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Volumn 129, Issue 1, 2007, Pages 68-78

Branched-chain amino acid metabolism in higher plants

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; CARBOHYDRATES; HYDROPHOBICITY; METABOLISM; PROTEINS; SYNTHESIS (CHEMICAL);

EID: 33845644112     PISSN: 00319317     EISSN: 13993054     Source Type: Journal    
DOI: 10.1111/j.1399-3054.2006.00800.x     Document Type: Conference Paper
Times cited : (127)

References (59)
  • 1
    • 0037466290 scopus 로고    scopus 로고
    • Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa
    • Ahn HJ, Eom SJ, Yoon HJ, Lee BI, Cho H, Suh SW (2003) Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa. J Mol Biol 328: 505-515
    • (2003) J Mol Biol , vol.328 , pp. 505-515
    • Ahn, H.J.1    Eom, S.J.2    Yoon, H.J.3    Lee, B.I.4    Cho, H.5    Suh, S.W.6
  • 2
    • 0000571335 scopus 로고
    • Purification and characterization of 3-methylcrotonyl-coenzyme a carboxylase from higher plant mitochondria
    • Alban C, Baldet P, Axiotis S, Douce R (1993) Purification and characterization of 3-methylcrotonyl-coenzyme A carboxylase from higher plant mitochondria. Plant Physiol 102: 957-965
    • (1993) Plant Physiol , vol.102 , pp. 957-965
    • Alban, C.1    Baldet, P.2    Axiotis, S.3    Douce, R.4
  • 3
    • 0001755965 scopus 로고    scopus 로고
    • 3-Methylcrotonyl-coenzyme a carboxylase is a component of the mitochondrial leucine catabolic pathway in plants
    • Anderson MD, Che P, Song J, Nikolau BJ, Wurtele ES (1998) 3-Methylcrotonyl-coenzyme A carboxylase is a component of the mitochondrial leucine catabolic pathway in plants. Plant Physiol 118: 1127-1138
    • (1998) Plant Physiol , vol.118 , pp. 1127-1138
    • Anderson, M.D.1    Che, P.2    Song, J.3    Nikolau, B.J.4    Wurtele, E.S.5
  • 4
    • 0029958895 scopus 로고    scopus 로고
    • Induction of beta-methylcrotonyl-coenzyme A carboxylase in higher plant cells during carbohydrate starvation: Evidence for a role of MCCase in leucine catabolism
    • Aubert S, Alban C, Bligny R, Douce R (1996) Induction of beta-methylcrotonyl-coenzyme A carboxylase in higher plant cells during carbohydrate starvation: evidence for a role of MCCase in leucine catabolism. FEBS Lett 383: 175-180
    • (1996) FEBS Lett , vol.383 , pp. 175-180
    • Aubert, S.1    Alban, C.2    Bligny, R.3    Douce, R.4
  • 5
    • 0037033115 scopus 로고    scopus 로고
    • Mitochondrial DNA instability mutants of the bifunctional protein Ilv5p have altered organization in mitochondria and are targeted for degradation by Hsp78 and the Pim1p protease
    • Bateman JM, Iacovino M, Perlman PS, Butow RA (2002) Mitochondrial DNA instability mutants of the bifunctional protein Ilv5p have altered organization in mitochondria and are targeted for degradation by Hsp78 and the Pim1p protease. J Biol Chem 277: 47946-47953
    • (2002) J Biol Chem , vol.277 , pp. 47946-47953
    • Bateman, J.M.1    Iacovino, M.2    Perlman, P.S.3    Butow, R.A.4
  • 6
    • 0030996769 scopus 로고    scopus 로고
    • The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 Å resolution
    • Biou V, Dumas R, Cohen-Addad C, Douce R, Job D, Pebay-Peyroula E (1997) The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 Å resolution. EMBO J 16: 3405-3415
    • (1997) EMBO J , vol.16 , pp. 3405-3415
    • Biou, V.1    Dumas, R.2    Cohen-Addad, C.3    Douce, R.4    Job, D.5    Pebay-Peyroula, E.6
  • 8
    • 0035983636 scopus 로고    scopus 로고
    • Metabolic and environmental regulation of 3-methylcrotonyl-coenzyme A carboxylase expression in Arabidopsis
