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Volumn 396, Issue 1, 2006, Pages 157-162

Folate synthesis in plants: Purification, kinetic properties, and inhibition of aminodeoxychorismate synthase

Author keywords

Aminodeoxychorismate synthase; C1 metabolism; Folate; Methotrexate; P aminobenzoate; Plastid

Indexed keywords

AMINES; COMPLEXATION; ESCHERICHIA COLI; METABOLISM; PLANTS (BOTANY); PURIFICATION;

EID: 33646810095     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051851     Document Type: Article
Times cited : (29)

References (34)
  • 1
    • 0342700245 scopus 로고    scopus 로고
    • Folic acid and folates: The feasibility for nutritional enhancement in plant foods
    • Scott, J., Rébeillé, F. and Fletcher, J. (2000) Folic acid and folates: the feasibility for nutritional enhancement in plant foods. J. Sci. Food Agric. 80, 795-824
    • (2000) J. Sci. Food Agric. , vol.80 , pp. 795-824
    • Scott, J.1    Rébeillé, F.2    Fletcher, J.3
  • 2
    • 31844446467 scopus 로고    scopus 로고
    • The uniqueness of tetrahydrofolate synthesis and one-carbon metabolism in plants
    • (Day, D. A., Millar, H. and Whelan, J., eds.). Kluwer Academic, Amsterdam
    • Ravanel, S., Douce, R. and Rébeillé, F. (2004) The uniqueness of tetrahydrofolate synthesis and one-carbon metabolism in plants. In Plant Mitochondria from Genome to Function (Day, D. A., Millar, H. and Whelan, J., eds.), pp. 277-292, Kluwer Academic, Amsterdam
    • (2004) Plant Mitochondria from Genome to Function , pp. 277-292
    • Ravanel, S.1    Douce, R.2    Rébeillé, F.3
  • 4
    • 14844341424 scopus 로고    scopus 로고
    • Folate synthesis and metabolism in plants and prospects for biofortification
    • Basset, G. J. C., Quinlivan, E. P., Gregory, J. F. and Hanson, A. D. (2005) Folate synthesis and metabolism in plants and prospects for biofortification. Crop Sci. 45, 449-453
    • (2005) Crop Sci. , vol.45 , pp. 449-453
    • Basset, G.J.C.1    Quinlivan, E.P.2    Gregory, J.F.3    Hanson, A.D.4
  • 7
    • 0010980140 scopus 로고    scopus 로고
    • The biosynthesis of tryptophan, tyrosine and phenylalanine from chorismate
    • (Singh, B. K., ed.). Marcel Dekker Inc., New York
    • Siehl, D. (1999) The biosynthesis of tryptophan, tyrosine and phenylalanine from chorismate. In Plant Amino Acids (Singh, B. K., ed.), pp. 171-204, Marcel Dekker Inc., New York
    • (1999) Plant Amino Acids , pp. 171-204
    • Siehl, D.1
  • 8
    • 1542306930 scopus 로고    scopus 로고
    • Conservation of mechanism in three chorismate-utilizing enzymes
    • He, Z., Stigers Lavoie, K. D., Bartlett, P. A. and Toney, M. D. (2004) Conservation of mechanism in three chorismate-utilizing enzymes. J. Am. Chem. Soc. 126, 2378-2385
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2378-2385
    • He, Z.1    Stigers Lavoie, K.D.2    Bartlett, P.A.3    Toney, M.D.4
  • 9
    • 0024403436 scopus 로고
    • Para-aminobenzoate synthesis from chorismate occurs in two steps
    • Nichols, B. P., Seibold, A. M. and Doktor, S. Z. (1989) para-aminobenzoate synthesis from chorismate occurs in two steps. J. Biol. Chem. 264, 8597-8601
    • (1989) J. Biol. Chem. , vol.264 , pp. 8597-8601
    • Nichols, B.P.1    Seibold, A.M.2    Doktor, S.Z.3
  • 10
    • 0028809784 scopus 로고
    • Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli
    • Viswanathan, V. K., Green, J. M. and Nichols, B. P. (1995) Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli. J. Bacteriol. 177, 5918-5923
    • (1995) J. Bacteriol. , vol.177 , pp. 5918-5923
    • Viswanathan, V.K.1    Green, J.M.2    Nichols, B.P.3
  • 11
    • 0027174079 scopus 로고
    • p-aminobenzoate synthesis in Escherichia coli: Mutational analysis of three conserved amino acid residues of the amidotransferase PabA
    • Roux, B. and Walsh, C. T. (1993) p-Aminobenzoate synthesis in Escherichia coli: mutational analysis of three conserved amino acid residues of the amidotransferase PabA. Biochemistry 32, 3763-3768
    • (1993) Biochemistry , vol.32 , pp. 3763-3768
    • Roux, B.1    Walsh, C.T.2
  • 12
    • 0025647889 scopus 로고
    • p-aminobenzoate synthesis in Escherichia coli: Purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase
    • Ye, Q. Z., Liu, J. and Walsh, C. T. (1990) p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase. Proc. Natl. Acad. Sci. U.S.A. 87, 9391-9395
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 9391-9395
    • Ye, Q.Z.1    Liu, J.2    Walsh, C.T.3
  • 13
    • 0025737957 scopus 로고
    • p-aminobenzoate biosynthesis in Escherichia coli: Purification of aminodeoxychorismate lyase and cloning of pabC
    • Green, J. M. and Nichols, B. P. (1991) p-Aminobenzoate biosynthesis in Escherichia coli: purification of aminodeoxychorismate lyase and cloning of pabC. J. Biol. Chem. 266, 12971-12975
    • (1991) J. Biol. Chem. , vol.266 , pp. 12971-12975
    • Green, J.M.1    Nichols, B.P.2
  • 14
    • 0026643934 scopus 로고
    • p-aminobenzoate synthesis in Escherichia coli: Kinetic and mechanistic characterization of the amidotransferase PabA
    • Roux, B. and Walsh, C. T. (1992) p-aminobenzoate synthesis in Escherichia coli: kinetic and mechanistic characterization of the amidotransferase PabA. Biochemistry 31, 6904-6910
    • (1992) Biochemistry , vol.31 , pp. 6904-6910
    • Roux, B.1    Walsh, C.T.2
  • 15
    • 0037133196 scopus 로고    scopus 로고
    • Structure of Escherichia coli aminodeoxychorismate synthase: Architectural conservation and diversity in chorismate-utilizing enzymes
    • Parsons, J. F., Jensen, P. Y., Pachikara, A. S., Howard, A. J., Eisenstein, E. and Ladner, J. E. (2002) Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes. Biochemistry 41, 2198-2208
    • (2002) Biochemistry , vol.41 , pp. 2198-2208
    • Parsons, J.F.1    Jensen, P.Y.2    Pachikara, A.S.3    Howard, A.J.4    Eisenstein, E.5    Ladner, J.E.6
  • 16
    • 0035123059 scopus 로고    scopus 로고
    • Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium
    • Morollo, A. A. and Eck, M. J. (2001) Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium. Nat. Struct. Biol. 8, 243-247
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 243-247
    • Morollo, A.A.1    Eck, M.J.2
  • 17
    • 4043179710 scopus 로고    scopus 로고
    • Identification of 4-amino-4-deoxychorismate synthase as the molecular target for the antimicrobial action of (6s)-6-fluoroshikimate
    • Bulloch, E. M., Jones, M. A., Parker, E. J., Osborne, A. P., Stephens, E., Davies, G. M., Coggins, J. R. and Abell, C. (2004) Identification of 4-amino-4-deoxychorismate synthase as the molecular target for the antimicrobial action of (6s)-6-fluoroshikimate. J. Am. Chem. Soc. 126, 9912-9913
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9912-9913
    • Bulloch, E.M.1    Jones, M.A.2    Parker, E.J.3    Osborne, A.P.4    Stephens, E.5    Davies, G.M.6    Coggins, J.R.7    Abell, C.8
  • 19
    • 0027483510 scopus 로고
    • The pab gene of Streptomyces griseus, encoding p-aminobenzoic acid synthase, is located between genes possibly involved in candicidin biosynthesis
    • Criado, L. M., Martin, J. F. and Gil, J. A. (1993) The pab gene of Streptomyces griseus, encoding p-aminobenzoic acid synthase, is located between genes possibly involved in candicidin biosynthesis. Gene 126, 135-139
    • (1993) Gene , vol.126 , pp. 135-139
    • Criado, L.M.1    Martin, J.F.2    Gil, J.A.3
  • 20
    • 0027230987 scopus 로고
    • Para-aminobenzoate synthase gene of Saccharomyces cerevisiae encodes a bifunctional enzyme
    • Edman, J. C., Goldstein, A. L. and Erbe, J. G. (1993) Para-aminobenzoate synthase gene of Saccharomyces cerevisiae encodes a bifunctional enzyme. Yeast 9, 669-675
    • (1993) Yeast , vol.9 , pp. 669-675
    • Edman, J.C.1    Goldstein, A.L.2    Erbe, J.G.3
  • 21
    • 0032777096 scopus 로고    scopus 로고
    • Plasmodium falciparum: A homologue of p-aminobenzoic acid synthetase
    • Triglia, T. and Cowman, A. F. (1999) Plasmodium falciparum: a homologue of p-aminobenzoic acid synthetase. Exp. Parasitol. 92, 154-158
    • (1999) Exp. Parasitol. , vol.92 , pp. 154-158
    • Triglia, T.1    Cowman, A.F.2
  • 23
    • 0018845614 scopus 로고
    • Methods for reduction, stabilization, and analyses of folates
    • Scrimgeour, K. G. (1980) Methods for reduction, stabilization, and analyses of folates. Methods Enzymol. 66, 517-523
    • (1980) Methods Enzymol. , vol.66 , pp. 517-523
    • Scrimgeour, K.G.1
  • 24
