메뉴 건너뛰기




Volumn 39, Issue 4, 2010, Pages 979-989

High-lysine maize: The key discoveries that have made it possible

Author keywords

Aspartic acid; Corn; Isoleucine; Lysine; Maize; Methionine; Threonine

Indexed keywords

AMINO ACID; ASPARTIC ACID; LYSINE; METHIONINE; SACCHAROPINE; THREONINE; UNCLASSIFIED DRUG;

EID: 78649983204     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-010-0576-5     Document Type: Review
Times cited : (48)

References (89)
  • 1
    • 0001306027 scopus 로고
    • Threonine-sensitive aspartate kinase and homoserine dehydrogenase from Pisum sativum
    • Aarnes H, Rognes SE (1974) Threonine-sensitive aspartate kinase and homoserine dehydrogenase from Pisum sativum. Phytochemistry 13:2717-2724
    • (1974) Phytochemistry , vol.13 , pp. 2717-2724
    • Aarnes, H.1    Rognes, S.E.2
  • 2
    • 67749095294 scopus 로고    scopus 로고
    • Nitrogen use efficiency. 3. Nitrogen fixation: Genes and costs
    • Andrews M, Lea PJ, Raven JA, Azevedo RA (2009) Nitrogen use efficiency. 3. Nitrogen fixation: genes and costs. Ann Appl Biol 155:1-13
    • (2009) Ann Appl Biol , vol.155 , pp. 1-13
    • Andrews, M.1    Lea, P.J.2    Raven, J.A.3    Azevedo, R.A.4
  • 3
    • 0001679489 scopus 로고
    • Amino-acid composition of vascular sap of maize ear peduncle
    • Arruda P, Silva WJ (1979) Amino-acid composition of vascular sap of maize ear peduncle. Phytochemistry 18:409-410
    • (1979) Phytochemistry , vol.18 , pp. 409-410
    • Arruda, P.1    Silva, W.J.2
  • 4
    • 0000082872 scopus 로고
    • Lysine-ketoglutarate reductase-activity in maize-its possible role in lysine metabolism of developing endosperm
    • Arruda P, Silva WJ (1983) Lysine-ketoglutarate reductase-activity in maize-its possible role in lysine metabolism of developing endosperm. Phytochemistry 22:2687-2689
    • (1983) Phytochemistry , vol.22 , pp. 2687-2689
    • Arruda, P.1    Silva, W.J.2
  • 5
    • 0001247558 scopus 로고
    • Lysine-ketoglutarate reductaseactivity in developing maize endosperm
    • Arruda P, Sodek L, Silva WJ (1982) Lysine-ketoglutarate reductaseactivity in developing maize endosperm. Plant Physiol 69:988-989
    • (1982) Plant Physiol , vol.69 , pp. 988-989
    • Arruda, P.1    Sodek, L.2    Silva, W.J.3
  • 6
    • 0005690391 scopus 로고
    • Regulation of aspartate kinase isoenzymes in barley mutants resistant to lysine plus threonine-construction and analysis of combinations of the LT1A, LT1B, and LT2 mutant-genes
    • Arruda P, Bright SWJ, Kueh JSH, Lea PJ, Rognes SE (1984) Regulation of aspartate kinase isoenzymes in barley mutants resistant to lysine plus threonine-construction and analysis of combinations of the LT1A, LT1B, and LT2 mutant-genes. Plant Physiol 76:442-446
    • (1984) Plant Physiol , vol.76 , pp. 442-446
    • Arruda, P.1    Swj, B.2    Jsh, K.3    Lea, P.J.4    Rognes, S.E.5
  • 8
    • 0035989811 scopus 로고    scopus 로고
    • Analysis of the aspartic acid metabolic pathway using mutant genes
    • Azevedo RA (2002) Analysis of the aspartic acid metabolic pathway using mutant genes. Amino Acids 22:217-230
    • (2002) Amino Acids , vol.22 , pp. 217-230
    • Azevedo, R.A.1
  • 9
    • 0035094676 scopus 로고    scopus 로고
    • Lysine metabolism in higher plants
    • Azevedo RA, Lea PJ (2001) Lysine metabolism in higher plants. Amino Acids 20:261-279
    • (2001) Amino Acids , vol.20 , pp. 261-279
    • Azevedo, R.A.1    Lea, P.J.2