    • Che P, Wurtele ES, Nikolau BJ (2002) Metabolic and environmental regulation of 3-methylcrotonyl-coenzyme A carboxylase expression in Arabidopsis. Plant Physiol 129: 625-637
    • (2002) Plant Physiol , vol.129 , pp. 625-637
    • Che, P.1    Wurtele, E.S.2    Nikolau, B.J.3
  • 9
    • 30044443050 scopus 로고    scopus 로고
    • Jasmonate-inducible plant enzymes degrade essential amino acids in the herbivore midgut
    • Chen H, Wilkerson CG, Kuchar JA, Phinney BS, Howe GA (2005) Jasmonate-inducible plant enzymes degrade essential amino acids in the herbivore midgut. Proc Natl Acad Sci USA 102: 19237-19242
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 19237-19242
    • Chen, H.1    Wilkerson, C.G.2    Kuchar, J.A.3    Phinney, B.S.4    Howe, G.A.5
  • 10
    • 0000123897 scopus 로고
    • Biosynthesis of mustard oil glucosides. Iv. The administration of methionine-C14 and related compounds to horseradish
    • Chisholm MD, Wetter LR (1964) Biosynthesis of mustard oil glucosides. Iv. The administration of methionine-C14 and related compounds to horseradish. Can J Biochem 42: 1033-1040
    • (1964) Can J Biochem , vol.42 , pp. 1033-1040
    • Chisholm, M.D.1    Wetter, L.R.2
  • 11
    • 0039175818 scopus 로고    scopus 로고
    • In plants a putative isovaleryl-CoA-dehydrogenase is located in mitochondria
    • Däschner K, Thalheim C, Guha C, Brennicke A, Binder S (1999) In plants a putative isovaleryl-CoA-dehydrogenase is located in mitochondria. Plant Mol Biol 39: 1275-1282
    • (1999) Plant Mol Biol , vol.39 , pp. 1275-1282
    • Däschner, K.1    Thalheim, C.2    Guha, C.3    Brennicke, A.4    Binder, S.5
  • 12
    • 0034979962 scopus 로고    scopus 로고
    • The mitochondrial isovaleryl-coenzyme a dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism
    • Däschner K, Couée I, 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    Couée, I.2    Binder, S.3
  • 13
    • 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, 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
  • 14
    • 0027525175 scopus 로고
    • Branched-chain-amino-acid biosynthesis in plants: Molecular cloning and characterization of the gene encoding acetohydroxy acid isomeroreductase (ketol-acid reductoisomerase) from Arabidopsis thaliana (thale cress)
    • Dumas R, Curien G, DeRose RT, Douce R (1993) Branched-chain-amino-acid biosynthesis in plants: molecular cloning and characterization of the gene encoding acetohydroxy acid isomeroreductase (ketol-acid reductoisomerase) from Arabidopsis thaliana (thale cress). Biochem J 294: 821-828
    • (1993) Biochem J , vol.294 , pp. 821-828
    • Dumas, R.1    Curien, G.2    DeRose, R.T.3    Douce, R.4
  • 15
    • 0034868638 scopus 로고    scopus 로고
    • Enzymology, structure, and dynamics of acetohydroxy acid isomeroreductase
    • Dumas R, Biou V, Halgand F, Douce R, Duggleby RG (2001) Enzymology, structure, and dynamics of acetohydroxy acid isomeroreductase. Acc Chem Res 34: 399-408
    • (2001) Acc Chem Res , vol.34 , pp. 399-408
    • Dumas, R.1    Biou, V.2    Halgand, F.3    Douce, R.4    Duggleby, R.G.5
  • 16
    • 0026813256 scopus 로고
    • Cloning of a cDNA for rape chloroplast 3-isopropylmalate dehydrogenase by genetic complementation in yeast
    • Ellerstrom M, Josefsson LG, Rask L, Ronne H (1992) Cloning of a cDNA for rape chloroplast 3-isopropylmalate dehydrogenase by genetic complementation in yeast. Plant Mol Biol 18: 557-566
    • (1992) Plant Mol Biol , vol.18 , pp. 557-566
