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Volumn 584, Issue 20, 2010, Pages 4357-4360

Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: The last homeless enzyme of aromatic amino acids biosynthesis

Author keywords

Aromatic amino acid; Aspartate aminotransferase; Enzymology; Metabolism; Plant; Prephenate aminotransferase

Indexed keywords

AMINOTRANSFERASE; AROMATIC AMINO ACID; ASPARTATE AMINOTRANSFERASE; GLUTAMIC ACID; PREPHENATE AMINOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 77957797082     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.09.037     Document Type: Article
Times cited : (52)

References (33)
  • 1
    • 0004112742 scopus 로고
    • John Wiley and Sons, Chichester, UK, E. Haslam (Ed.)
    • Shikimic Acid Metabolism and Metabolites 1993, John Wiley and Sons, Chichester, UK. E. Haslam (Ed.).
    • (1993) Shikimic Acid Metabolism and Metabolites
  • 3
    • 0032007403 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • Dewick P.M. The biosynthesis of shikimate metabolites. Nat. Prod. Rep. 1998, 15:17-58.
    • (1998) Nat. Prod. Rep. , vol.15 , pp. 17-58
    • Dewick, P.M.1
  • 5
    • 0016230417 scopus 로고
    • Blue-green bacteria synthesize l-tyrosine by pretyrosine pathway
    • Stenmark S.L., Pierson D.L., Jensen R.A. Blue-green bacteria synthesize l-tyrosine by pretyrosine pathway. Nature 1974, 247:290-292.
    • (1974) Nature , vol.247 , pp. 290-292
    • Stenmark, S.L.1    Pierson, D.L.2    Jensen, R.A.3
  • 6
    • 0018388495 scopus 로고
    • Obligatory biosynthesis of l-tyrosine via the pretyrosine branchlet in Coryneform bacteria
    • Fazel A.M., Jensen R.A. Obligatory biosynthesis of l-tyrosine via the pretyrosine branchlet in Coryneform bacteria. J. Bacteriol. 1979, 138:805-815.
    • (1979) J. Bacteriol. , vol.138 , pp. 805-815
    • Fazel, A.M.1    Jensen, R.A.2
  • 7
    • 0020038934 scopus 로고
    • Biochemical diversity for biosynthesis of aromatic-amino-acids among the Cyanobacteria
    • Hall G.C., Flick M.B., Gherna R.L., Jensen R.A. Biochemical diversity for biosynthesis of aromatic-amino-acids among the Cyanobacteria. J. Bacteriol. 1982, 149:65-78.
    • (1982) J. Bacteriol. , vol.149 , pp. 65-78
    • Hall, G.C.1    Flick, M.B.2    Gherna, R.L.3    Jensen, R.A.4
  • 8
    • 0022386450 scopus 로고
    • Arogenate dehydrogenase from Streptomyces phaeochromogenes - purification and properties
    • Keller B., Keller E., Lingens F. Arogenate dehydrogenase from Streptomyces phaeochromogenes - purification and properties. Biol. Chem. Hoppe Seyler 1985, 366:1063-1066.
    • (1985) Biol. Chem. Hoppe Seyler , vol.366 , pp. 1063-1066
    • Keller, B.1    Keller, E.2    Lingens, F.3
  • 9
    • 0024728967 scopus 로고
    • Purification and properties of arogenate dehydrogenase from Actinoplanes missouriensis
    • Hund H.K., Bar G., Lingens F. Purification and properties of arogenate dehydrogenase from Actinoplanes missouriensis. Z. Naturforsch., C. 1989, 44:797-801.
    • (1989) Z. Naturforsch., C. , vol.44 , pp. 797-801
    • Hund, H.K.1    Bar, G.2    Lingens, F.3
  • 10
    • 0014939940 scopus 로고
    • Enzymology of prephenate dehydrogenase in Bacillus subtilis
    • Champney W.S., Jensen R.A. Enzymology of prephenate dehydrogenase in Bacillus subtilis. J. Biol. Chem. 1970, 245:3763.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3763
    • Champney, W.S.1    Jensen, R.A.2
  • 11
    • 0019157036 scopus 로고
    • Variable enzymological patterning in tyrosine biosynthesis as a means of determining natural relatedness among the Pseudomonadaceae
    • Byng G.S., Whitaker R.J., Gherna R.L., Jensen R.A. Variable enzymological patterning in tyrosine biosynthesis as a means of determining natural relatedness among the Pseudomonadaceae. J. Bacteriol. 1980, 144:247-257.
    • (1980) J. Bacteriol. , vol.144 , pp. 247-257
    • Byng, G.S.1    Whitaker, R.J.2    Gherna, R.L.3    Jensen, R.A.4
