • 0023901907 scopus 로고
    • Mechanisms of gene regulation in the general control of amino acid biosynthesis in Saccharomyces serevisiae
    • Hinnebusch AG. 1988. Mechanisms of gene regulation in the general control of amino acid biosynthesis in Saccharomyces serevisiae. Microbiol. Rev. 52:248-73
    • (1988) Microbiol. Rev. , vol.52 , pp. 248-273
    • Hinnebusch, A.G.1
  • 88
    • 0029833770 scopus 로고    scopus 로고
    • A phylogenetic analysis of Pisum based on morphological characters, allozyme and RAPD markers
    • Hoey BK, Crowe KR, Jones VM, Polans NO. 1996. A phylogenetic analysis of Pisum based on morphological characters, allozyme and RAPD markers. Theor. Appl. Genet. 92:92-100
    • (1996) Theor. Appl. Genet. , vol.92 , pp. 92-100
    • Hoey, B.K.1    Crowe, K.R.2    Jones, V.M.3    Polans, N.O.4
  • 89
    • 37049119730 scopus 로고
    • Pyruvic acid and D-glucose precursors in mytomycin biosynthesis by Streptomyces verticillatus
    • Hornemann R, Kehrer JP, Eggen JH. 1974. Pyruvic acid and D-glucose precursors in mytomycin biosynthesis by Streptomyces verticillatus. J. Chem. Soc. Chem. Commun. 1974:1045-46
    • (1974) J. Chem. Soc. Chem. Commun. , vol.1974 , pp. 1045-1046
    • Hornemann, R.1    Kehrer, J.P.2    Eggen, J.H.3
  • 90
    • 0030773958 scopus 로고    scopus 로고
    • Using isoenzyme polymorphisms for identifying and assessing genetic variation in cultivated pawpaw
    • Huang H, Layne DR, Peterson RN. 1997. Using isoenzyme polymorphisms for identifying and assessing genetic variation in cultivated pawpaw. J. Am. Soc. Hortic. Sci. 122:504-11
    • (1997) J. Am. Soc. Hortic. Sci. , vol.122 , pp. 504-511
    • Huang, H.1    Layne, D.R.2    Peterson, R.N.3
  • 92
    • 0030062566 scopus 로고    scopus 로고
    • Stability and expression of amplified EPSPS genes in glyphosate resistant tobacco cells and plantlets
    • Jones JD, Goldsbrough PB, Weller SC. 1996. Stability and expression of amplified EPSPS genes in glyphosate resistant tobacco cells and plantlets. Plant Cell Rep. 15:431-36
    • (1996) Plant Cell Rep. , vol.15 , pp. 431-436
    • Jones, J.D.1    Goldsbrough, P.B.2    Weller, S.C.3
  • 93
    • 0022796778 scopus 로고
    • Chloroplasts of higher plants synthesize L-phenylalanine via L-arogenate
    • Jung E, Zamir LO, Jensen RA. 1986. Chloroplasts of higher plants synthesize L-phenylalanine via L-arogenate. Proc. Natl. Acad. Sci. USA 83:7231-35
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7231-7235
    • Jung, E.1    Zamir, L.O.2    Jensen, R.A.3
  • 94
    • 0028005083 scopus 로고
    • Subcellular localization of quinate:Oxidoreductase from Phaseolus mungo L. sprouts
    • Kang X, Neuhaus HE, Scheibe R. 1994. Subcellular localization of quinate:oxidoreductase from Phaseolus mungo L. sprouts. Z. Naturforsch. Teil C 49:415-20
    • (1994) Z. Naturforsch. Teil C , vol.49 , pp. 415-420
    • Kang, X.1    Neuhaus, H.E.2    Scheibe, R.3
  • 95
    • 0025997703 scopus 로고
    • Differential induction of 3-deoxy-D-araèmo-heptulosonate 7-phosphate synthase genes in Arabidopsis thaliana by wounding and pathogenic attack
    • Keith B, Dong X, Ausube FM, Fink GR. 1991. Differential induction of 3-deoxy-D-araèmo-heptulosonate 7-phosphate synthase genes in Arabidopsis thaliana by wounding and pathogenic attack. Proc. Natl. Acad. Sci. USA 88:8821-25
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8821-8825
    • Keith, B.1    Dong, X.2    Ausube, F.M.3    Fink, G.R.4
  • 96
    • 0031001311 scopus 로고    scopus 로고
    • Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli
    • Kikuchi Y, Tsujimoto K, Kurahashi O. 1997. Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli. Appl. Environ. Microbiol. 63:761-62
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 761-762
    • Kikuchi, Y.1    Tsujimoto, K.2    Kurahashi, O.3
  • 97
    • 9444271749 scopus 로고    scopus 로고
    • Biosynthesis of 3-amino-5-hydroxybenzoic acid, the precursor of mC7N units in ansamycin antibiotics
    • Kim CG, Kirschning A, Bergon P, Zhou P, Su E, et al. 1996. Biosynthesis of 3-amino-5-hydroxybenzoic acid, the precursor of mC7N units in ansamycin antibiotics. J. Am. Chem. Soc. 118:7486-91
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7486-7491
    • Kim, C.G.1    Kirschning, A.2    Bergon, P.3    Zhou, P.4    Su, E.5
  • 98
    • 0032513247 scopus 로고    scopus 로고
    • 3-Amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics
    • Kim CG, Yu TW, Fryhle CB, Handa S, Floss HG. 1998. 3-Amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics. J. Biol. Chem. 273:6030-40
    • (1998) J. Biol. Chem. , vol.273 , pp. 6030-6040
    • Kim, C.G.1    Yu, T.W.2    Fryhle, C.B.3    Handa, S.4    Floss, H.G.5
  • 99
    • 0029917940 scopus 로고    scopus 로고
    • Analysis of fluoromethyl group chirality establishes a common stereochemical course of the enolpyruvyl transfers catalyzed by EPSP synthase and UDP-GIcNAc enolpyruvyl transferase
    • Kim DH, Tucker-Kellog GW, Lees WJ, Walsh CT. 1996. Analysis of fluoromethyl group chirality establishes a common stereochemical course of the enolpyruvyl transfers catalyzed by EPSP synthase and UDP-GIcNAc enolpyruvyl transferase. Biochemistry 35:5435-40
    • (1996) Biochemistry , vol.35 , pp. 5435-5440
    • Kim, D.H.1    Tucker-Kellog, G.W.2    Lees, W.J.3    Walsh, C.T.4
  • 100
    • 0023896661 scopus 로고
    • Amino acid biosynthesis inhibitors as herbicides
    • Kishore GM, Shah DM. 1988. Amino acid biosynthesis inhibitors as herbicides. Annu. Rev. Biochem. 57:627-63
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 627-663
    • Kishore, G.M.1    Shah, D.M.2
  • 101
    • 0025294082 scopus 로고
    • Active site labeling of the shikimate pathway enzyme dehydroquinase
    • Kleanthous C, Campbell DG, Coggins JR. 1990. Active site labeling of the shikimate pathway enzyme dehydroquinase. J. Biol. Chem. 265:10929-34
    • (1990) J. Biol. Chem. , vol.265 , pp. 10929-10934
    • Kleanthous, C.1    Campbell, D.G.2    Coggins, J.R.3
  • 102
    • 0026575985 scopus 로고
    • A comparison of the enzymological and biophysical properties of two distinct classes of dehydroquinase enzymes
    • Kleanthous C, Deka R, Davis K, Kelly SM, Cooper A, et al. 1992. A comparison of the enzymological and biophysical properties of two distinct classes of dehydroquinase enzymes. Biochem. J. 282:687-95
    • (1992) Biochem. J. , vol.282 , pp. 687-695
    • Kleanthous, C.1    Deka, R.2    Davis, K.3    Kelly, S.M.4    Cooper, A.5
  • 103
    • 0023484198 scopus 로고
    • Cloning of an Arabidopsis thaliana gene encoding 5-enolpyruvylshi-kimate 3-phosphate synthase: Sequence analysis and manipulation to obtain glyphosate tolerant plants