    • Ellerstrom, M.1    Josefsson, L.G.2    Rask, L.3    Ronne, H.4
  • 17
    • 0035088030 scopus 로고    scopus 로고
    • Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria
    • Faivre-Nitschke SE, Couée I, Vermel M, Grienenberger JM, Gualberto JM (2001) Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria. Eur J Biochem 268: 1332-1339
    • (2001) Eur J Biochem , vol.268 , pp. 1332-1339
    • Faivre-Nitschke, S.E.1    Couée, I.2    Vermel, M.3    Grienenberger, J.M.4    Gualberto, J.M.5
  • 19
    • 0034102077 scopus 로고    scopus 로고
    • Isolation and characterization of cDNA clones for the E1β and E2 subunits of the branched-chain alpha-ketoacid dehydrogenase complex in Arabidopsis
    • Fujiki Y, Sato T, Ito M, Watanabe A (2000) Isolation and characterization of cDNA clones for the E1β and E2 subunits of the branched-chain alpha-ketoacid dehydrogenase complex in Arabidopsis. J Biol Chem 275: 6007-6013
    • (2000) J Biol Chem , vol.275 , pp. 6007-6013
    • Fujiki, Y.1    Sato, T.2    Ito, M.3    Watanabe, A.4
  • 20
    • 0001001724 scopus 로고
    • Peroxisomal degradation of branched-chain 2-oxo acids
    • Gerbling H, Gerhardt B (1989) Peroxisomal degradation of branched-chain 2-oxo acids. Plant Physiol 91: 1387-1392
    • (1989) Plant Physiol , vol.91 , pp. 1387-1392
    • Gerbling, H.1    Gerhardt, B.2
  • 21
    • 14244250066 scopus 로고    scopus 로고
    • Convergent evolution of a 2-methylbutyryl-CoA dehydrogenase from isovaleryl-CoA dehydrogenase in Solanum tuberosum
    • Goetzman ES, Mohsen AW, Prasad K, Vockley J (2005) Convergent evolution of a 2-methylbutyryl-CoA dehydrogenase from isovaleryl-CoA dehydrogenase in Solanum tuberosum. J Biol Chem 280: 4873-4879
    • (2005) J Biol Chem , vol.280 , pp. 4873-4879
    • Goetzman, E.S.1    Mohsen, A.W.2    Prasad, K.3    Vockley, J.4
  • 22
    • 0034659867 scopus 로고    scopus 로고
    • The methionine chain elongation pathway in the biosynthesis of glucosinolates in Eruca sativa (Brassicaceae)
    • Graser G, Schneider B, Oldham NJ, 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
  • 23
    • 32544436982 scopus 로고    scopus 로고
    • Glucosinolate metabolism and its control
    • Grubb CD, 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
  • 24
    • 0027715164 scopus 로고
    • Leucine synthesis in spinach chloroplasts: Partial characterization of 2-isopropylmalate synthase
    • Hagelstein P, Schultz G (1993) Leucine synthesis in spinach chloroplasts: partial characterization of 2-isopropylmalate synthase. Biol Chem 374: 1105-1108
    • (1993) Biol Chem , vol.374 , pp. 1105-1108
    • Hagelstein, P.1    Schultz, G.2
  • 25
    • 0030939682 scopus 로고    scopus 로고
    • Leucine synthesis in chloroplasts: Leucine/isoleucine aminotransferase and valine aminotransferase are different enzymes in spinach chloroplasts
    • Hagelstein P, Sieve B, Klein M, Jans H, Schultz G (1997) Leucine synthesis in chloroplasts: leucine/isoleucine aminotransferase and valine aminotransferase are different enzymes in spinach chloroplasts. J Plant Phys 150: 23-30
    • (1997) J Plant Phys , vol.150 , pp. 23-30
    • Hagelstein, P.1    Sieve, B.2    Klein, M.3    Jans, H.4    Schultz, G.5
  • 26
    • 0037137213 scopus 로고    scopus 로고
    • Biochemical and mass spectrometric evidence for quaternary structure modifications of plant threonine deaminase induced by isoleucine
    • Halgand F, Wessel PM, Laprevote O, Dumas R (2002) Biochemical and mass spectrometric evidence for quaternary structure modifications of plant threonine deaminase induced by isoleucine. Biochemistry 41: 13767-13773