  • 12
    • 0017696820 scopus 로고
    • Dual enzymatic routes to l-tyrosine and l-phenylalanine via pretyrosine in Pseudomonas aeruginosa
    • Patel N., Pierson D.L., Jensen R.A. Dual enzymatic routes to l-tyrosine and l-phenylalanine via pretyrosine in Pseudomonas aeruginosa. J. Biol. Chem. 1977, 252:5839-5846.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5839-5846
    • Patel, N.1    Pierson, D.L.2    Jensen, R.A.3
  • 13
    • 0027510178 scopus 로고
    • An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis
    • Zhao G., Xia T.H., Ingram L.O., Jensen R.A. An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis. Eur. J. Biochem. 1993, 212:157-165.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 157-165
    • Zhao, G.1    Xia, T.H.2    Ingram, L.O.3    Jensen, R.A.4
  • 14
    • 0034037947 scopus 로고    scopus 로고
    • Cyclohexadienyl dehydrogenase from Pseudomonas stutzeri exemplifies a widespread type of tyrosine-pathway dehydrogenase in the TyrA protein family
    • Xie G., Bonner C.A., Jensen R.A. Cyclohexadienyl dehydrogenase from Pseudomonas stutzeri exemplifies a widespread type of tyrosine-pathway dehydrogenase in the TyrA protein family. Comp. Biochem. Physiol., C: Toxicol. Pharmacol. 2000, 125:65-83.
    • (2000) Comp. Biochem. Physiol., C: Toxicol. Pharmacol. , vol.125 , pp. 65-83
    • Xie, G.1    Bonner, C.A.2    Jensen, R.A.3
  • 15
    • 0028813444 scopus 로고
    • Molecular organization of the shikimate pathway in higher plants
    • Schmid J., Amrhein N. Molecular organization of the shikimate pathway in higher plants. Phytochemistry 1995, 39:737-749.
    • (1995) Phytochemistry , vol.39 , pp. 737-749
    • Schmid, J.1    Amrhein, N.2
  • 17
    • 40849135777 scopus 로고    scopus 로고
    • Cohesion group approach for evolutionary analysis of TyrA, a protein family with wide-ranging substrate specificities
    • Bonner C.A., Disz T., Hwang K., Song B., Vonstein V., Overbeek R., Jensen R.A. Cohesion group approach for evolutionary analysis of TyrA, a protein family with wide-ranging substrate specificities. Microbiol. Mol. Biol. Rev. 2008, 72:13-53.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 13-53
    • Bonner, C.A.1    Disz, T.2    Hwang, K.3    Song, B.4    Vonstein, V.5    Overbeek, R.6    Jensen, R.A.7
  • 18
    • 0022796778 scopus 로고
    • Chloroplasts of higher plants synthesize l-phenylalanine via l-arogenate
    • Jung E., Zamir L.O., Jensen R.A. Chloroplasts of higher plants synthesize l-phenylalanine via l-arogenate. Proc. Natl Acad. Sci. USA 1986, 83:7231-7235.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 7231-7235
    • Jung, E.1    Zamir, L.O.2    Jensen, R.A.3
  • 19
    • 0022567272 scopus 로고
    • Tyrosine biosynthesis in Sorghum bicolore - characteristics of prephenate aminotransferase
    • Siehl D.L., Connelly J.A., Conn E.E. Tyrosine biosynthesis in Sorghum bicolore - characteristics of prephenate aminotransferase. Z. Naturforsch., C. 1986, 41:79-86.
    • (1986) Z. Naturforsch., C. , vol.41 , pp. 79-86
    • Siehl, D.L.1    Connelly, J.A.2    Conn, E.E.3
  • 20
    • 0036399671 scopus 로고    scopus 로고
    • Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana
    • Rippert P., Matringe M. Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana. Eur. J. Biochem. 2002, 269:4753-4761.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4753-4761
    • Rippert, P.1    Matringe, M.2
  • 21
    • 0022050797 scopus 로고
    • Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris
    • Bonner C.A., Jensen R.A. Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris. Arch. Biochem. Biophys. 1985, 238:237-246.
    • (1985) Arch. Biochem. Biophys. , vol.238 , pp. 237-246
    • Bonner, C.A.1    Jensen, R.A.2
  • 22
    • 0024289208 scopus 로고
    • Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures
    • De-Eknamkul W., Ellis B.E. Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures. Arch. Biochem. Biophys. 1988, 267:87-94.
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 87-94
    • De-Eknamkul, W.1    Ellis, B.E.2
  • 23
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0016160429 scopus 로고
    • Measurement of protein by spectroscopy at 205nm
    • Scopes R.K. Measurement of protein by spectroscopy at 205nm. Anal. Biochem. 1974, 59:277-282.
    • (1974) Anal. Biochem. , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 25
    • 2542430082 scopus 로고    scopus 로고
    • Methionine metabolism in plants: chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosylmethionine from the cytosol
    • Ravanel S., Block M.A., Rippert P., Jabrin S., Curien G., Rebeille F., Douce R. Methionine metabolism in plants: chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosylmethionine from the cytosol. J. Biol. Chem. 2004, 279:22548-22557.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22548-22557
    • Ravanel, S.1    Block, M.A.2    Rippert, P.3    Jabrin, S.4    Curien, G.5    Rebeille, F.6    Douce, R.7
  • 28
    • 33646476472 scopus 로고    scopus 로고
    • Biochemical characterization and crystal structure of Synechocystis arogenate dehydrogenase provide insights into catalytic reaction
    • Legrand P., Dumas R., Seux M., Rippert P., Ravelli R., Ferrer J.L., Matringe M. Biochemical characterization and crystal structure of Synechocystis arogenate dehydrogenase provide insights into catalytic reaction. Structure 2006, 14:767-776.
    • (2006) Structure , vol.14 , pp. 767-776
    • Legrand, P.1    Dumas, R.2    Seux, M.3    Rippert, P.4    Ravelli, R.5    Ferrer, J.L.6    Matringe, M.7
  • 29
    • 72949124984 scopus 로고
    • Glutamic-oxaloacetic transaminase of cauliflower
    • Ellis R.J., Davies D.D. Glutamic-oxaloacetic transaminase of cauliflower. Biochem. J. 1961, 78:615-623.
    • (1961) Biochem. J. , vol.78 , pp. 615-623
    • Ellis, R.J.1    Davies, D.D.2
  • 30
    • 0028369994 scopus 로고
    • Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis
    • Ilag L.L., Kumar A.M., Soll D. Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis. Plant Cell 1994, 6:265-275.
    • (1994) Plant Cell , vol.6 , pp. 265-275
    • Ilag, L.L.1    Kumar, A.M.2    Soll, D.3
  • 31
    • 33645690084 scopus 로고    scopus 로고
    • Identification and functional analysis of a prokaryotic-type aspartate aminotransferase: implications for plant amino acid metabolism
    • de la Torre F., De Santis L., Suarez M.F., Crespillo R., Canovas F.M. Identification and functional analysis of a prokaryotic-type aspartate aminotransferase: implications for plant amino acid metabolism. Plant J. 2006, 46:414-425.
    • (2006) Plant J. , vol.46 , pp. 414-425
    • de la Torre, F.1    De Santis, L.2    Suarez, M.F.3    Crespillo, R.4    Canovas, F.M.5
  • 32
    • 63549135053 scopus 로고    scopus 로고
    • Tyrosine and phenylalanine are synthesized within the plastids in Arabidopsis
    • Rippert P., Puyaubert J., Grisollet D., Derrier L., Matringe M. Tyrosine and phenylalanine are synthesized within the plastids in Arabidopsis. Plant Physiol. 2009, 149:1251-1260.
    • (2009) Plant Physiol. , vol.149 , pp. 1251-1260
    • Rippert, P.1    Puyaubert, J.2    Grisollet, D.3    Derrier, L.4    Matringe, M.5
  • 33
    • 0032053022 scopus 로고    scopus 로고
    • Recombinant expression, purification, and characterization of three isoenzymes of aspartate aminotransferase from Arabidopsis thaliana
    • Wilkie S.E., Warren M.J. Recombinant expression, purification, and characterization of three isoenzymes of aspartate aminotransferase from Arabidopsis thaliana. Protein Expr. Purif. 1998, 12:381-389.
    • (1998) Protein Expr. Purif. , vol.12 , pp. 381-389
    • Wilkie, S.E.1    Warren, M.J.2


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