    • Klee HJ, Muskopf YM, Gasser CS. 1987. Cloning of an Arabidopsis thaliana gene encoding 5-enolpyruvylshi-kimate 3-phosphate synthase: sequence analysis and manipulation to obtain glyphosate tolerant plants. Mol. Gen. Genet. 210:437-42
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 437-442
    • Klee, H.J.1    Muskopf, Y.M.2    Gasser, C.S.3
  • 104
    • 0023811599 scopus 로고
    • trp represser interactions with the trp, aroH, and trpR operators
    • Klig LS, Carey J, Yanofsky C. 1988. trp represser interactions with the trp, aroH, and trpR operators. J. Mol. Biol. 202:769-77
    • (1988) J. Mol. Biol. , vol.202 , pp. 769-777
    • Klig, L.S.1    Carey, J.2    Yanofsky, C.3
  • 105
    • 0032557708 scopus 로고    scopus 로고
    • The three-dimensional structure of shikimate kinase
    • Krell T, Coggins JR, Lapthorn AJ. 1998. The three-dimensional structure of shikimate kinase. J. Mol. Biol. 278:983-97
    • (1998) J. Mol. Biol. , vol.278 , pp. 983-997
    • Krell, T.1    Coggins, J.R.2    Lapthorn, A.J.3
  • 107
    • 0028847967 scopus 로고
    • The use of electrospray mass spectrometry to identify an essential arginine residue in type II dehydroquinases
    • Krell T, Pitt AR, Coggins JR. 1995. The use of electrospray mass spectrometry to identify an essential arginine residue in type II dehydroquinases. FEBS Lett. 360:93-96
    • (1995) FEBS Lett. , vol.360 , pp. 93-96
    • Krell, T.1    Pitt, A.R.2    Coggins, J.R.3
  • 108
    • 0026514560 scopus 로고
    • Cloning, primary structure and regulation of the ARO4 gene, encoding the tyrosine-inhibited 3-deoxy-D-araemo-heptulosonate 7-phosphate synthase from Saccharomyces cerevisiae
    • Künzler M, Paravicini G, Egli CM, Irniger S, Braus GH. 1992. Cloning, primary structure and regulation of the ARO4 gene, encoding the tyrosine-inhibited 3-deoxy-D-araemo-heptulosonate 7-phosphate synthase from Saccharomyces cerevisiae. Gene 113:67-74
    • (1992) Gene , vol.113 , pp. 67-74
    • Künzler, M.1    Paravicini, G.2    Egli, C.M.3    Irniger, S.4    Braus, G.H.5
  • 109
    • 0028964283 scopus 로고
    • Activation and repression of the yeast ARO3 gene by global transcription factors
    • Künzler M, Springer C, Braus GH. 1995. Activation and repression of the yeast ARO3 gene by global transcription fac-tors. Mol. Microbiol. 15:167-78
    • (1995) Mol. Microbiol. , vol.15 , pp. 167-178
    • Künzler, M.1    Springer, C.2    Braus, G.H.3
  • 110
    • 0030799269 scopus 로고    scopus 로고
    • Linkage analysis of isoenzyme and dwarf loci, and detection of lethal genes in sugi
    • Kuramoto N, Tomaru N, Murai M, Ohba K. 1997. Linkage analysis of isoenzyme and dwarf loci, and detection of lethal genes in sugi. Breed. Sci. 47:259-66
    • (1997) Breed. Sci. , vol.47 , pp. 259-266
    • Kuramoto, N.1    Tomaru, N.2    Murai, M.3    Ohba, K.4
  • 111
    • 0025827981 scopus 로고
    • In vivo overproduction of the pentafunctional arom polypeptide in Aspergillus nidulans affects metabolic flux in the quinate pathway
    • Lamb HK, Bagshaw CR, Hawkins AR. 1991. In vivo overproduction of the pentafunctional arom polypeptide in Aspergillus nidulans affects metabolic flux in the quinate pathway. Mol. Gen. Genet. 227:187-96
    • (1991) Mol. Gen. Genet. , vol.227 , pp. 187-196
    • Lamb, H.K.1    Bagshaw, C.R.2    Hawkins, A.R.3
  • 112
    • 0030002461 scopus 로고    scopus 로고
    • The QUTA activator and QUTR repressor proteins of Aspergillus nidulans interact to regulate transcription of the quinate utilization pathway genes
    • Lamb HK, Newton GH, Levett LJ, Cairns E, Roberts CF, Hawkins AR. 1996. The QUTA activator and QUTR repressor proteins of Aspergillus nidulans interact to regulate transcription of the quinate utilization pathway genes. Microbiology 142:1477-90
    • (1996) Microbiology , vol.142 , pp. 1477-1490
    • Lamb, H.K.1    Newton, G.H.2    Levett, L.J.3    Cairns, E.4    Roberts, C.F.5    Hawkins, A.R.6
  • 114
    • 0027987492 scopus 로고
    • Regulation of aroL expression by tyrR protein and trp repressor in Escherichia coli K-12
    • Lawley B, Pittard AJ. 1994. Regulation of aroL expression by tyrR protein and trp repressor in Escherichia coli K-12. J. Bacteriol. 176:6921-30
    • (1994) J. Bacteriol. , vol.176 , pp. 6921-6930
    • Lawley, B.1    Pittard, A.J.2
  • 115
    • 0028845362 scopus 로고
    • Mutagenesis of active site residues in type I dehydroquinase from Escherichia coli
    • Leech AP, James R, Coggins JR, Kleanthous C. 1995. Mutagenesis of active site residues in type I dehydroquinase from Escherichia coli. J. Biol. Chem. 270: 25827-36
    • (1995) J. Biol. Chem. , vol.270 , pp. 25827-25836
    • Leech, A.P.1    James, R.2    Coggins, J.R.3    Kleanthous, C.4
  • 116
    • 0028813642 scopus 로고
    • The metabolism of quinate in pea roots: Purification and partial characterization of a quinate hydrolyase
    • Leuschner C, Herrmann KM, Schultz G. 1995. The metabolism of quinate in pea roots: purification and partial characterization of a quinate hydrolyase. Plant Physiol. 108:319-25
    • (1995) Plant Physiol. , vol.108 , pp. 319-325
    • Leuschner, C.1    Herrmann, K.M.2    Schultz, G.3
  • 117
    • 0030054297 scopus 로고    scopus 로고
    • Domain structure and function within the QUTA protein of Aspergillus nidulans: Implications for the control of transcription
    • Levesley I, Newton GH, Lamb HK, van Schothorst E, Dalgleish RWM, et al. 1996. Domain structure and function within the QUTA protein of Aspergillus nidulans: implications for the control of transcription. Microbiology 142:87-98
    • (1996) Microbiology , vol.142 , pp. 87-98
    • Levesley, I.1    Newton, G.H.2    Lamb, H.K.3    Van Schothorst, E.4    Dalgleish, R.W.M.5
  • 118
    • 0030065765 scopus 로고    scopus 로고
    • Binding of the oxidized, reduced, and radical flavin species to chorismate synthase. An investigation by spectroscopy, fluorimetry, and electron paramagnetic resonance and electron nuclear double resonance spectroscopy
    • Macheroux P, Petersen J, Bornemann S, Lowe DJ, Thomeley RNF. 1996. Binding of the oxidized, reduced, and radical flavin species to chorismate synthase. An investigation by spectroscopy, fluorimetry, and electron paramagnetic resonance and electron nuclear double resonance spectroscopy. Biochemistry 35:1643-52
    • (1996) Biochemistry , vol.35 , pp. 1643-1652
    • Macheroux, P.1    Petersen, J.2    Bornemann, S.3    Lowe, D.J.4    Thomeley, R.N.F.5
  • 119
    • 0027994499 scopus 로고
    • Increased disease susceptibility of transgenic tobacco plants with suppressed levels of preformed phenylpropanoid products
