메뉴 건너뛰기




Volumn 18, Issue 10, 2006, Pages 2664-2679

BRANCHED-CHAIN AMINOTRANSFERASE4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; METABOLISM; PLANTS (BOTANY);

EID: 33750975632     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.105.039339     Document Type: Article
Times cited : (155)

References (67)
  • 1
    • 0042768158 scopus 로고    scopus 로고
    • Genome-wide insertional mutagenesis of Arabidopsis thaliana
    • Alonso, J.M., et al. (2003). Genome-wide insertional mutagenesis of Arabidopsis thaliana. Science 301, 653-657.
    • (2003) Science , vol.301 , pp. 653-657
    • Alonso, J.M.1
  • 3
    • 9244221583 scopus 로고    scopus 로고
    • Aromatic amino acid transamination and methicnine recycling in trypanosomatids
    • Berger, B.J., Dai, W.W., Wang, H., Stark, R.E., and Cerami, A. (1996). Aromatic amino acid transamination and methicnine recycling in trypanosomatids. Proc. Natl. Acad. Sci. USA 93, 4126-4130.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4126-4130
    • Berger, B.J.1    Dai, W.W.2    Wang, H.3    Stark, R.E.4    Cerami, A.5
  • 4
    • 0037384217 scopus 로고    scopus 로고
    • Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
    • Berger, B.J., English, S., Chan, G., and Knodel, M.H. (2003). Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis. J. Bacteriol. 185, 2418-2431.
    • (2003) J. Bacteriol. , vol.185 , pp. 2418-2431
    • Berger, B.J.1    English, S.2    Chan, G.3    Knodel, M.H.4
  • 5
    • 0034932250 scopus 로고    scopus 로고
    • Methionine regeneration and aspartate aminotransferase in parasitic protozoa
    • Berger, L.C., Wilson, J., Wood, P., and Berger, B.J. (2001). Methionine regeneration and aspartate aminotransferase in parasitic protozoa. J. Bacteriol. 183, 4421-4434.
    • (2001) J. Bacteriol. , vol.183 , pp. 4421-4434
    • Berger, L.C.1    Wilson, J.2    Wood, P.3    Berger, B.J.4
  • 6
  • 8
    • 0037311116 scopus 로고    scopus 로고
    • Variation of glucosinolate accumulation among different organs and developmental stages of Arabidopsis thaliana
    • Brown, P.D., Tokuhisa, J.G., Reichelt, M., and Gershenzon, J. (2003). Variation of glucosinolate accumulation among different organs and developmental stages of Arabidopsis thaliana. Phytochemistry 62, 471-481.
    • (2003) Phytochemistry , vol.62 , pp. 471-481
    • Brown, P.D.1    Tokuhisa, J.G.2    Reichelt, M.3    Gershenzon, J.4
  • 9
    • 0000544202 scopus 로고
    • Purification and characterization of methionine:glyoxylate aminotransferase from Brassica carinata and Brassica napus
    • Chappie, C.C.S., Glover, J.R., and Ellis, B.E. (1990). Purification and characterization of methionine:glyoxylate aminotransferase from Brassica carinata and Brassica napus. Plant Physiol. 94, 1887-1896.
    • (1990) Plant Physiol. , vol.94 , pp. 1887-1896
    • Chappie, C.C.S.1    Glover, J.R.2    Ellis, B.E.3
  • 12
    • 0042838359 scopus 로고    scopus 로고
    • S-adenosyl-L-methionine is an effector in the posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis
    • Chiba, Y., Sakurai, R., Yoshino, M., Ominato, K., Ishikawa, M., Onouchi, H., and Naito, S. (2003). S-adenosyl-L-methionine is an effector in the posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis. Proc. Natl. Acad. Sci. USA 100, 10225-10230.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10225-10230
    • Chiba, Y.1    Sakurai, R.2    Yoshino, M.3    Ominato, K.4    Ishikawa, M.5    Onouchi, H.6    Naito, S.7
  • 13
    • 0034979962 scopus 로고    scopus 로고
    • The mitochondrial isovaleryl-coenzyme a dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism
    • Däschner, K., Couee, I., and Binder, S. (2001). The mitochondrial isovaleryl-coenzyme a dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism. Plant Physiol. 126, 601-612.