  • 10
    • 0002599959 scopus 로고
    • Biochemical genetics of the interaction of the lysine plus threonine resistant mutant Ltr*1 with opaque-2 maize mutant
    • Azevedo RA, Arana JL, Arruda P (1990) Biochemical genetics of the interaction of the lysine plus threonine resistant mutant Ltr*1 with opaque-2 maize mutant. Plant Sci 70:81-90
    • (1990) Plant Sci , vol.70 , pp. 81-90
    • Azevedo, R.A.1    Arana, J.L.2    Arruda, P.3
  • 11
    • 0001136267 scopus 로고
    • Aspects of aspartate kinase regulation in maize: Co-purification of aspartate kinase and homoserine dehydrogenase sensitive to threonine
    • Azevedo RA, Smith RJ, Lea PJ (1992) Aspects of aspartate kinase regulation in maize: co-purification of aspartate kinase and homoserine dehydrogenase sensitive to threonine. Phytochemistry 31:3731-3734
    • (1992) Phytochemistry , vol.31 , pp. 3731-3734
    • Azevedo, R.A.1    Smith, R.J.2    Lea, P.J.3
  • 12
    • 0031260404 scopus 로고    scopus 로고
    • The biosynthesis and metabolism of the aspartate derived amino acids in higher plants
    • Azevedo RA, Arruda P, Turner WL, Lea PJ (1997) The biosynthesis and metabolism of the aspartate derived amino acids in higher plants. Phytochemistry 46:395-419
    • (1997) Phytochemistry , vol.46 , pp. 395-419
    • Azevedo, R.A.1    Arruda, P.2    Turner, W.L.3    Lea, P.J.4
  • 16
    • 33645237056 scopus 로고    scopus 로고
    • The aspartic acid metabolic pathway, an exciting and essential pathway in plants
    • Azevedo RA, Lancien M, Lea PJ (2006) The aspartic acid metabolic pathway, an exciting and essential pathway in plants. Amino Acids 30:143-162
    • (2006) Amino Acids , vol.30 , pp. 143-162
    • Azevedo, R.A.1    Lancien, M.2    Lea, P.J.3
  • 19
    • 0019944566 scopus 로고
    • Two genes for threonine accumulation in barley seeds
    • Bright SWJ, Kueh JSH, Franklin J, Rognes SE, Miflin BJ (1982) Two genes for threonine accumulation in barley seeds. Nature 299:278-279
    • (1982) Nature , vol.299 , pp. 278-279
    • Swj, B.1    Jsh, K.2    Franklin, J.3    Rognes, S.E.4    Miflin, B.J.5
  • 20
    • 0000690359 scopus 로고
    • Partial purification and characterization of lysine-ketoglutarate reductase activity in normal and opaque-2 maize endosperms
    • Brochetto-Braga MR, Leite A, Arruda P (1992) Partial purification and characterization of lysine-ketoglutarate reductase activity in normal and opaque-2 maize endosperms. Plant Physiol 98:1139-1147
    • (1992) Plant Physiol , vol.98 , pp. 1139-1147
    • Brochetto-Braga, M.R.1    Leite, A.2    Arruda, P.3
  • 22
    • 0014215410 scopus 로고
    • Ribonuclease activity in the developing seeds of normal and opaque-2 maize
    • Dalby A, Davies IAI (1967) Ribonuclease activity in the developing seeds of normal and opaque-2 maize. Science 155:1573-1575
    • (1967) Science , vol.155 , pp. 1573-1575
    • Dalby, A.1    Iai, D.2
  • 23
    • 0014559754 scopus 로고
    • Familial hyperlysinemia with lysine-ketoglutarate reductase insufficiency
    • Dancis J, Hutzler J, Cox RP, Woody NC (1969) Familial hyperlysinemia with lysine-ketoglutarate reductase insufficiency. J Clin Invest 48:1447-1452
    • (1969) J Clin Invest , vol.48 , pp. 1447-1452
    • Dancis, J.1    Hutzler, J.2    Cox, R.P.3    Woody, N.C.4
  • 24
    • 0000587863 scopus 로고
    • Proposed nomenclature for the alcohol-soluble proteins (zeins) of maize (Zea mays l.)