    • Maher EA, Bate NJ, Ni W, Elkind Y, Dixon RA, Lamb CJ. 1994. Increased disease susceptibility of transgenic tobacco plants with suppressed levels of preformed phenylpropanoid products. Proc. Natl. Acad. Sci. USA 91:7802-6
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7802-7806
    • Maher, E.A.1    Bate, N.J.2    Ni, W.3    Elkind, Y.4    Dixon, R.A.5    Lamb, C.J.6
  • 122
    • 0018088444 scopus 로고
    • Iron, an essential element for biosynthesis of aromatic compounds
    • McCandliss RJ, Herrmann KM. 1978. Iron, an essential element for biosynthesis of aromatic compounds. Proc. Natl. Acad. Sci. USA 75:4810-13
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4810-4813
    • McCandliss, R.J.1    Herrmann, K.M.2
  • 123
    • 0017864182 scopus 로고
    • 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli
    • McCandliss RJ, Poling MD, Herrmann KM. 1978. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli. J. Biol. Chem. 253:4259-65
    • (1978) J. Biol. Chem. , vol.253 , pp. 4259-4265
    • McCandliss, R.J.1    Poling, M.D.2    Herrmann, K.M.3
  • 124
    • 0024741670 scopus 로고
    • Induction of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase by fungal elicitor in cultures of Petroselinum crispum
    • McCue KF, Conn EE. 1989. Induction of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase by fungal elicitor in cultures of Petroselinum crispum. Proc. Natl. Acad. Sci. USA 86:7374-77
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7374-7377
    • McCue, K.F.1    Conn, E.E.2
  • 125
    • 0000191235 scopus 로고
    • Induction of shikimic acid pathway enzymes by light in suspension cultured cells of parsley (Petroselinum crispum)
    • McCue KF, Conn EE. 1990. Induction of shikimic acid pathway enzymes by light in suspension cultured cells of parsley (Petroselinum crispum). Plant Physiol. 94:507-10
    • (1990) Plant Physiol. , vol.94 , pp. 507-510
    • McCue, K.F.1    Conn, E.E.2
  • 126
    • 0029868793 scopus 로고    scopus 로고
    • Ligand geometry of the ternary complex of 5-enolpyruvyl shikimate 3-phosphate synthase from rotational-echo double-resonance NMR
    • McDowell LM, Klug CA, Beusen DD, Schaefer J. 1996. Ligand geometry of the ternary complex of 5-enolpyruvyl shikimate 3-phosphate synthase from rotational-echo double-resonance NMR. Biochemistry 35:5395-403
    • (1996) Biochemistry , vol.35 , pp. 5395-5403
    • McDowell, L.M.1    Klug, C.A.2    Beusen, D.D.3    Schaefer, J.4
  • 127
    • 0029864204 scopus 로고    scopus 로고
    • Structural constraints on the ternary complex of 5-enolpyruvyl shikimate 3-phosphate synthase from rotational-echo doubleresonance NMR
    • McDowell LM, Schmidt A, Cohen ER, Studelska DR, Schaefer J. 1996. Structural constraints on the ternary complex of 5-enolpyruvyl shikimate 3-phosphate synthase from rotational-echo doubleresonance NMR. J. Mol. Biol. 256:160-71.
    • (1996) J. Mol. Biol. , vol.256 , pp. 160-171
    • McDowell, L.M.1    Schmidt, A.2    Cohen, E.R.3    Studelska, D.R.4    Schaefer, J.5
  • 128
    • 0023042223 scopus 로고
    • The complete amino acid sequence of 3-dehydroquinate synthase of Escherichia coli K12
    • Millar G, Coggins JR. 1986. The complete amino acid sequence of 3-dehydroquinate synthase of Escherichia coli K12. FEBS Lett. 200:11-17
    • (1986) FEBS Lett. , vol.200 , pp. 11-17
    • Millar, G.1    Coggins, J.R.2
  • 129
    • 0027984358 scopus 로고
    • EPSP synthase inhibitor design IV. New aromatic substrate analogs and symmetrical inhibitors containing novel 3-phosphate mimics
    • Miller MJ, Braccolino DS, Cleary DG, Ream JE, Walker MC, Sikorski JA. 1994. EPSP synthase inhibitor design IV. New aromatic substrate analogs and symmetrical inhibitors containing novel 3-phosphate mimics. Bioorg. Med. Chem. Lett. 21:2605-8
    • (1994) Bioorg. Med. Chem. Lett. , vol.21 , pp. 2605-2608
    • Miller, M.J.1    Braccolino, D.S.2    Cleary, D.G.3    Ream, J.E.4    Walker, M.C.5    Sikorski, J.A.6
  • 130
    • 0029563920 scopus 로고
    • New EPSP synthase inhibitors: Synthesis and evaluation of an aromatic tetrahedral intermediate mimic containing a 3-malonate ether as a 3-phosphate surrogate
    • Miller MJ, Cleary DG, Ream JE, Snyder KR, Sikorski JA. 1995. New EPSP synthase inhibitors: synthesis and evaluation of an aromatic tetrahedral intermediate mimic containing a 3-malonate ether as a 3-phosphate surrogate. Bioorg. Med. Chem. 3:1685-92
    • (1995) Bioorg. Med. Chem. , vol.3 , pp. 1685-1692
    • Miller, M.J.1    Cleary, D.G.2    Ream, J.E.3    Snyder, K.R.4    Sikorski, J.A.5
  • 131
    • 0030959729 scopus 로고    scopus 로고
    • Cyclohexenyl and cyclohexylidene inhibitors of 3-dehydroquinate synthase: Active site interactions relevant to enzyme mechanism and inhibitor design
    • Montchamp JL, Frost JW. 1997. Cyclohexenyl and cyclohexylidene inhibitors of 3-dehydroquinate synthase: active site interactions relevant to enzyme mechanism and inhibitor design. J. Am. Chem. Soc. 119:7645-53
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 7645-7653
    • Montchamp, J.L.1    Frost, J.W.2
  • 132
    • 0028073651 scopus 로고
    • Inversion of an asymmetric center in carbocyclic inhibitors of 3-dehydroquinate synthase: Examining and exploiting the mechanism for synelimination during substrate turnover
    • Montchamp JL, Peng JR, Frost JW 1994. Inversion of an asymmetric center in carbocyclic inhibitors of 3-dehydroquinate synthase: examining and exploiting the mechanism for synelimination during substrate turnover. J. Org. Chem. 59:6999-7007
    • (1994) J. Org. Chem. , vol.59 , pp. 6999-7007
    • Montchamp, J.L.1    Peng, J.R.2    Frost, J.W.3
  • 133
  • 134
    • 0026792847 scopus 로고
    • Inducible over-production of the Aspergillus nidulans pentafunctional AROM protein and the type-I and -II 3-dedydroquinases from Salmonella typhi and Mycobacterium tuberculosis
    • Moore JD, Lamb HK, Garbe T, Servos S, Dougan G, et al. 1992. Inducible over-production of the Aspergillus nidulans pentafunctional AROM protein and the type-I and -II 3-dedydroquinases from Salmonella typhi and Mycobacterium tuberculosis. Biochem. J. 287:173-81
    • (1992) Biochem. J. , vol.287 , pp. 173-181
    • Moore, J.D.1    Lamb, H.K.2    Garbe, T.3    Servos, S.4    Dougan, G.5
  • 135
    • 0000902112 scopus 로고
    • Purification and characterzation of bifunctional dehydroquinaseshikimate:NADP oxidoreductase from pea seedlings
    • Mousdale DM, Campbell MS, Coggins j JR. 1987. Purification and characterzation of bifunctional dehydroquinaseshikimate:NADP oxidoreductase from pea seedlings. Phytochemistry 26:2665-70
    • (1987) Phytochemistry , vol.26 , pp. 2665-2670
    • Mousdale, D.M.1    Campbell, M.S.2    Coggins, J.R.3
  • 136
    • 0001069728 scopus 로고