    • (2002) Biochemistry , vol.41 , pp. 13767-13773
    • Halgand, F.1    Wessel, P.M.2    Laprevote, O.3    Dumas, R.4
  • 27
    • 33745218882 scopus 로고    scopus 로고
    • Biology and biochemistry of glucosinolates
    • Halkier BA, Gershenzon J (2006) Biology and biochemistry of glucosinolates. Annu Rev Plant Biol 57: 309-333
    • (2006) Annu Rev Plant Biol , vol.57 , pp. 309-333
    • Halkier, B.A.1    Gershenzon, J.2
  • 28
    • 0033617449 scopus 로고    scopus 로고
    • A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes
    • Hayashi H, De Bellis L, Ciurli A, Kondo M, Hayashi M, Nishimura M (1999) A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. J Biol Chem 274: 12715-12721
    • (1999) J Biol Chem , vol.274 , pp. 12715-12721
    • Hayashi, H.1    De Bellis, L.2    Ciurli, A.3    Kondo, M.4    Hayashi, M.5    Nishimura, M.6
  • 29
    • 0033167288 scopus 로고    scopus 로고
    • Cloning and functional expression of the small subunit of acetolactate synthase from Nicotiana plumbaginifolia
    • Hershey HP, Schwartz LJ, Gale JP, Abell LM (1999) Cloning and functional expression of the small subunit of acetolactate synthase from Nicotiana plumbaginifolia. Plant Mol Biol 40: 795-806
    • (1999) Plant Mol Biol , vol.40 , pp. 795-806
    • Hershey, H.P.1    Schwartz, L.J.2    Gale, J.P.3    Abell, L.M.4
  • 30
    • 33644688603 scopus 로고    scopus 로고
    • The critical role of Arabidopsis electron-transfer flavoprotein: ubiquinone oxidoreductase during dark-induced starvation
    • Ishizaki K, Larson TR, Schauer N, Fernie AR, Graham IA, Leaver CJ (2005) The critical role of Arabidopsis electron-transfer flavoprotein:ubiquinone oxidoreductase during dark-induced starvation. Plant Cell 17: 2587-2600
    • (2005) Plant Cell , vol.17 , pp. 2587-2600
    • Ishizaki, K.1    Larson, T.R.2    Schauer, N.3    Fernie, A.R.4    Graham, I.A.5    Leaver, C.J.6
  • 31
    • 0027475392 scopus 로고
    • Cloning and expression analysis of beta-isopropylmalate dehydrogenase from potato
    • Jackson SD, Sonnewald U, Willmitzer L (1993) Cloning and expression analysis of beta-isopropylmalate dehydrogenase from potato. Mol Gen Genet 236: 309-314
    • (1993) Mol Gen Genet , vol.236 , pp. 309-314
    • Jackson, S.D.1    Sonnewald, U.2    Willmitzer, L.3
  • 32
    • 0036896517 scopus 로고    scopus 로고
    • Isolation and expression analysis of the isopropylmalate synthase gene family of Arabidopsis thaliana
    • Junk DJ, Mourad GS (2002) Isolation and expression analysis of the isopropylmalate synthase gene family of Arabidopsis thaliana. J Exp Bot 53: 2453-2454
    • (2002) J Exp Bot , vol.53 , pp. 2453-2454
    • Junk, D.J.1    Mourad, G.S.2
  • 33
    • 0038271823 scopus 로고    scopus 로고
    • Different elongation pathways in the biosynthesis of acyl groups of trichome exudate sugar esters from various solanaceous plants
    • Kroumova AB, Wagner GJ (2003) Different elongation pathways in the biosynthesis of acyl groups of trichome exudate sugar esters from various solanaceous plants. Planta 216: 1013-1021
    • (2003) Planta , vol.216 , pp. 1013-1021
    • Kroumova, A.B.1    Wagner, G.J.2
  • 34
    • 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 JG, Falk KL, Bartram S, Gershenzon J, 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
  • 35
    • 0344198474 scopus 로고    scopus 로고
    • Evolutionary dynamics of an Arabidopsis insect resistance quantitative trait locus