    • (2001) Plant Physiol. , vol.126 , pp. 601-612
    • Däschner, K.1    Couee, I.2    Binder, S.3
  • 14
    • 0032030760 scopus 로고    scopus 로고
    • Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants
    • Davis, S.J., and Vierstra, R.D. (1998). Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants. Plant Mol. Biol. 36, 521-528.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 521-528
    • Davis, S.J.1    Vierstra, R.D.2
  • 15
    • 0035983618 scopus 로고    scopus 로고
    • The branched-chain amino acid transaminase gene family in Arabidopsis encodes plastid and mitochondrial proteins
    • Diebold, R., Schuster, J., Däschner, K., and Binder, S. (2002). The branched-chain amino acid transaminase gene family in Arabidopsis encodes plastid and mitochondrial proteins. Plant Physiol. 129, 540-550.
    • (2002) Plant Physiol. , vol.129 , pp. 540-550
    • Diebold, R.1    Schuster, J.2    Däschner, K.3    Binder, S.4
  • 16
    • 0029103642 scopus 로고
    • Selective induction of glucosinolates in oilseed rape seed leaves with methyl jasmonate
    • Doughty, P.A., Kiddle, G.A., Pye, B.J., Wallsgrove, R.M., and Pickett, J.A. (1995). Selective induction of glucosinolates in oilseed rape seed leaves with methyl jasmonate. Phytochemistry 38, 347-350.
    • (1995) Phytochemistry , vol.38 , pp. 347-350
    • Doughty, P.A.1    Kiddle, G.A.2    Pye, B.J.3    Wallsgrove, R.M.4    Pickett, J.A.5
  • 17
    • 0141953689 scopus 로고    scopus 로고
    • Efficient regeneration from cotelydon protoplast in Arabidopsis thaliana
    • Dovzhenko, A., Dal Bosco, C., Meuer, J., and Koop, H.-U. (2003). Efficient regeneration from cotelydon protoplast in Arabidopsis thaliana. Protoplasma 222, 107-111.
    • (2003) Protoplasma , vol.222 , pp. 107-111
    • Dovzhenko, A.1    Dal Bosco, C.2    Meuer, J.3    Koop, H.-U.4
  • 18
    • 1942419908 scopus 로고    scopus 로고
    • Glucosinolate biosynthesis: Demonstration and characterization of the condensing enzyme of the chain elongation cycle in Eruca sativa
    • Falk, K.L., Vogel, C., Textor, S., Bartram, S., Hick, A., Pickett, J.A., and Gershenzon, J. (2004). Glucosinolate biosynthesis: Demonstration and characterization of the condensing enzyme of the chain elongation cycle in Eruca sativa. Phytochemistry 65, 1073-1084.
    • (2004) Phytochemistry , vol.65 , pp. 1073-1084
    • Falk, K.L.1    Vogel, C.2    Textor, S.3    Bartram, S.4    Hick, A.5    Pickett, J.A.6    Gershenzon, J.7
  • 20
    • 0033736521 scopus 로고    scopus 로고
    • Mechanisms to account for maintenance of the soluble methionine pool in transgenic Arabidopsis plants expressing antisense cystathionine gamma-synthase cDNA
    • Gakiere, B., Ravanel, S., Droux, M., Douce, R., and Job, D. (2000). Mechanisms to account for maintenance of the soluble methionine pool in transgenic Arabidopsis plants expressing antisense cystathionine gamma-synthase cDNA. C. R. Acad. Sci. III 323, 841-851.
    • (2000) C. R. Acad. Sci. III , vol.323 , pp. 841-851
    • Gakiere, B.1    Ravanel, S.2    Droux, M.3    Douce, R.4    Job, D.5
  • 21
    • 0034659867 scopus 로고    scopus 로고
    • The methionine chain elongation pathway in the biosynthesis of glucosinolates in Eruca sativa (Brassicaceae)
    • Graser, G., Schneider, B., Oldham, N.J., and Gershenzon, J. (2000). The methionine chain elongation pathway in the biosynthesis of glucosinolates in Eruca sativa (Brassicaceae). Arch. Biochem. Biophys. 378, 411-419.
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 411-419
    • Graser, G.1    Schneider, B.2    Oldham, N.J.3    Gershenzon, J.4
  • 22
    • 32544436982 scopus 로고    scopus 로고
    • Glucosinolate metabolism and its control
    • Grubb, C.D., and Abel, S. (2006). Glucosinolate metabolism and its control. Trends Plant Sci. 11, 89-100.