    • Esen A (1987) Proposed nomenclature for the alcohol-soluble proteins (zeins) of maize (Zea mays l.). J Cereal Sci 5:117-128
    • (1987) J Cereal Sci , vol.5 , pp. 117-128
    • Esen, A.1
  • 27
    • 0001524023 scopus 로고
    • Two feedback-insensitive enzymes of the aspartate pathway in Nicotiana sylvestris
    • Frankard V, Ghislain M, Jacobs M (1992) Two feedback-insensitive enzymes of the aspartate pathway in Nicotiana sylvestris. Plant Physiol 99:1285-1293
    • (1992) Plant Physiol , vol.99 , pp. 1285-1293
    • Frankard, V.1    Ghislain, M.2    Jacobs, M.3
  • 28
    • 36849093996 scopus 로고    scopus 로고
    • Modifying lysine biosynthesis and catabolism in corn with a single bifunctional expression/silencing transgene cassette
    • Frizzi A, Huang S, Gilbertson LA, Armstrong TA, Luethy MH, Malvar TM (2008) Modifying lysine biosynthesis and catabolism in corn with a single bifunctional expression/silencing transgene cassette. Plant Biotech J 6:13-21
    • (2008) Plant Biotech J , vol.6 , pp. 13-21
    • Frizzi, A.1    Huang, S.2    Gilbertson, L.A.3    Armstrong, T.A.4    Luethy, M.H.5    Malvar, T.M.6
  • 29
    • 0037004052 scopus 로고    scopus 로고
    • New insights into the regulation and functional significance of lysine metabolism in plants
    • Galili G (2002) New insights into the regulation and functional significance of lysine metabolism in plants. Annu Rev Plant Biol 53:27-43
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 27-43
    • Galili, G.1
  • 30
    • 26844445269 scopus 로고    scopus 로고
    • Improving the levels of essential amino acids and sulfur metabolites in plants
    • Galili G, Amir R, Roefgen R, Hesse H (2005) Improving the levels of essential amino acids and sulfur metabolites in plants. Biol Chem 386:817-831
    • (2005) Biol Chem , vol.386 , pp. 817-831
    • Galili, G.1    Amir, R.2    Roefgen, R.3    Hesse, H.4
  • 31
    • 0030758692 scopus 로고    scopus 로고
    • The enzymology of lysine catabolism in rice seeds-isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase saccharopine dehydrogenase bifunctional polypeptide
    • Gaziola SA, Teixeira CMG, Lugli J, Sodek L, Azevedo RA (1997) The enzymology of lysine catabolism in rice seeds-isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase saccharopine dehydrogenase bifunctional polypeptide. Eur J Biochem 247:364-371
    • (1997) Eur J Biochem , vol.247 , pp. 364-371
    • Gaziola, S.A.1    Cmg, T.2    Lugli, J.3    Sodek, L.4    Azevedo, R.A.5
  • 32
    • 0032915561 scopus 로고    scopus 로고
    • Quality protein maize: A biochemical study of enzymes involved in lysine metabolism
    • Gaziola SA, Alessi ES, Guimarães PEO, Damerval C, Azevedo RA (1999) Quality protein maize: a biochemical study of enzymes involved in lysine metabolism. J Agric Food Chem 47:1268-1275
    • (1999) J Agric Food Chem , vol.47 , pp. 1268-1275
    • Gaziola, S.A.1    Alessi, E.S.2    Peo, G.3    Damerval, C.4    Azevedo, R.A.5
  • 33
    • 15244339647 scopus 로고    scopus 로고
    • Molecular genetic approaches to developing quality protein maize
    • Gibbon BC, Larkins BA (2005) Molecular genetic approaches to developing quality protein maize. Trends Genet 21:227-233
    • (2005) Trends Genet , vol.21 , pp. 227-233
    • Gibbon, B.C.1    Larkins, B.A.2
  • 34
    • 0346103683 scopus 로고    scopus 로고
    • Altered starch structure is associated with endosperm modification in Quality Protein Maize
    • Gibbon BC, Wang XL, Larkins BA (2003) Altered starch structure is associated with endosperm modification in Quality Protein Maize. Proc Natl Acad Sci USA 100:15329-15334
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15329-15334