    • Kroymann J, Donnerhacke S, Schnabelrauch D, Mitchell-Olds T (2003) Evolutionary dynamics of an Arabidopsis insect resistance quantitative trait locus. Proc Natl Acad Sci USA 100(Suppl 2): 14587-14592
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.SUPPL. 2 , pp. 14587-14592
    • Kroymann, J.1    Donnerhacke, S.2    Schnabelrauch, D.3    Mitchell-Olds, T.4
  • 36
    • 3342962408 scopus 로고    scopus 로고
    • An Arabidopsis mutant disrupted in valine catabolism is also compromised in peroxisomal fatty acid beta-oxidation
    • Lange PR, Eastmond PJ, Madagan K, Graham IA (2004) An Arabidopsis mutant disrupted in valine catabolism is also compromised in peroxisomal fatty acid beta-oxidation. FEBS Lett 571: 147-153
    • (2004) FEBS Lett , vol.571 , pp. 147-153
    • Lange, P.R.1    Eastmond, P.J.2    Madagan, K.3    Graham, I.A.4
  • 37
    • 0035849510 scopus 로고    scopus 로고
    • Identification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit
    • Lee YT, Duggleby RG (2001) Identification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit. Biochemistry 40: 6836-6844
    • (2001) Biochemistry , vol.40 , pp. 6836-6844
    • Lee, Y.T.1    Duggleby, R.G.2
  • 42
    • 0033150518 scopus 로고    scopus 로고
    • Cloning and characterization of the dihydrolipoamide S-acetyltransferase subunit of the plastid pyruvate dehydrogenase complex (E2) from Arabidopsis
    • Mooney BP, Miernyk JA, Randall DD (1999) Cloning and characterization of the dihydrolipoamide S-acetyltransferase subunit of the plastid pyruvate dehydrogenase complex (E2) from Arabidopsis. Plant Physiol 120: 443-452
    • (1999) Plant Physiol , vol.120 , pp. 443-452
    • Mooney, B.P.1    Miernyk, J.A.2    Randall, D.D.3
  • 44
    • 0034721793 scopus 로고    scopus 로고
    • Cloning of a gene for an acyl-CoA dehydrogenase from Pisum sativum L. and purification and characterization of its product as an isovaleryl-CoA dehydrogenase
    • Reinard T, Janke V, Willard J, Buck F, Jacobsen HJ, Vockley J (2000) Cloning of a gene for an acyl-CoA dehydrogenase from Pisum sativum L. and purification and characterization of its product as an isovaleryl-CoA dehydrogenase. J Biol Chem 275: 33738-33743
    • (2000) J Biol Chem , vol.275 , pp. 33738-33743
    • Reinard, T.1    Janke, V.2    Willard, J.3    Buck, F.4    Jacobsen, H.J.5    Vockley, J.6
  • 45
    • 16544384619 scopus 로고    scopus 로고
    • AraPerox. A database of putative Arabidopsis proteins from plant peroxisomes
    • Reumann S, Ma C, Lemke S, Babujee L (2004) AraPerox. A database of putative Arabidopsis proteins from plant peroxisomes. Plant Physiol 136: 2587-2608
    • (2004) Plant Physiol , vol.136 , pp. 2587-2608
    • Reumann, S.1    Ma, C.2    Lemke, S.3    Babujee, L.4
  • 46
    • 17744374145 scopus 로고    scopus 로고
    • The mitochondrial branchedchain aminotransferase (AtBCAT-1) is capable to initiate degradation of leucine, isoleucine and valine in almost all tissues in Arabidopsis thaliana
    • Schuster J, Binder S (2005) The mitochondrial branchedchain 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
  • 47
    • 0000959598 scopus 로고    scopus 로고
    • Biosynthesis of valine, leucine and isoleucine
    • Singh BK (ed). Marcel Dekker, New York
    • Singh BK (1999) Biosynthesis of valine, leucine and isoleucine. In: Singh BK (ed) Plant Amino Acids: Biochemistry and Biotechnology. Marcel Dekker, New York, pp 227-247
    • (1999) Plant Amino Acids: Biochemistry and Biotechnology , pp. 227-247
    • Singh, B.K.1
  • 48
    • 0028794939 scopus 로고
    • Biosynthesis of branched chain amino acids: From test tube to field