    • (2006) Trends Plant Sci. , vol.11 , pp. 89-100
    • Grubb, C.D.1    Abel, S.2
  • 23
    • 85047681599 scopus 로고    scopus 로고
    • The N-terminal region of Arabidopsis cystathionine gamma-synthase plays an imporregulatory role in methionine metabolism
    • Hacham, Y., Avraham, T., and Amir, R. (2002). The N-terminal region of Arabidopsis cystathionine gamma-synthase plays an imporregulatory role in methionine metabolism. Plant Physiol. 128, 454-462.
    • (2002) Plant Physiol. , vol.128 , pp. 454-462
    • Hacham, Y.1    Avraham, T.2    Amir, R.3
  • 24
    • 33644771070 scopus 로고    scopus 로고
    • An in vivo internal deletion in the N-terminus region of Arabidopsis cystathionine gamma-synthase results in CGS expression that is insensitive to methionine
    • Hacham, Y., Schuster, G., and Amir, R. (2006). An in vivo internal deletion in the N-terminus region of Arabidopsis cystathionine gamma-synthase results in CGS expression that is insensitive to methionine. Plant J. 45, 955-967.
    • (2006) Plant J. , vol.45 , pp. 955-967
    • Hacham, Y.1    Schuster, G.2    Amir, R.3
  • 25
    • 0033028593 scopus 로고    scopus 로고
    • Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumonias
    • Heilbronn, J., Wilson, J., and Berger, B.J. (1999). Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumonias. J. Bacteriol. 181, 1739-1747.
    • (1999) J. Bacteriol. , vol.181 , pp. 1739-1747
    • Heilbronn, J.1    Wilson, J.2    Berger, B.J.3
  • 26
    • 4344566293 scopus 로고    scopus 로고
    • Current understanding of the regulation of methionine biosynthesis in plants
    • Hesse, H., Kreft, O., Maimann, S., Zeh, M., and Hoefgen, R. (2004). Current understanding of the regulation of methionine biosynthesis in plants. J. Exp. Bot. 55, 1799-1808.
    • (2004) J. Exp. Bot. , vol.55 , pp. 1799-1808
    • Hesse, H.1    Kreft, O.2    Maimann, S.3    Zeh, M.4    Hoefgen, R.5
  • 27
    • 0344177200 scopus 로고    scopus 로고
    • Global expression profiling of sulfur-starved Arabidopsis by DNA macroarray reveals the role of O-acetyl-l-serine as a general regulator of gene expression in response to sulfur nutrition
    • Hirai, M.Y., Fujiwara, T., Awazuhara, M., Kimura, T., Noji, M., and Saito, K. (2003). Global expression profiling of sulfur-starved Arabidopsis by DNA macroarray reveals the role of O-acetyl-l-serine as a general regulator of gene expression in response to sulfur nutrition. Plant J. 33, 651-663.
    • (2003) Plant J. , vol.33 , pp. 651-663
    • Hirai, M.Y.1    Fujiwara, T.2    Awazuhara, M.3    Kimura, T.4    Noji, M.5    Saito, K.6
  • 28
    • 21844472259 scopus 로고    scopus 로고
    • Elucidation of gene-to-gene and metabolite-to-gene networks in Arabidopsis by integration of metabolomics and transcriptomics
    • Hirai, M.Y., et al. (2005). Elucidation of gene-to-gene and metabolite-to-gene networks in Arabidopsis by integration of metabolomics and transcriptomics. J. Biol. Chem. 280, 25590-25595.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25590-25595
    • Hirai, M.Y.1
  • 29
    • 3042750616 scopus 로고    scopus 로고
    • Integration of transcriptomics and metabolomics for understanding of global responses to nutritional stresses in Arabidopsis thaliana
    • Hirai, M.Y., Yano, M., Goodenowe, D.B., Kanaya, S., Kimura, T., Awazuhara, M., Arita, M., Fujiwara, T., and Saito, K. (2004). Integration of transcriptomics and metabolomics for understanding of global responses to nutritional stresses in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 101, 10205-10210.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10205-10210
    • Hirai, M.Y.1    Yano, M.2    Goodenowe, D.B.3    Kanaya, S.4    Kimura, T.5    Awazuhara, M.6    Arita, M.7    Fujiwara, T.8    Saito, K.9
  • 30
    • 0029438206 scopus 로고
    • The beta-glucuronidase (GUS) reporter gene system. Gene fusions, spectrophotometric, fluorometric, and histochemical detection
    • H. Jones, ed (Totowa, NJ: Humana Press)
    • Hull, G.A., and Devic, M. (1995). The beta-glucuronidase (GUS) reporter gene system. Gene fusions, spectrophotometric, fluorometric, and histochemical detection. In Methods in Molecular Biology, H. Jones, ed (Totowa, NJ: Humana Press), pp. 125-141.