    • Wounding induces one of two isoenzymes of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Solatium tuberosum L
    • Muday GK, Herrmann KM. 1992. Wounding induces one of two isoenzymes of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Solatium tuberosum L. Plant Physiol. 98:496-500
    • (1992) Plant Physiol. , vol.98 , pp. 496-500
    • Muday, G.K.1    Herrmann, K.M.2
  • 137
    • 0025835584 scopus 로고
    • The tyrosine repressor negatively regulates aroH expression in Escherichia coli
    • Muday GK, Johnson DI, Somerville RL, Herrmann KM. 1991. The tyrosine repressor negatively regulates aroH expression in Escherichia coli. J. Bacteriol. 173:3930-32
    • (1991) J. Bacteriol. , vol.173 , pp. 3930-3932
    • Muday, G.K.1    Johnson, D.I.2    Somerville, R.L.3    Herrmann, K.M.4
  • 138
    • 0031934574 scopus 로고    scopus 로고
    • Stability and culture medium limitations of gene amplification in glyphosate resistant carrot cell lines
    • Murata M, Ryu JH, Caretto S, Rao D, Song HS, Widholm JM. 1998. Stability and culture medium limitations of gene amplification in glyphosate resistant carrot cell lines. J. Plant Physiol. 152:112-17
    • (1998) J. Plant Physiol. , vol.152 , pp. 112-117
    • Murata, M.1    Ryu, J.H.2    Caretto, S.3    Rao, D.4    Song, H.S.5    Widholm, J.M.6
  • 141
    • 0023853960 scopus 로고
    • Characterization of aromatic- and purine-dependent Salmonella typhimurium: Attenuation, persistence, and ability to induce protective immunity in BALB/c mice
    • O'Callaghan D, Maskell D, LiewFY, Easmon CS, Dougan G. 1988. Characterization of aromatic- and purine-dependent Salmonella typhimurium: attenuation, persistence, and ability to induce protective immunity in BALB/c mice. Infect. Immun. 56:419-23
    • (1988) Infect. Immun. , vol.56 , pp. 419-423
    • O'Callaghan, D.1    Maskell, D.2    Liew, F.Y.3    Easmon, C.S.4    Dougan, G.5
  • 143
    • 0028843278 scopus 로고
    • Development, identification, and characterization of a glyphosate-tolerant soybean line
    • Padgette SR, Kolacz KH, Delannay X, Re DB, LaVallee BJ. 1995. Development, identification, and characterization of a glyphosate-tolerant soybean line. Crop Sci. 35:1451-61
    • (1995) Crop Sci. , vol.35 , pp. 1451-1461
    • Padgette, S.R.1    Kolacz, K.H.2    Delannay, X.3    Re, D.B.4    LaVallee, B.J.5
  • 144
    • 0025837325 scopus 로고
    • Sitedirected mutagenesis of a conserved region of the 5-enolpyruvylshikimate 3-phosphate synthase active site
    • Padgette SR, Re DB, Gasser CS, Eichholtz DA, Frazier RB, et al. 1991. Sitedirected mutagenesis of a conserved region of the 5-enolpyruvylshikimate 3-phosphate synthase active site. J. Biol. Chem. 266:22364-69
    • (1991) J. Biol. Chem. , vol.266 , pp. 22364-22369
    • Padgette, S.R.1    Re, D.B.2    Gasser, C.S.3    Eichholtz, D.A.4    Frazier, R.B.5
  • 145
    • 0030659720 scopus 로고    scopus 로고
    • Detection and identification of transient enzyme intermediates using rapid mixing, pulsedflow electrospray mass spectrometry
    • Paiva AA, Tilton RF, Crooks GP, Huang LQ, Anderson KS. 1997. Detection and identification of transient enzyme intermediates using rapid mixing, pulsedflow electrospray mass spectrometry. Biochemistry 36:15472-76
    • (1997) Biochemistry , vol.36 , pp. 15472-15476
    • Paiva, A.A.1    Tilton, R.F.2    Crooks, G.P.3    Huang, L.Q.4    Anderson, K.S.5
  • 146
    • 0024203872 scopus 로고
    • Structure of the ARO3 gene of Saccharomyces cerevisiae
    • Paravicini G, Braus G, Hütter R. 1988. Structure of the ARO3 gene of Saccharomyces cerevisiae. Mol. Gen. Genet. 214:165-69
    • (1988) Mol. Gen. Genet. , vol.214 , pp. 165-169
    • Paravicini, G.1    Braus, G.2    Hütter, R.3
  • 147
    • 0024486889 scopus 로고
    • The general control activator protein GCN4 is essential for a basal level of ARO3 gene expression in Saccharomyces cerevisiae
    • Paravicini G, Mösch HU, Schmidheini T, Braus G. 1989. The general control activator protein GCN4 is essential for a basal level of ARO3 gene expression in Saccharomyces cerevisiae. Mol Cell. Biol. 9:144-51
    • (1989) Mol Cell. Biol. , vol.9 , pp. 144-151
    • Paravicini, G.1    Mösch, H.U.2    Schmidheini, T.3    Braus, G.4
  • 148
    • 0024839980 scopus 로고
    • Purification and properties of the 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (phenylalanine-inhibitable) of Saccharomyces cerevisiae
    • Paravicini G, Schmidheini T, Braus G. 1989. Purification and properties of the 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (phenylalanine-inhibitable) of Saccharomyces cerevisiae. Eur. J. Biochem. 186:361-66
    • (1989) Eur. J. Biochem. , vol.186 , pp. 361-366
    • Paravicini, G.1    Schmidheini, T.2    Braus, G.3
  • 149
    • 0000239859 scopus 로고    scopus 로고
    • Derailing dehydroquinate synthase by introducing a stabilizing stereoelectronic effect in a reaction intermediate
    • Parker EJ, Coggins JR, Abell C. 1997. Derailing dehydroquinate synthase by introducing a stabilizing stereoelectronic effect in a reaction intermediate. J. Org. Chem. 62:8582-85
    • (1997) J. Org. Chem. , vol.62 , pp. 8582-8585
    • Parker, E.J.1    Coggins, J.R.2    Abell, C.3
  • 150
    • 0030117457 scopus 로고    scopus 로고
    • Aromatic amino-acid biosynthesis in Candida albicans: Identification of the ARO4 gene encoding a second DAHP synthase
    • Pereira SA, Livi GP. 1996. Aromatic amino-acid biosynthesis in Candida albicans: identification of the ARO4 gene encoding a second DAHP synthase. Curr. Genet. 29:441-45
    • (1996) Curr. Genet. , vol.29 , pp. 441-445
    • Pereira, S.A.1    Livi, G.P.2
  • 151
    • 0028834892 scopus 로고
    • Molecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium Pseudomonas aureofaciens 30-84
    • Pierson LS III, Gaffney T, Lam S, Gong FC. 1995. Molecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium Pseudomonas aureofaciens 30-84. FEMS Microbiol. Lett. 134:299-307
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 299-307
    • Pierson L.S. III1    Gaffney, T.2    Lam, S.3    Gong, F.C.4
  • 152
    • 0007504414 scopus 로고
    • Glyphosate induces 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in potato (Solarium tuberosum L.) cells grown in suspension culture
    • Pinto JEBP, Dyer WE, Weller SC, Herrmann KM. 1988. Glyphosate induces 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in potato (Solarium tuberosum L.) cells grown in suspension culture. Plant Physiol. 87:891-93
    • (1988) Plant Physiol. , vol.87 , pp. 891-893
    • Pinto, J.E.B.P.1    Dyer, W.E.2    Weller, S.C.3    Herrmann, K.M.4
  • 153
    • 0005627658 scopus 로고
    • 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from potato tuber (Solanum tuberosum L.)