    • Gibbon, B.C.1    Wang, X.L.2    Larkins, B.A.3
  • 35
    • 0030042427 scopus 로고    scopus 로고
    • Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize
    • Gonçalves-Butruille M, Szajner P, Torigoi E, Leite A, Arruda P (1996) Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize. Plant Physiol 110:765-771
    • (1996) Plant Physiol , vol.110 , pp. 765-771
    • Gonçalves-Butruille, M.1    Szajner, P.2    Torigoi, E.3    Leite, A.4    Arruda, P.5
  • 36
    • 0001501960 scopus 로고
    • Potential selection system for mutants with increased lysine, threonine, and methionine in cereal crops
    • Green CE, Phillips RL (1974) Potential selection system for mutants with increased lysine, threonine, and methionine in cereal crops. Crop Sci 14:827-830
    • (1974) Crop Sci , vol.14 , pp. 827-830
    • Green, C.E.1    Phillips, R.L.2
  • 37
    • 54949105026 scopus 로고    scopus 로고
    • Phenotypic characterization of quality protein maize endosperm modification and amino acid contents in a segregating recombinant inbred population
    • Gutierrez-Rojas A, Paul-Scott M, Leyva OR, Menz M, Betrán J (2008) Phenotypic characterization of quality protein maize endosperm modification and amino acid contents in a segregating recombinant inbred population. Crop Sci 48:1714-1722
    • (2008) Crop Sci , vol.48 , pp. 1714-1722
    • Gutierrez-Rojas, A.1    Paul-Scott, M.2    Leyva, O.R.3    Menz, M.4    Betrán, J.5
  • 38
    • 34548125412 scopus 로고    scopus 로고
    • Lysine enhances methionine content by modulating the expression of S-adenosylmethionine synthase
    • Hacham Y, Song L, Schuster G, Amir R (2007) Lysine enhances methionine content by modulating the expression of S-adenosylmethionine synthase. Plant J 51:850-861
    • (2007) Plant J , vol.51 , pp. 850-861
    • Hacham, Y.1    Song, L.2    Schuster, G.3    Amir, R.4
  • 39
    • 41849149314 scopus 로고    scopus 로고
    • Overexpression of mutated forms of aspartate kinase and cystathionine gammasynthase in tobacco leaves resulted in the high accumulation of methionine and threonine
    • Hacham Y, Matityahu I, Schuster G, Amir R (2008) Overexpression of mutated forms of aspartate kinase and cystathionine gammasynthase in tobacco leaves resulted in the high accumulation of methionine and threonine. Plant J 54:260-271
    • (2008) Plant J , vol.54 , pp. 260-271
    • Hacham, Y.1    Matityahu, I.2    Schuster, G.3    Amir, R.4
  • 40
    • 0028039390 scopus 로고
    • Selection of Arabidospis thaliana (L.) Heynh Mutants resistant to aspartate-derived amino acids and analogues
    • Heremans B, Jacobs M (1994) Selection of Arabidospis thaliana (L.) Heynh. Mutants resistant to aspartate-derived amino acids and analogues. Plant Sci 101:151-162
    • (1994) Plant Sci , vol.101 , pp. 151-162
    • Heremans, B.1    Jacobs, M.2
  • 41
    • 0020069497 scopus 로고
    • Inheritance and expression of lysine plus threonine resistance selected in maize tissue culture
    • Hibberd KA, Green CE (1982) Inheritance and expression of lysine plus threonine resistance selected in maize tissue culture. Proc Natl Acad Sci USA 79:559-563
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 559-563
    • Hibberd, K.A.1    Green, C.E.2
  • 46
    • 33745685913 scopus 로고    scopus 로고
    • High lysine and high tryptophan transgenic maize resulting from the reduction of both 19- and 22-kD a-zeins
    • Huang S, Frizzi A, Florida CA, Kruger DE, Luethy MH (2006) High lysine and high tryptophan transgenic maize resulting from the reduction of both 19- and 22-kD a-zeins. Plant Mol Biol 61:525-535
    • (2006) Plant Mol Biol , vol.61 , pp. 525-535