    • (1995) Methods in Molecular Biology , pp. 125-141
    • Hull, G.A.1    Devic, M.2
  • 31
    • 0035233080 scopus 로고    scopus 로고
    • Structure and function of branched chain aminotransferases
    • Hutson, S. (2001). Structure and function of branched chain aminotransferases. Prog. Nucleic Acid Res. Mol. Biol. 70, 175-206.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.70 , pp. 175-206
    • Hutson, S.1
  • 32
    • 0020972316 scopus 로고
    • o-phtaldialdehyde precolumn derivatization and reversed phase high-performance liquid chromatography of polypeptide hydrolysates and physiological fluids
    • Jones, N.J., and Gilligan, J.P. (1983). o-Phtaldialdehyde precolumn derivatization and reversed phase high-performance liquid chromatography of polypeptide hydrolysates and physiological fluids. J. Chromatogr. 266, 471-481.
    • (1983) J. Chromatogr , vol.266 , pp. 471-481
    • Jones, N.J.1    Gilligan, J.P.2
  • 33
    • 85047686305 scopus 로고    scopus 로고
    • Constitutive overexpression of cystathionine gamma-synthase in Arabidopsis leads to accumulation of soluble methionine and S-methylmethionine
    • Kim, J., Lee, M., Chalam, R., Martin, M.N., Leustek, T., and Boerjan, W. (2002). Constitutive overexpression of cystathionine gamma-synthase in Arabidopsis leads to accumulation of soluble methionine and S-methylmethionine. Plant Physiol. 128, 95-107.
    • (2002) Plant Physiol. , vol.128 , pp. 95-107
    • Kim, J.1    Lee, M.2    Chalam, R.3    Martin, M.N.4    Leustek, T.5    Boerjan, W.6
  • 34
    • 0031616480 scopus 로고    scopus 로고
    • Purification of mitochondria from Arabidopsis
    • Klein, M., Binder, S., and Brennicke, A. (1998). Purification of mitochondria from Arabidopsis. Methods Mol. Biol. 82, 49-53.
    • (1998) Methods Mol. Biol. , vol.82 , pp. 49-53
    • Klein, M.1    Binder, S.2    Brennicke, A.3
  • 35
    • 33644875639 scopus 로고    scopus 로고
    • The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed
    • Klein, M., Reichelt, M., Gershenzon, J., and Papenbrock, J. (2006). The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed. FEBS J. 273, 122-136.
    • (2006) FEBS J. , vol.273 , pp. 122-136
    • Klein, M.1    Reichelt, M.2    Gershenzon, J.3    Papenbrock, J.4
  • 36
    • 0037393243 scopus 로고    scopus 로고
    • Insertional inactivation of the methionine S-methyltransferase gene eliminates the S-methylmethionine cycle and increases the methylation ratio
    • Kocsis, M.G., et al. (2003). Insertional inactivation of the methionine S-methyltransferase gene eliminates the S-methylmethionine cycle and increases the methylation ratio. Plant Physiol. 131, 1808-1815.
    • (2003) Plant Physiol. , vol.131 , pp. 1808-1815
    • Kocsis, M.G.1
  • 37
    • 0029818050 scopus 로고    scopus 로고
    • Integration of foreign sequences into the tobacco plastome via polyethylene glycol-mediated protoplast transformation
    • Koop, H.U., Steinmuller, K., Wagner, H., Rossler, C., Eibl, C., and Sacher, L. (1996). Integration of foreign sequences into the tobacco plastome via polyethylene glycol-mediated protoplast transformation. Planta 199, 193-201.
    • (1996) Planta , vol.199 , pp. 193-201
    • Koop, H.U.1    Steinmuller, K.2    Wagner, H.3    Rossler, C.4    Eibl, C.5    Sacher, L.6
  • 38
    • 0033794245 scopus 로고    scopus 로고
    • Identification of a new glucosinolate-rich cell type in Arabidopsis flower stalk
    • Koroleva, O.A., Davies, A., Decken, R., Thorpe, M.R., Tomos, A.D., and Hedrich, R. (2000). Identification of a new glucosinolate-rich cell type in Arabidopsis flower stalk. Plant Physiol. 124, 599-608.