    • Pinto JEBP, Suzich JA, Herrmann KM. 1986. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from potato tuber (Solanum tuberosum L.). Plant Physiol. 82:1040-44
    • (1986) Plant Physiol. , vol.82 , pp. 1040-1044
    • Pinto, J.E.B.P.1    Suzich, J.A.2    Herrmann, K.M.3
  • 154
    • 0039803503 scopus 로고
    • Probing lethal metabolic perturbations in plants with chemical inhibition of dehydroquinate synthase
    • Pompliano DL, Reimer LM, Myrvold S, Frost JW. 1989. Probing lethal metabolic perturbations in plants with chemical inhibition of dehydroquinate synthase. J. Am. Chem. Soc. 111:1866-71
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 1866-1871
    • Pompliano, D.L.1    Reimer, L.M.2    Myrvold, S.3    Frost, J.W.4
  • 155
    • 0001178304 scopus 로고
    • Reaction of (6R)-6-F-EPSP with recombinant Escherichia coli chorismate synthase generates a stable flavin mononucleotide semiquinone radical
    • Ramjee MN, Balasubramanian S, Abell C, Coggins JR, Davies GM, et al. 1992. Reaction of (6R)-6-F-EPSP with recombinant Escherichia coli chorismate synthase generates a stable flavin mononucleotide semiquinone radical. J. Am. Chem. Soc. 114:3151-53
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3151-3153
    • Ramjee, M.N.1    Balasubramanian, S.2    Abell, C.3    Coggins, J.R.4    Davies, G.M.5
  • 156
    • 0000244683 scopus 로고
    • Spectrophotometric detection of a modified flavin mononucleotide (FMN) intermediate formed during the catalytic cycle of chorismate synthase
    • Ramjee MN, Coggins JR, Hawkes TR, Lowe DJ, Thorneley RNF. 1991. Spectrophotometric detection of a modified flavin mononucleotide (FMN) intermediate formed during the catalytic cycle of chorismate synthase. J. Am. Chem. Soc. 113:8566-67
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 8566-8567
    • Ramjee, M.N.1    Coggins, J.R.2    Hawkes, T.R.3    Lowe, D.J.4    Thorneley, R.N.F.5
  • 157
  • 158
    • 0026065718 scopus 로고
    • Purification and properties of tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli
    • Ray JM, Bauerle R. 1991. Purification and properties of tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli. J. Bacteriol. 173:1894-901
    • (1991) J. Bacteriol. , vol.173 , pp. 1894-1901
    • Ray, J.M.1    Bauerle, R.2
  • 159
    • 0024255488 scopus 로고
    • Mutational analysis of the catalytic and feedback sites of the tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli
    • Ray JM, Yanofsky C, Bauerle R. 1988. Mutational analysis of the catalytic and feedback sites of the tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli. J. Bacteriol. 170:5500-6
    • (1988) J. Bacteriol. , vol.170 , pp. 5500-5506
    • Ray, J.M.1    Yanofsky, C.2    Bauerle, R.3
  • 160
    • 0028155588 scopus 로고
    • Pico-tag analysis of arogenic acid and related free amino acids from plant and fungal extracts
    • Razal RA, Lewis NG, Towers GHN. 1994. Pico-tag analysis of arogenic acid and related free amino acids from plant and fungal extracts. Phytochem. Anal. 5:98-104
    • (1994) Phytochem. Anal. , vol.5 , pp. 98-104
    • Razal, R.A.1    Lewis, N.G.2    Towers, G.H.N.3
  • 161
    • 0032565968 scopus 로고    scopus 로고
    • Evidence for the shikimate pathway in apicomplexan parasites
    • Roberts F, Roberts CW, Johnson JJ, Kyle DE, Krell T, et al. 1998. Evidence for the shikimate pathway in apicomplexan parasites. Nature 393:801-5
    • (1998) Nature , vol.393 , pp. 801-805
    • Roberts, F.1    Roberts, C.W.2    Johnson, J.J.3    Kyle, D.E.4    Krell, T.5
  • 162
    • 0030729349 scopus 로고    scopus 로고
    • A second type-I PKS gene cluster isolated from Streptomyces hygroscopicus ATCC 29253, a rifamycin-producing strain
    • Ruan XA, Stassi D, Lax SA, Katz L. 1997. A second type-I PKS gene cluster isolated from Streptomyces hygroscopicus ATCC 29253, a rifamycin-producing strain. Gene 203:1-9
    • (1997) Gene , vol.203 , pp. 1-9
    • Ruan, X.A.1    Stassi, D.2    Lax, S.A.3    Katz, L.4
  • 163
    • 0001117919 scopus 로고
    • Differentially regulated isozymes of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from seedlings of Vigna radiata [L.] Wilczek
    • Rubin JL, Jensen RA. 1985. Differentially regulated isozymes of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from seedlings of Vigna radiata [L.] Wilczek. Plant Physiol. 79:711-18
    • (1985) Plant Physiol. , vol.79 , pp. 711-718
    • Rubin, J.L.1    Jensen, R.A.2
  • 164
    • 0039803504 scopus 로고    scopus 로고
    • Genetic diversity and phylogenetic relationships in cotton based on isoenzyme markers
    • Saha S, Zipf A. 1998. Genetic diversity and phylogenetic relationships in cotton based on isoenzyme markers. J. Crop. Prod. 1:79-93
    • (1998) J. Crop. Prod. , vol.1 , pp. 79-93
    • Saha, S.1    Zipf, A.2
  • 165
    • 0029053555 scopus 로고
    • Reevaluating glyphosate as a transition state inhibitor of EPSP synthase: Identification of an EPSP synthase-EPSP-glyphosate ternary complex
    • Sammons RD, Gruys KJ, Anderson KS, Johnson KA, Sikorski JA. 1995. Reevaluating glyphosate as a transition state inhibitor of EPSP synthase: identification of an EPSP synthase-EPSP-glyphosate ternary complex. Biochemistry 34:6433-40
    • (1995) Biochemistry , vol.34 , pp. 6433-6440
    • Sammons, R.D.1    Gruys, K.J.2    Anderson, K.S.3    Johnson, K.A.4    Sikorski, J.A.5
  • 166
    • 0025885540 scopus 로고
    • Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers
    • Schaller A, Schmid J, Leibinger U, Amrhein N. 1991. Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers. J. Biol. Chem. 266:21434-38
    • (1991) J. Biol. Chem. , vol.266 , pp. 21434-21438
    • Schaller, A.1    Schmid, J.2    Leibinger, U.3    Amrhein, N.4
  • 167
    • 0025083312 scopus 로고
    • Purification of chorismate synthase from a cell culture of the higher plant Corydalis sempervirens Pers
    • Schaller A, Windhofer V, Amrhein N. 1990. Purification of chorismate synthase from a cell culture of the higher plant Corydalis sempervirens Pers. Arch. Biochem. Biophys. 282:437-42
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 437-442
    • Schaller, A.1    Windhofer, V.2    Amrhein, N.3
  • 168
    • 0028813444 scopus 로고
    • Molecular organization of the shikimate pathway in higher plants
    • Schmid J, Amrhein N. 1995. Molecular organization of the shikimate pathway in higher plants. Phytochemistry 39:737-49
    • (1995) Phytochemistry , vol.39 , pp. 737-749
    • Schmid, J.1    Amrhein, N.2
  • 169
    • 0026864722 scopus 로고
    • The in vitro synthesized tomato shikimate kinase precursor is enzymatically active and is imported and processed to the mature enzyme by chloroplasts
    • Schmid J, Schaller A, Leibinger U, Boll W, Amrhein N. 1992. The in vitro synthesized tomato shikimate kinase precursor is enzymatically active and is imported and processed to the mature enzyme by chloroplasts. Plant J. 2:375-83
    • (1992) Plant J. , vol.2 , pp. 375-383
    • Schmid, J.1    Schaller, A.2    Leibinger, U.3    Boll, W.4    Amrhein, N.5
  • 170
    • 0007146139 scopus 로고
    • Shikimate kinase from spinach chloroplasts. Purification, characterization, and regulatory function in aromatic amino acid biosynthesis
    • Schmidt CL, Danneel HJ, Schultz G, Buchanan BB. 1990. Shikimate kinase from spinach chloroplasts. Purification, characterization, and regulatory function in aromatic amino acid biosynthesis. Plant Physiol. 93:758-66
    • (1990) Plant Physiol. , vol.93 , pp. 758-766
    • Schmidt, C.L.1    Danneel, H.J.2    Schultz, G.3    Buchanan, B.B.4
  • 171
    • 85007587770 scopus 로고
    • Shikimate pathway in non-photosynthetic tissues. Identification of common enzymes and partial purification of dehydroquinate hydrolyase-shikimate oxidoreductase and chorismate mutase from roots