    • Huang, S.1    Frizzi, A.2    Florida, C.A.3    Kruger, D.E.4    Luethy, M.H.5
  • 47
    • 33645808723 scopus 로고    scopus 로고
    • An LLdiaminopimelate aminotransferase defines a novel variant of the lysine pathway in plants
    • Hudson AO, Singh BK, Leustek T, Gilvarg C (2006) An LLdiaminopimelate aminotransferase defines a novel variant of the lysine pathway in plants. Plant Physiol 140:292-301
    • (2006) Plant Physiol , vol.140 , pp. 292-301
    • Hudson, A.O.1    Singh, B.K.2    Leustek, T.3    Gilvarg, C.4
  • 49
    • 0001572731 scopus 로고
    • Storage protein-synthesis in maize. 2. Reduced synthesis of a major zein component by opaque-2 mutant of maize
    • Jones RA, Larkins BA, Tsai CY (1977a) Storage protein-synthesis in maize. 2. Reduced synthesis of a major zein component by opaque-2 mutant of maize. Plant Physiol 59:525-529
    • (1977) Plant Physiol , vol.59 , pp. 525-529
    • Jones, R.A.1    Larkins, B.A.2    Tsai, C.Y.3
  • 50
    • 0345085335 scopus 로고
    • Storage protein-synthesis in maize. 3. Developmental changes in membrane bound polyribosome composition and in vitro protein synthesis of normal and opaque-2 maize
    • Jones RA, Larkins BA, Tsai CY (1977b) Storage protein-synthesis in maize. 3. Developmental changes in membrane bound polyribosome composition and in vitro protein synthesis of normal and opaque-2 maize. Plant Physiol 59:733-737
    • (1977) Plant Physiol , vol.59 , pp. 733-737
    • Jones, R.A.1    Larkins, B.A.2    Tsai, C.Y.3
  • 51
    • 0032079778 scopus 로고    scopus 로고
    • Structure and regulation of the bifunctional enzyme-lysine-oxoglutarate reductase-saccharopine dehydrogenase in maize
    • Kemper EL, Cord-Neto G, Capella AN, Goncalves-Butruile M, Azevedo RA, Arruda P (1998) Structure and regulation of the bifunctional enzyme-lysine-oxoglutarate reductase-saccharopine dehydrogenase in maize. Eur J Biochem 253:720-729
    • (1998) Eur J Biochem , vol.253 , pp. 720-729
    • Kemper, E.L.1    Cord-Neto, G.2    Capella, A.N.3    Goncalves-Butruile, M.4    Azevedo, R.A.5    Arruda, P.6
  • 52
    • 0345504761 scopus 로고    scopus 로고
    • The role of Opaque2 in the control of lysine-degrading activities in developing maize endosperm
    • Kemper EL, Neto GC, Papes F, Moraes KCM, Leite A, Arruda P (1999) The role of Opaque2 in the control of lysine-degrading activities in developing maize endosperm. Plant Cell 11:1981-1993
    • (1999) Plant Cell , vol.11 , pp. 1981-1993
    • Kemper, E.L.1    Neto, G.C.2    Papes, F.3    Kcm, M.4    Leite, A.5    Arruda, P.6
  • 53
    • 0024301748 scopus 로고
    • The opaque-2 mutation of maize differentially reduces zein gene-transcription
    • Kodrzycki R, Boston RS, Larkins BA (1989) The opaque-2 mutation of maize differentially reduces zein gene-transcription. Plant Cell 1:105-114
    • (1989) Plant Cell , vol.1 , pp. 105-114
    • Kodrzycki, R.1    Boston, R.S.2    Larkins, B.A.3
  • 54
    • 0011409993 scopus 로고
    • Relative performance of normal and modified protein (opaque-2) maize hydrides
    • Lambert RJ, Alexander DE, Dudley JW (1969) Relative performance of normal and modified protein (opaque-2) maize hydrides. Crop Sci 9:242-243
    • (1969) Crop Sci , vol.9 , pp. 242-243
    • Lambert, R.J.1    Alexander, D.E.2    Dudley, J.W.3
  • 55
    • 0038419791 scopus 로고    scopus 로고
    • Quantitation of zeins from the lysine content of grain, endosperm and glutelins of maize
    • Landry J (2003) Quantitation of zeins from the lysine content of grain, endosperm and glutelins of maize. Maydica 48:39-54
    • (2003) Maydica , vol.48 , pp. 39-54
    • Landry, J.1
  • 56