    • 0001835763 scopus 로고
    • Chemical and physical properties of folic acid and reduced derivatives
    • (Blakley, R. L. and Benkovic, S. J., eds.). Wiley (Interscience), New York
    • Temple, Jr, C. and Montgomery, J. A. (1984) Chemical and physical properties of folic acid and reduced derivatives. In Folates and Pterins (Blakley, R. L. and Benkovic, S. J., eds.), vol. 1, pp. 61-120, Wiley (Interscience), New York
    • (1984) Folates and Pterins , vol.1 , pp. 61-120
    • Temple Jr., C.1    Montgomery, J.A.2
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H. and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223-231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 27
    • 0000620845 scopus 로고
    • L-glutamate: UV-assay with glutamate dehydrogenase and NAD
    • (Bergmeyer, H. U., ed.). Academic Press, New York
    • Bernt, E. and Bergmeyer, H. U. (1974) L-glutamate: UV-assay with glutamate dehydrogenase and NAD. In Methods of Enzymatic Analysis (Bergmeyer, H. U., ed.), pp. 1704-1708, Academic Press, New York
    • (1974) Methods of Enzymatic Analysis , pp. 1704-1708
    • Bernt, E.1    Bergmeyer, H.U.2
  • 28
    • 0001262581 scopus 로고
    • Pyruvate. Fluorimetric assay
    • (Bergmeyer, H., ed.). Academic Press, New York
    • Czok, R. and Lamprecht, W. (1974) Pyruvate. Fluorimetric assay. In Methods of Enzymatic Analysis (Bergmeyer, H., ed.), pp. 1446-1451, Academic Press, New York
    • (1974) Methods of Enzymatic Analysis , pp. 1446-1451
    • Czok, R.1    Lamprecht, W.2
  • 29
    • 0028931375 scopus 로고
    • Chorismate-utilizing enzymes isochorismate synthase, anthranilate synthase, and p-aminobenzoate synthase: Mechanistic insight through inhibitor design
    • Kozlowski, M. C., Tom, N. J., Seto, C. T., Sefler, A. M. and Bartlett, P. A. (1995) Chorismate-utilizing enzymes isochorismate synthase, anthranilate synthase, and p-aminobenzoate synthase: mechanistic insight through inhibitor design. J. Am. Chem. Soc. 117, 2128-2140
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2128-2140
    • Kozlowski, M.C.1    Tom, N.J.2    Seto, C.T.3    Sefler, A.M.4    Bartlett, P.A.5
  • 30
    • 0029294740 scopus 로고
    • Anthranilate synthase in microorganisms and plants
    • Romero, R. M., Roberts, M. F. and Phillipson, J. D. (1995) Anthranilate synthase in microorganisms and plants. Phytochemistry 39, 263-276
    • (1995) Phytochemistry , vol.39 , pp. 263-276
    • Romero, R.M.1    Roberts, M.F.2    Phillipson, J.D.3
  • 31
    • 0030295189 scopus 로고    scopus 로고
    • Cytosolic and plastidic chorismate mutase isozymes from Arabidopsis thaliana: Molecular characterization and enzymatic properties
    • Eberhard, J., Ehrler, T. T., Epple, P., Felix, G., Raesecke, H. R., Amrhein, N. and Schmid, J. (1996) Cytosolic and plastidic chorismate mutase isozymes from Arabidopsis thaliana: molecular characterization and enzymatic properties. Plant J. 10, 815-821
    • (1996) Plant J. , vol.10 , pp. 815-821
    • Eberhard, J.1    Ehrler, T.T.2    Epple, P.3    Felix, G.4    Raesecke, H.R.5    Amrhein, N.6    Schmid, J.7
  • 32
    • 0003518480 scopus 로고
    • John Wiley and Sons, New York
    • Segel, I. H. (1975) Enzyme Kinetics, John Wiley and Sons, New York
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 33
    • 0001870161 scopus 로고    scopus 로고
    • Folate synthesis and compartmentation in higher plants
    • (Kruger, N. J., Hill, S. A. and Ratcliffe, R. G., eds.). Kluwer Academic Publishers, Amsterdam
    • Rébeillé, F. and Douce, R. (1999) Folate synthesis and compartmentation in higher plants. In Regulation of Primary Metabolic Pathways in Plants (Kruger, N. J., Hill, S. A. and Ratcliffe, R. G., eds.), Kluwer Academic Publishers, Amsterdam
    • (1999) Regulation of Primary Metabolic Pathways in Plants
    • Rébeillé, F.1    Douce, R.2
  • 34
    • 0036843244 scopus 로고    scopus 로고
    • Recycled plastids: A 'green movement' in eukaryotic evolution
    • Archibald, J. M. and Keeling, P. J. (2002) Recycled plastids: a 'green movement' in eukaryotic evolution. Trends Genet. 18, 577-584
    • (2002) Trends Genet. , vol.18 , pp. 577-584
    • Archibald, J.M.1    Keeling, P.J.2


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