    • Schmidt CL, Gründemann D, Groth G, Müller B, Hennig H, Schultz G. 1991. Shikimate pathway in non-photosynthetic tissues. Identification of
    • (1991) J. Plant Physiol. , vol.138 , pp. 51-56
    • Schmidt, C.L.1    Gründemann, D.2    Groth, G.3    Müller, B.4    Hennig, H.5    Schultz, G.6
  • 172
    • 0031840694 scopus 로고    scopus 로고
    • The two 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase isoenzymes from Saccharomyces cerevisiae show different kinetic modes of inhibition
    • Schnappauf G, Hartmann M, Künzler M, Braus GH. 1998. The two 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase isoenzymes from Saccharomyces cerevisiae show different kinetic modes of inhibition. Arch. Microbiol. 169:517-24
    • (1998) Arch. Microbiol. , vol.169 , pp. 517-524
    • Schnappauf, G.1    Hartmann, M.2    Künzler, M.3    Braus, G.H.4
  • 173
    • 0017114285 scopus 로고
    • 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli
    • Schoner R, Herrmann KM. 1976. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli. J. Biol. Chem. 251:5440-47
    • (1976) J. Biol. Chem. , vol.251 , pp. 5440-5447
    • Schoner, R.1    Herrmann, K.M.2
  • 174
    • 0040395928 scopus 로고
    • Z-9-Fluoro-EPSP is not a substrate for EPSP synthase: Implications for the enzyme mechanism
    • Seto CT, Bartlett PA. 1994. (Z)-9-Fluoro-EPSP is not a substrate for EPSP synthase: implications for the enzyme mechanism. J. Org. Chem. 59:7130-32
    • (1994) J. Org. Chem. , vol.59 , pp. 7130-7132
    • Seto, C.T.1    Bartlett, P.A.2
  • 175
    • 0031081517 scopus 로고    scopus 로고
    • New aromatic inhibitors of EPSP synthase incorporating hydroxymalonates as novel 3-phosphate replacements
    • Shah A, Font JL, Miller MJ, Ream JE, Walker MC, Sikorski JA. 1997. New aromatic inhibitors of EPSP synthase incorporating hydroxymalonates as novel 3-phosphate replacements. Bioorg. Med. Chem. 5:323-34
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 323-334
    • Shah, A.1    Font, J.L.2    Miller, M.J.3    Ream, J.E.4    Walker, M.C.5    Sikorski, J.A.6
  • 177
    • 0027237831 scopus 로고
    • Evidence for opposite stereochemical courses for the reactions catalyzed by type I and type II dehydroquinases
    • Shneier A, Harris J, Kleanthous C, Coggins JR, Hawkins AR, Abell C. 1993. Evidence for opposite stereochemical courses for the reactions catalyzed by type I and type II dehydroquinases. Bioorg. Med. Chem. Lett. 3:1399-402
    • (1993) Bioorg. Med. Chem. Lett. , vol.3 , pp. 1399-1402
    • Shneier, A.1    Harris, J.2    Kleanthous, C.3    Coggins, J.R.4    Hawkins, A.R.5    Abell, C.6
  • 178
    • 85005455220 scopus 로고
    • Observation of an imine intermediate on dehydroquinase by electrospray mass spectrometry
    • Shneier A, Kleanthous C, Deka R, Coggins JR, Abell C. 1991. Observation of an imine intermediate on dehydroquinase by electrospray mass spectrometry. J. Am. Chem.Soc. 113:9416-18
    • (1991) J. Am. Chem.soc. , vol.113 , pp. 9416-9418
    • Shneier, A.1    Kleanthous, C.2    Deka, R.3    Coggins, J.R.4    Abell, C.5
  • 179
    • 0029926388 scopus 로고    scopus 로고
    • Purification, crystallization, and preliminary crystallographic analysis of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli
    • Shumilin IA, Kretsinger RH, Bauerle R. 1996. Purification, crystallization, and preliminary crystallographic analysis of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli. Proteins 24:404-6
    • (1996) Proteins , vol.24 , pp. 404-406
    • Shumilin, I.A.1    Kretsinger, R.H.2    Bauerle, R.3
  • 180
    • 0028361223 scopus 로고
    • Site directed mutagenesis and NMR studies of histidine385 mutants of 5-enolpyruvylshikimate 3-phosphate synthase
    • Shuttleworth WA, Evans JN. 1994. Site directed mutagenesis and NMR studies of histidine385 mutants of 5-enolpyruvylshikimate 3-phosphate synthase. Biochemistry 33:7062-68
    • (1994) Biochemistry , vol.33 , pp. 7062-7068
    • Shuttleworth, W.A.1    Evans, J.N.2
  • 181
    • 0030271176 scopus 로고    scopus 로고
    • The H385N mutant of 5-enolpyruvylshikimate 3-phosphate synthase: Kinetics, fluorescence, and nuclear magnetic resonance studies
    • Shuttleworth WA, Evans JN. 1996. The H385N mutant of 5-enolpyruvylshikimate 3-phosphate synthase: kinetics, fluorescence, and nuclear magnetic resonance studies. Arch. Biochem. Biophys. 334:37-42
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 37-42
    • Shuttleworth, W.A.1    Evans, J.N.2
  • 182
    • 0008739457 scopus 로고
    • Characterization of the glyphosate selection of carrot suspension cultures resulting in gene amplification
    • Shyr YJ, Caretto S, Widholm JM. 1993. Characterization of the glyphosate selection of carrot suspension cultures resulting in gene amplification. Plant Sci. 88:219-28
    • (1993) Plant Sci. , vol.88 , pp. 219-228
    • Shyr, Y.J.1    Caretto, S.2    Widholm, J.M.3
  • 183
    • 0001853354 scopus 로고    scopus 로고
    • Understanding glyphosate's molecular mode of action with EPSP synthase: Evidence favoring an allosteric inhibitor model
    • Sikorski JA, Gruys KJ. 1997. Understanding glyphosate's molecular mode of action with EPSP synthase: evidence favoring an allosteric inhibitor model. Acc. Chem. Res. 30:2-8
    • (1997) Acc. Chem. Res. , vol.30 , pp. 2-8
    • Sikorski, J.A.1    Gruys, K.J.2
  • 186
    • 0022393780 scopus 로고
    • Selective overproduction of 5-enolpyruvylshikimate 3-phosphate synthase in a plant cell culture which tolerates high doses of the herbicide glyphosate
    • Smart CC, Johänning D, Müller G, Amrhein N. 1985. Selective overproduction of 5-enolpyruvylshikimate 3-phosphate synthase in a plant cell culture which tolerates high doses of the herbicide glyphosate. J. Biol Chem. 260:16338-46
    • (1985) J. Biol Chem. , vol.260 , pp. 16338-16346
    • Smart, C.C.1    Johänning, D.2    Müller, G.3    Amrhein, N.4
  • 187
    • 0001745087 scopus 로고
    • Increased 5-enolpyruvylshikimic acid 3-phosphate synthase activity in a glyphosate-tolerant variant strain of tomato cells
    • Smith CM, Pratt D, Thompson GA. 1986. Increased 5-enolpyruvylshikimic acid 3-phosphate synthase activity in a glyphosate-tolerant variant strain of tomato cells. Plant Cell Rep. 5:298-301
    • (1986) Plant Cell Rep. , vol.5 , pp. 298-301
    • Smith, C.M.1    Pratt, D.2    Thompson, G.A.3
  • 188
    • 0021827241 scopus 로고
    • A single amino acid substitution in the enzyme 5-enolpyruvylshikimate 3-phosphate synthase confers resistance to the herbicide glyphosate
    • Stalker DM, Hiatt WR, Comai L. 1985. A single amino acid substitution in the enzyme 5-enolpyruvylshikimate 3-phosphate synthase confers resistance to the herbicide glyphosate. J. Biol. Chem. 260:4724-28
    • (1985) J. Biol. Chem. , vol.260 , pp. 4724-4728
    • Stalker, D.M.1    Hiatt, W.R.2    Comai, L.3
  • 189
    • 0025754179 scopus 로고
    • Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate 3-phosphate synthase: A distinctive protein fold
    • Stallings WC, Abdel-Meguid SS, Lim LW, Shieh HS, Dayringer HE. et al. 1991. Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate 3-phosphate synthase: a distinctive protein fold. Proc. Natl. Acad. Sci. USA 88:5046-50
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5046-5050
    • Stallings, W.C.1    Abdel-Meguid, S.S.2    Lim, L.W.3    Shieh, H.S.4    Dayringer, H.E.5
  • 190
    • 0018932939 scopus 로고
    • The herbicide glyphosate is a potent inhibitor of 5-enolpyruvylshikimic acid 3-phosphate synthase
    • Steinrücken HC, Amrhein N. 1980. The herbicide glyphosate is a potent inhibitor of 5-enolpyruvylshikimic acid 3-phosphate synthase. Biochem. Biophys. Res. Commun. 94:1207-12