    • (2000) Plant Physiol. , vol.124 , pp. 599-608
    • Koroleva, O.A.1    Davies, A.2    Decken, R.3    Thorpe, M.R.4    Tomos, A.D.5    Hedrich, R.6
  • 39
    • 0035204571 scopus 로고    scopus 로고
    • A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway
    • Kroymann, J., Textor, S., Tokuhisa, J.G., Falk, K.L., Bartram, S., Gershenzon, J., and Mitchell-Olds, T. (2001). A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway. Plant Physiol. 127, 1077-1088.
    • (2001) Plant Physiol. , vol.127 , pp. 1077-1088
    • Kroymann, J.1    Textor, S.2    Tokuhisa, J.G.3    Falk, K.L.4    Bartram, S.5    Gershenzon, J.6    Mitchell-Olds, T.7
  • 41
  • 42
    • 0001334704 scopus 로고
    • The methionine salvage pathway in relation to ethylene and polyamine biosynthesis
    • Miyazaki, J.H., and Yang, S.F. (1987). The methionine salvage pathway in relation to ethylene and polyamine biosynthesis. Physiol. Plant. 69, 366-370.
    • (1987) Physiol. Plant. , vol.69 , pp. 366-370
    • Miyazaki, J.H.1    Yang, S.F.2
  • 43
    • 0037296141 scopus 로고    scopus 로고
    • Transcriptome analysis of sulfur depletion in Arabidopsis thaliana: Interlacing of biosynthetic pathways provides response specificity
    • Nikiforova, V., Freitag, J., Kempa, S., Adamik, M., Hesse, H., and Hoefgen, R. (2003). Transcriptome analysis of sulfur depletion in Arabidopsis thaliana: Interlacing of biosynthetic pathways provides response specificity. Plant J. 33, 633-650.
    • (2003) Plant J. , vol.33 , pp. 633-650
    • Nikiforova, V.1    Freitag, J.2    Kempa, S.3    Adamik, M.4    Hesse, H.5    Hoefgen, R.6
  • 44
    • 0037184035 scopus 로고    scopus 로고
    • Identification of a short highly conserved amino acid sequence as the functional region required for posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis
    • Ominato, K., Akita, H., Suzuki, A., Kijima, F., Yoshino, T., Yoshino, M., Chiba, Y., Onouchi, H., and Naito, S. (2002). Identification of a short highly conserved amino acid sequence as the functional region required for posttranscriptional autoregulation of the cystathionine gamma-synthase gene in Arabidopsis. J. Biol. Chem. 277, 36380-36386.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36380-36386
    • Ominato, K.1    Akita, H.2    Suzuki, A.3    Kijima, F.4    Yoshino, T.5    Yoshino, M.6    Chiba, Y.7    Onouchi, H.8    Naito, S.9
  • 45
    • 10944251699 scopus 로고    scopus 로고
    • Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze the final step in the biosynthesis of the glucosinolate core structure
    • Piotrowski, M., Schemenewitz, A., Lopukhina, A., Müller, A., Janowitz, T., Weiler, E.W., and Oecking, C. (2004). Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze the final step in the biosynthesis of the glucosinolate core structure. J. Biol. Chem. 279, 50717-50725.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50717-50725
    • Piotrowski, M.1    Schemenewitz, A.2    Lopukhina, A.3    Müller, A.4    Janowitz, T.5    Weiler, E.W.6    Oecking, C.7
  • 46
    • 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., and Douce, R. (2004). Methionine metabolism in plants: Chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosylmethionine from the cytosol. J. Biol. Chem. 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
  • 48
    • 1642465435 scopus 로고    scopus 로고
    • An Arabidopsis thaliana T-DNA mutagenized population (GABI-Kat) for flanking sequence tag-based reverse genetics
    • Rosso, M.G., Li, Y., Strizhov, N., Reiss, B., Dekker, K., and Weisshaar, B. (2003). An Arabidopsis thaliana T-DNA mutagenized population (GABI-Kat) for flanking sequence tag-based reverse genetics. Plant Mol. Biol. 53, 247-259.