    • Singh BK, Shaner DL (1995) Biosynthesis of branched chain amino acids: from test tube to field. Plant Cell 7: 935-944
    • (1995) Plant Cell , vol.7 , pp. 935-944
    • Singh, B.K.1    Shaner, D.L.2
  • 49
    • 0028365515 scopus 로고
    • Molecular cloning and characterization of the cDNA coding for the biotin-containing subunit of 3-methylcrotonoyl-CoA carboxylase: Identification of the biotin carboxylase and biotin-carrier domains
    • Song J, Wurtele ES, Nikolau BJ (1994) Molecular cloning and characterization of the cDNA coding for the biotin-containing subunit of 3-methylcrotonoyl-CoA carboxylase: identification of the biotin carboxylase and biotin-carrier domains. Proc Natl Acad Sci USA 91: 5779-5783
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5779-5783
    • Song, J.1    Wurtele, E.S.2    Nikolau, B.J.3
  • 50
    • 33645244088 scopus 로고    scopus 로고
    • Herbicidal inhibitors of amino acid biosynthesis and herbicide-tolerant crops
    • Tan S, Evans R, Singh B (2006) Herbicidal inhibitors of amino acid biosynthesis and herbicide-tolerant crops. Amino Acids 30: 195-204
    • (2006) Amino Acids , vol.30 , pp. 195-204
    • Tan, S.1    Evans, R.2    Singh, B.3
  • 51
    • 1342287231 scopus 로고    scopus 로고
    • Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis
    • Taylor NL, Heazlewood JL, Day DA, Millar AH (2004) Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis. Plant Physiol 134: 838-848
    • (2004) Plant Physiol , vol.134 , pp. 838-848
    • Taylor, N.L.1    Heazlewood, J.L.2    Day, D.A.3    Millar, A.H.4
  • 52
    • 0034710671 scopus 로고    scopus 로고
    • A deeply knotted protein structure and how it might fold
    • Taylor WR (2000) A deeply knotted protein structure and how it might fold. Nature 406: 916-919
    • (2000) Nature , vol.406 , pp. 916-919
    • Taylor, W.R.1
  • 53
    • 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 KL, Hick A, Pickett JA, 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
  • 54
    • 0034111648 scopus 로고    scopus 로고
    • Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose
    • Thomazeau K, Dumas R, Halgand F, Forest E, Douce R, Biou V (2000) Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose. Acta Crystallogr D Biol Crystallogr 56: 389-397
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 389-397
    • Thomazeau, K.1    Dumas, R.2    Halgand, F.3    Forest, E.4    Douce, R.5    Biou, V.6
  • 55
    • 28844506786 scopus 로고    scopus 로고
    • The crystal structure of a bacterial class II ketol-acid reductoisomerase: Domain conservation and evolution
    • Tyagi R, Duquerroy S, Navaza J, Guddat LW, Duggleby RG (2005) The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution. Protein Sci 14: 3089-3100
    • (2005) Protein Sci , vol.14 , pp. 3089-3100
    • Tyagi, R.1    Duquerroy, S.2    Navaza, J.3    Guddat, L.W.4    Duggleby, R.G.5
  • 58
    • 0001159978 scopus 로고    scopus 로고
    • Inhibitors of valine, leucine and isoleucine biosynthesis
    • Singh BK (ed), Marcel Dekker, New York
    • Wittenbach VA, Abell LM (1999) Inhibitors of valine, leucine and isoleucine biosynthesis. In: Singh BK (ed), Plant Amino Acids: Biochemistry and Biotechnology. Marcel Dekker, New York, pp 385-416
    • (1999) Plant Amino Acids: Biochemistry and Biotechnology , pp. 385-416
    • Wittenbach, V.A.1    Abell, L.M.2
  • 59
    • 0036615409 scopus 로고    scopus 로고
    • Glucosinolate research in the Arabidopsis era
    • Wittstock U, Halkier BA (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.