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 1207-1212
    • Steinrücken, H.C.1    Amrhein, N.2
  • 191
    • 0025720117 scopus 로고
    • Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli
    • Stephens CM, Bauerle R. 1991. Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli. J. Biol. Chem. 266:20810-17
    • (1991) J. Biol. Chem. , vol.266 , pp. 20810-20817
    • Stephens, C.M.1    Bauerle, R.2
  • 192
    • 0026640807 scopus 로고
    • Essential cysteines in 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli
    • Stephens CM, Bauerle R. 1992. Essential cysteines in 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli. J. Biol. Chem. 267:5762-67
    • (1992) J. Biol. Chem. , vol.267 , pp. 5762-5767
    • Stephens, C.M.1    Bauerle, R.2
  • 193
    • 0027915546 scopus 로고
    • Purification and characterization of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Streptomyces rimosus
    • Stuart F, Hunter IS. 1993. Purification and characterization of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Streptomyces rimosus. Biochim. Biophys. Acta 1161:209-15
    • (1993) Biochim. Biophys. Acta , vol.1161 , pp. 209-215
    • Stuart, F.1    Hunter, I.S.2
  • 194
    • 0030014748 scopus 로고    scopus 로고
    • Longrange distance measurements of protein binding sites by rotational-echo double-resonance NMR
    • Studelska DR, Klug CA, Beusen DD, McDowell LM, Schaefer J. 1996. Longrange distance measurements of protein binding sites by rotational-echo double-resonance NMR. J. Am. Chem. Soc. 118: 5476-77
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5476-5477
    • Studelska, D.R.1    Klug, C.A.2    Beusen, D.D.3    McDowell, L.M.4    Schaefer, J.5
  • 195
    • 0031439457 scopus 로고    scopus 로고
    • Slowed enzymatic turnover allows characterization of intermediates by solid-state NMR
    • Studelska DR, McDowell LM, Espe MP, Klug CA, Schaefer J. 1997. Slowed enzymatic turnover allows characterization of intermediates by solid-state NMR. Biochemistry 36:15555-60
    • (1997) Biochemistry , vol.36 , pp. 15555-15560
    • Studelska, D.R.1    McDowell, L.M.2    Espe, M.P.3    Klug, C.A.4    Schaefer, J.5
  • 196
    • 0031963257 scopus 로고    scopus 로고
    • Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae in the context of its membership in a protein family containing a subset of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases
    • Subramaniam PS, Xie G, Xia T, Jensen RA. 1998. Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae in the context of its membership in a protein family containing a subset of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases. J. Bacteriol. 180:119-27
    • (1998) J. Bacteriol. , vol.180 , pp. 119-127
    • Subramaniam, P.S.1    Xie, G.2    Xia, T.3    Jensen, R.A.4
  • 197
    • 0027600516 scopus 로고
    • Structure of amplified 5-enolpyruvylshikimate 3-phosphate synthase gene in glyphosate-resistant carrot cells
    • Sub H, Hepburn AG, Kriz AL, Widholm JM. 1993. Structure of amplified 5-enolpyruvylshikimate 3-phosphate synthase gene in glyphosate-resistant carrot cells. Plant Mol. Biol. 22:195-205
    • (1993) Plant Mol. Biol. , vol.22 , pp. 195-205
    • Sub, H.1    Hepburn, A.G.2    Kriz, A.L.3    Widholm, J.M.4
  • 198
    • 0001218840 scopus 로고
    • 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from carrot root (Daucus carota) is a hysteretic enzyme
    • Suzich JA, Dean JFD, Hermann KM. 1985. 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from carrot root (Daucus carota) is a hysteretic enzyme. Plant Physiol. 79:765-70
    • (1985) Plant Physiol. , vol.79 , pp. 765-770
    • Suzich, J.A.1    Dean, J.F.D.2    Hermann, K.M.3
  • 199
    • 0029139330 scopus 로고
    • Studies on elicitor-signal transduction leading to differential expression of defense genes in cultured tobacco cells
    • Suzuki K, Fukuda Y, Shinshi H. 1995. Studies on elicitor-signal transduction leading to differential expression of defense genes in cultured tobacco cells. Plant Cell Physiol. 36:281-89
    • (1995) Plant Cell Physiol. , vol.36 , pp. 281-289
    • Suzuki, K.1    Fukuda, Y.2    Shinshi, H.3
  • 200
    • 0029760686 scopus 로고    scopus 로고
    • Purification and characterization of a cytosolic isoenzyme of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from cultured carrot cells
    • Suzuki N, Sakuta M, Shimizu S. 1996. Purification and characterization of a cytosolic isoenzyme of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from cultured carrot cells. J. Plant Physiol. 149:19-22
    • (1996) J. Plant Physiol. , vol.149 , pp. 19-22
    • Suzuki, N.1    Sakuta, M.2    Shimizu, S.3
  • 201
    • 0028854429 scopus 로고
    • Changes in the activity of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase in suspension-cultured cells of Vitis
    • Suzuki N, Sakuta M, Shimizu S, Komamine A. 1995. Changes in the activity of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase in suspension-cultured cells of Vitis. Physiol. Plant. 94:591-96
    • (1995) Physiol. Plant. , vol.94 , pp. 591-596
    • Suzuki, N.1    Sakuta, M.2    Shimizu, S.3    Komamine, A.4
  • 202
    • 0026500055 scopus 로고
    • Characterization of a zinc finger DNA-binding protein expressed specifically in Petunia petals and seedlings
    • Takatsuji H, Mori M, Benfey PN, Ren L, Chua NH. 1992. Characterization of a zinc finger DNA-binding protein expressed specifically in Petunia petals and seedlings. EMBO J. 11:241-49
    • (1992) EMBO J. , vol.11 , pp. 241-249
    • Takatsuji, H.1    Mori, M.2    Benfey, P.N.3    Ren, L.4    Chua, N.H.5
  • 204
    • 0030576991 scopus 로고    scopus 로고
    • Activation of plasma membrane voltage-dependent calcium-permeable channels by disruption of microtubules in carrot cells
    • Thion L, Mazars C, Thuleau P, Graziana A, Rossignol M, et al. 1996. Activation of plasma membrane voltage-dependent calcium-permeable channels by disruption of microtubules in carrot cells. FEBS Lett. 393:13-18
    • (1996) FEBS Lett. , vol.393 , pp. 13-18
    • Thion, L.1    Mazars, C.2    Thuleau, P.3    Graziana, A.4    Rossignol, M.5
  • 205
    • 0028607140 scopus 로고
    • Recruitment of plasma membrane voltage-dependent calcium-permeable channels in carrot cells
    • Thuleau P, Moreau M, Schroeder JI, Ranjeva R. 1994. Recruitment of plasma membrane voltage-dependent calcium-permeable channels in carrot cells. EMBO J. 13:5843-47
    • (1994) EMBO J. , vol.13 , pp. 5843-5847
    • Thuleau, P.1    Moreau, M.2    Schroeder, J.I.3    Ranjeva, R.4
  • 206
    • 0039803498 scopus 로고    scopus 로고
    • note
    • Deleted in proof
  • 207
    • 0030024983 scopus 로고    scopus 로고
    • Molecular cloning and characterization of genes expressed during early tomato (Lycopersicon esculentum MILL.) fruit development by mRNA differential display
    • Tieman DM, Handa AK. 1996. Molecular cloning and characterization of genes expressed during early tomato (Lycopersicon esculentum MILL.) fruit development by mRNA differential display. J. Am. Soc. Hortic. Sci. 121:52-56
    • (1996) J. Am. Soc. Hortic. Sci. , vol.121 , pp. 52-56
    • Tieman, D.M.1    Handa, A.K.2
  • 208
    • 0001046736 scopus 로고
    • Allozyme, chloroplast DNA, and RAPD markers for determining genetic relationships between Abies alba and the relic population of Abies nebrodensis
    • Vicario F, Vendramin GG, Rossi P, Lio P, Giannini R. 1995. Allozyme, chloroplast DNA, and RAPD markers for determining genetic relationships between Abies alba and the relic population of Abies nebrodensis. Theor. Appl. Genet. 90:1012-18
    • (1995) Theor. Appl. Genet. , vol.90 , pp. 1012-1018
    • Vicario, F.1    Vendramin, G.G.2    Rossi, P.3    Lio, P.4    Giannini, R.5