    • (2003) Plant Mol. Biol. , vol.53 , pp. 247-259
    • Rosso, M.G.1    Li, Y.2    Strizhov, N.3    Reiss, B.4    Dekker, K.5    Weisshaar, B.6
  • 49
    • 0015072056 scopus 로고
    • Fluorescence reaction for amino acids
    • Roth, M. (1971). Fluorescence reaction for amino acids. Anal. Chem. 43, 880-882.
    • (1971) Anal. Chem. , vol.43 , pp. 880-882
    • Roth, M.1
  • 50
    • 0033729605 scopus 로고    scopus 로고
    • Mitochondrial localization of AtOXA1, an Arabidopsis homologue of yeast Oxa1p involved in the insertion and assembly of protein complexes in mitochondrial inner membrane
    • Sakamoto, W., Spielewoy, N., Bonnard, G., Murata, M., and Wintz, H. (2000). Mitochondrial localization of AtOXA1, an Arabidopsis homologue of yeast Oxa1p involved in the insertion and assembly of protein complexes in mitochondrial inner membrane. Plant Cell Physiol. 41, 1157-1163.
    • (2000) Plant Cell Physiol. , vol.41 , pp. 1157-1163
    • Sakamoto, W.1    Spielewoy, N.2    Bonnard, G.3    Murata, M.4    Wintz, H.5
  • 52
    • 0027311063 scopus 로고
    • Evaluation of liquid chromatographic analysis of nutritionally important amino acids in food and physiological samples
    • Sarwar, G., and Bolting, H.G. (1993). Evaluation of liquid chromatographic analysis of nutritionally important amino acids in food and physiological samples. J. Chromatogr. 615, 1-22.
    • (1993) J. Chromatogr. , vol.615 , pp. 1-22
    • Sarwar, G.1    Bolting, H.G.2
  • 53
    • 0029887441 scopus 로고    scopus 로고
    • Coupled enzymatic assay for estimation of branched-chain L-amino acid aminotransferase activity with 2-oxo acid substrates
    • Schadewaldt, P., and Adelmeyer, F. (1996). Coupled enzymatic assay for estimation of branched-chain L-amino acid aminotransferase activity with 2-oxo acid substrates. Anal. Biochem. 238, 65-71.
    • (1996) Anal. Biochem. , vol.238 , pp. 65-71
    • Schadewaldt, P.1    Adelmeyer, F.2
  • 55
    • 17744374145 scopus 로고    scopus 로고
    • The mitochondrial branched-chain aminotransferase (AtBCAT-1) is capable to initiate degradation of leucine, isoleucine and valine in almost all tissues in Arabidopsis thaliana
    • Schuster, J., and Binder, S. (2005). The mitochondrial branched-chain aminotransferase (AtBCAT-1) is capable to initiate degradation of leucine, isoleucine and valine in almost all tissues in Arabidopsis thaliana. Plant Mol. Biol. 57, 241-254.
    • (2005) Plant Mol. Biol. , vol.57 , pp. 241-254
    • Schuster, J.1    Binder, S.2
  • 57
    • 0000035170 scopus 로고
    • Enzymatic formation of alpha-isopropylmalic acid, an intermediate in leucine biosynthesis
    • Strassman, M., and Ceci, L.N. (1963). Enzymatic formation of alpha-isopropylmalic acid, an intermediate in leucine biosynthesis. J. Biol. Chem. 238, 2445-2452.
    • (1963) J. Biol. Chem. , vol.238 , pp. 2445-2452
    • Strassman, M.1    Ceci, L.N.2
  • 58
    • 3042581434 scopus 로고    scopus 로고
    • Functional analysis of the tandem-duplicated P450 genes SPS/BUS/CYP79F1 and CYP79F2 in glucosinolate biosynthesis and plant development by Ds transposition-generated double mutants
    • Tantikanjana, T., Mikkelsen, M.D., Hussain, M., Halkier, B.A., and Sundaresan, V. (2004). Functional analysis of the tandem-duplicated P450 genes SPS/BUS/CYP79F1 and CYP79F2 in glucosinolate biosynthesis and plant development by Ds transposition-generated double mutants. Plant Physiol. 135, 840-848.
    • (2004) Plant Physiol. , vol.135 , pp. 840-848
    • Tantikanjana, T.1    Mikkelsen, M.D.2    Hussain, M.3    Halkier, B.A.4    Sundaresan, V.5
  • 59
    • 1942487253 scopus 로고    scopus 로고
    • Biosynthesis of methionine-derived glucosinolates in Arabidopsis thaliana: Recombinant expression and characterization of methylthioalkylmalate synthase, the condensing enzyme of the chain-elongation cycle
    • Textor, S., Bartram, S., Kroymann, J., Falk, K.L., Hick, A., Pickett, J.A., and Gershenzon, J. (2004). Biosynthesis of methionine-derived glucosinolates in Arabidopsis thaliana: Recombinant expression and characterization of methylthioalkylmalate synthase, the condensing enzyme of the chain-elongation cycle. Planta 218, 1026-1035.
    • (2004) Planta , vol.218 , pp. 1026-1035
    • Textor, S.1    Bartram, S.2    Kroymann, J.3    Falk, K.L.4    Hick, A.5    Pickett, J.A.6    Gershenzon, J.7
  • 61
    • 1042301833 scopus 로고    scopus 로고
    • Interactions between aboveground and belowground induction of glucosinolates in two wild Brassica species
    • van Dam, N.M., Witjes, L., and Svatos, A. (2003). Interactions between aboveground and belowground induction of glucosinolates in two wild Brassica species. New Phytol. 161, 801-810.
    • (2003) New Phytol. , vol.161 , pp. 801-810
    • Van Dam, N.M.1    Witjes, L.2    Svatos, A.3
  • 62
    • 8844278368 scopus 로고    scopus 로고
    • Branched-chain amino acid aminotransferase and methionine formation in Mycobacterium tuberculosis
    • Venos, E.S., Knodel, M.H., Radford, C.L., and Berger, B.J. (2004). Branched-chain amino acid aminotransferase and methionine formation in Mycobacterium tuberculosis. BMC Microbiol. 4, 39.
    • (2004) BMC Microbiol. , vol.4 , pp. 39
    • Venos, E.S.1    Knodel, M.H.2    Radford, C.L.3    Berger, B.J.4
  • 63
    • 0041821504 scopus 로고    scopus 로고
    • Polyamines and plant disease
    • Walters, D.R. (2003). Polyamines and plant disease. Phytochemistry 64, 97-107.
    • (2003) Phytochemistry , vol.64 , pp. 97-107
    • Walters, D.R.1
  • 64
    • 0001467537 scopus 로고
    • Recycling of 5′-methylthioadenosine-ribose carbon atoms into methionine in tomato tissue in relation to ethylene production
    • Wang, S.Y., Adams, D.O., and Lieberman, M. (1982). Recycling of 5′-methylthioadenosine-ribose carbon atoms into methionine in tomato tissue in relation to ethylene production. Plant Physiol. 70, 117-121.
    • (1982) Plant Physiol. , vol.70 , pp. 117-121
    • Wang, S.Y.1    Adams, D.O.2    Lieberman, M.3
  • 65
    • 0036615409 scopus 로고    scopus 로고
    • Glucosinolate research in the Arabidopsis era
    • Wittstock, U., and Halkier, B.A. (2002). Glucosinolate research in the Arabidopsis era. Trends Plant Sci. 7, 263-270.
    • (2002) Trends Plant Sci. , vol.7 , pp. 263-270
    • Wittstock, U.1    Halkier, B.A.2
  • 66
    • 26944468704 scopus 로고    scopus 로고
    • The xylem and phloem transcriptomes from secondary tissues of the Arabidopsis root-hypocotyl
    • Zhao, C., Craig, U.C., Petzold, H.E., Dickerman, A.W., and Beers, E.P. (2005). The xylem and phloem transcriptomes from secondary tissues of the Arabidopsis root-hypocotyl. Plant Physiol. 138, 803-818.
    • (2005) Plant Physiol. , vol.138 , pp. 803-818
    • Zhao, C.1    Craig, U.C.2    Petzold, H.E.3    Dickerman, A.W.4    Beers, E.P.5
  • 67
    • 0037389267 scopus 로고    scopus 로고
    • Increased lysine synthesis coupled with a knockout of its catabolism synergistically boosts lysine content and also transregulates the metabolism of other amino acids in Arabidopsis seeds
    • Zhu, X., and Galili, G. (2003). Increased lysine synthesis coupled with a knockout of its catabolism synergistically boosts lysine content and also transregulates the metabolism of other amino acids in Arabidopsis seeds. Plant Cell 15, 845-853.
    • (2003) Plant Cell , vol.15 , pp. 845-853
    • Zhu, X.1    Galili, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.