  • 209
    • 0029991644 scopus 로고    scopus 로고
    • Mecillinam resistance in Escherichia coli is conferred by loss of a second activity of the aroK protein
    • Vinella D, Gagny B, Joseleau-Petit D, D'Ari R, Cashel M. 1996. Mecillinam resistance in Escherichia coli is conferred by loss of a second activity of the aroK protein. J. Bacteriol. 178:3818-28
    • (1996) J. Bacteriol. , vol.178 , pp. 3818-3828
    • Vinella, D.1    Gagny, B.2    Joseleau-Petit, D.3    D'Ari, R.4    Cashel, M.5
  • 210
    • 0029846030 scopus 로고    scopus 로고
    • Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa
    • Walker GE, Dunbar B, Hunter IS, Nimmo HG, Coggins JR. 1996. Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa. Microbiology 142:1973-82
    • (1996) Microbiology , vol.142 , pp. 1973-1982
    • Walker, G.E.1    Dunbar, B.2    Hunter, I.S.3    Nimmo, H.G.4    Coggins, J.R.5
  • 211
    • 0000687016 scopus 로고
    • Z-3-fluorophosphoenol-pyruvate as a pseudosubstrate of EPSP synthase: Enzymatic synthesis of a stable fluoro analog of the catalytic intermediate
    • Walker MC, Jones CR, Somerville RL, Sikorski JA. 1992. (Z)-3-fluorophosphoenol-pyruvate as a pseudosubstrate of EPSP synthase: enzymatic synthesis of a stable fluoro analog of the catalytic intermediate. J. Am. Chem. Soc. 114:7601-3
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7601-7603
    • Walker, M.C.1    Jones, C.R.2    Somerville, R.L.3    Sikorski, J.A.4
  • 212
    • 0005647566 scopus 로고
    • Cloning and nucleotide sequence of a complementary DNA encoding 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from tobacco
    • Wang Y, Herrmann KM, Weller SC, Goldsbrough PB. 1991. Cloning and nucleotide sequence of a complementary DNA encoding 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from tobacco. Plant Physiol. 97:847-48
    • (1991) Plant Physiol. , vol.97 , pp. 847-848
    • Wang, Y.1    Herrmann, K.M.2    Weller, S.C.3    Goldsbrough, P.B.4
  • 214
    • 0025016270 scopus 로고
    • Cloning of an aroF allele encoding a tyrosine-insensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
    • Weaver LM, Herrmann KM. 1990. Cloning of an aroF allele encoding a tyrosine-insensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. J. Bacteriol. 172:6581-84
    • (1990) J. Bacteriol. , vol.172 , pp. 6581-6584
    • Weaver, L.M.1    Herrmann, K.M.2
  • 216
    • 0029961539 scopus 로고    scopus 로고
    • Control of metabolic flux through the quinate pathway in Aspergillus nidulans
    • Wheeler KA, Lamb HK, Hawkins AR. 1996. Control of metabolic flux through the quinate pathway in Aspergillus nidulans.Biochem J. 315:195-205
    • (1996) Biochem J. , vol.315 , pp. 195-205
    • Wheeler, K.A.1    Lamb, H.K.2    Hawkins, A.R.3
  • 217
    • 0028967182 scopus 로고
    • A reassessment of the relationship between aroK- and aroL-encoded shikimate kinase enzymes of Escherichia coli
    • Whipp MJ, Pittard AJ. 1995. A reassessment of the relationship between aroK- and aroL-encoded shikimate kinase enzymes of Escherichia coli. J. Bacteriol. 177:1627-29
    • (1995) J. Bacteriol. , vol.177 , pp. 1627-1629
    • Whipp, M.J.1    Pittard, A.J.2
  • 218
    • 0023897228 scopus 로고
    • The overexpression, purification and complete amino acid sequence of chorismate synthase from Escherichia coli K12 and its comparison with the enzyme from Neurospora crassa
    • White PJ, Millar G, Coggins JR. 1988. The overexpression, purification and complete amino acid sequence of chorismate synthase from Escherichia coli K12 and its comparison with the enzyme from Neurospora crassa. Biochem. J. 251:313-22
    • (1988) Biochem. J. , vol.251 , pp. 313-322
    • White, P.J.1    Millar, G.2    Coggins, J.R.3
  • 219
    • 0025176821 scopus 로고
    • The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor
    • White PJ, Young J, Hunter IS, Nimmo HG, Coggins JR. 1990. The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor. Biochem. J. 265:735-38
    • (1990) Biochem. J. , vol.265 , pp. 735-738
    • White, P.J.1    Young, J.2    Hunter, I.S.3    Nimmo, H.G.4    Coggins, J.R.5
  • 220
    • 0024517021 scopus 로고
    • Dehydroquinate synthase: A sheep in wolf's clothing?
    • Widlanski T, Bender SL, Knowles JR. 1989. Dehydroquinate synthase: a sheep in wolf's clothing? J. Am. Chem. Soc. 111:2299-300
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 2299-2300
    • Widlanski, T.1    Bender, S.L.2    Knowles, J.R.3
  • 221
    • 0024974081 scopus 로고
    • Dehydroquinate synthase: The use of substrate analogues to probe the late steps of the catalyzed reaction
    • Widlanski T, Bender SL, Knowles JR. 1989. Dehydroquinate synthase: the use of substrate analogues to probe the late steps of the catalyzed reaction. Biochemistry 28:7572-82
    • (1989) Biochemistry , vol.28 , pp. 7572-7582
    • Widlanski, T.1    Bender, S.L.2    Knowles, J.R.3
  • 222
    • 0028852680 scopus 로고
    • Shikimate dehydrogenase allozymes: Inheritance and close linkage to fruit color in the diploid strawberry
    • Williamson SC, Yu H, Davis TM. 1995. Shikimate dehydrogenase allozymes: inheritance and close linkage to fruit color in the diploid strawberry. J. Hered. 86:74-76
    • (1995) J. Hered. , vol.86 , pp. 74-76
    • Williamson, S.C.1    Yu, H.2    Davis, T.M.3
  • 224
    • 0022537538 scopus 로고
    • Cloning and characterization of the gene encoding 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Escherichia coli
    • Woisetschläger M, Högenauer G. 1986. Cloning and characterization of the gene encoding 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Escherichia coli. J. Bacteriol. 168:437-39
    • (1986) J. Bacteriol. , vol.168 , pp. 437-439
    • Woisetschläger, M.1    Högenauer, G.2
  • 225
    • 0009426318 scopus 로고
    • Purification and metal requirements of 3-dehydroquinate synthase from Phaseolus mungo seedlings
    • Yamamoto E. 1980. Purification and metal requirements of 3-dehydroquinate synthase from Phaseolus mungo seedlings. Phytochemistry 19:779-81
    • (1980) Phytochemistry , vol.19 , pp. 779-781
    • Yamamoto, E.1
  • 226
    • 0029068519 scopus 로고
    • Enzymatic carbocycle formation in microbial secondary metabolism. The mechanism of the 2-deoxy-scyllo-inosose synthase reaction as a crucial step in the 2-deoxystreptamine biosynthesis in Streptomyces fradiae
    • Yamauchi N, Kakinuma K. 1995. Enzymatic carbocycle formation in microbial secondary metabolism. The mechanism of the 2-deoxy-scyllo-inosose synthase reaction as a crucial step in the 2-deoxystreptamine biosynthesis in Streptomyces fradiae. J. Org. Chem. 60:5614-19
    • (1995) J. Org. Chem. , vol.60 , pp. 5614-5619
    • Yamauchi, N.1    Kakinuma, K.2
  • 227
    • 0005757157 scopus 로고
    • Cloning and sequencing of a second cDNA encoding 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Solanum tuberosum L
    • Zhao J, Herrmann KM. 1992. Cloning and sequencing of a second cDNA encoding 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Solanum tuberosum L. Plant Physiol. 100:1075-76
    • (1992) Plant Physiol. , vol.100 , pp. 1075-1076
    • Zhao, J.1    Herrmann, K.M.2
  • 228
    • 0019382235 scopus 로고
    • Structure and regulation of aroH, the structural gene for the tryptophan-repressible 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli
    • Zurawski G, Gunsalus RP, Brown KD, Yanofsky C. 1981. Structure and regulation of aroH, the structural gene for the tryptophan-repressible 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli. J. Mol. Biol 145:47-73
    • (1981) J. Mol. Biol , vol.145 , pp. 47-73
    • Zurawski, G.1    Gunsalus, R.P.2    Brown, K.D.3    Yanofsky, C.4


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