    • 36549053215 scopus 로고    scopus 로고
    • Influence of genotype and texture on zein content in endosperm of maize grains
    • Landry J, Delhaye S (2007) Influence of genotype and texture on zein content in endosperm of maize grains. Ann Appl Biol 151:349-356
    • (2007) Ann Appl Biol , vol.151 , pp. 349-356
    • Landry, J.1    Delhaye, S.2
  • 57
    • 22244466474 scopus 로고    scopus 로고
    • Effect of the opaque and floury mutations on the accumulation of dry matter and protein fractions in maize endosperm
    • Landry J, Damerval C, Azevedo RA, Delhaye S (2005) Effect of the opaque and floury mutations on the accumulation of dry matter and protein fractions in maize endosperm. Plant Physiol Biochem 43:549-556
    • (2005) Plant Physiol Biochem , vol.43 , pp. 549-556
    • Landry, J.1    Damerval, C.2    Azevedo, R.A.3    Delhaye, S.4
  • 58
    • 34547753620 scopus 로고    scopus 로고
    • Suppression of C-hordein synthesis in barley by antisense constructs results in a more balanced amino acid composition
    • Lange M, Vincze E, Wieser H, Schjoerring JK, Holm PB (2007) Suppression of C-hordein synthesis in barley by antisense constructs results in a more balanced amino acid composition. J Agric Food Chem 55:6074-6081
    • (2007) J Agric Food Chem , vol.55 , pp. 6074-6081
    • Lange, M.1    Vincze, E.2    Wieser, H.3    Schjoerring, J.K.4    Holm, P.B.5
  • 59
    • 36549045684 scopus 로고    scopus 로고
    • Nitrogen use efficiency. 2. Amino acid metabolism
    • Lea PJ, Azevedo RA (2007) Nitrogen use efficiency. 2. Amino acid metabolism. Ann Appl Biol 151:269-275
    • (2007) Ann Appl Biol , vol.151 , pp. 269-275
    • Lea, P.J.1    Azevedo, R.A.2
  • 60
    • 0041370661 scopus 로고
    • Use of amino acid analogs in studies on plant metabolism
    • Lea PJ, Norris RD (1976) Use of amino acid analogs in studies on plant metabolism. Phytochemistry 15:585-595
    • (1976) Phytochemistry , vol.15 , pp. 585-595
    • Lea, P.J.1    Norris, R.D.2
  • 62
    • 34249767380 scopus 로고
    • Genetic analysis of opaque2 modifier gene activity in maize endosperm
    • Lopes MA, Larkins BA (1995) Genetic analysis of opaque2 modifier gene activity in maize endosperm. Theor Appl Genet 91:274-281
    • (1995) Theor Appl Genet , vol.91 , pp. 274-281
    • Lopes, M.A.1    Larkins, B.A.2
  • 64
    • 35348881985 scopus 로고    scopus 로고
    • Broiler performance and carcass characteristics when fed diets containing lysine maize (LY038 or LY038 9 MON 810), control, or Conventional Reference Maize
    • Lucas DM, Taylor ML, Hartnell GF, Nemeth MA, Glenn KC, Davis SW (2007) Broiler performance and carcass characteristics when fed diets containing lysine maize (LY038 or LY038 9 MON 810), control, or Conventional Reference Maize. Poult Sci 86:2152-2161
    • (2007) Poult Sci , vol.86 , pp. 2152-2161
    • Lucas, D.M.1    Taylor, M.L.2    Hartnell, G.F.3    Nemeth, M.A.4    Glenn, K.C.5    Davis, S.W.6
  • 65
    • 0001311990 scopus 로고
    • Mutant gene that changes protein composition and increase lysine content of maize endosperm
    • Mertz ET, Bates LS, Nelson OE (1964) Mutant gene that changes protein composition and increase lysine content of maize endosperm. Science 145:279-280
    • (1964) Science , vol.145 , pp. 279-280
    • Mertz, E.T.1    Bates, L.S.2    Nelson, O.E.3
  • 66
    • 0006914596 scopus 로고
    • Photosynthetic formation of the aspartate family of amino acids in isolated chloroplasts
    • Mills WR, Lea PJ, Miflin BJ (1980) Photosynthetic formation of the aspartate family of amino acids in isolated chloroplasts. Plant Physiol 65:1166-1172
    • (1980) Plant Physiol , vol.65 , pp. 1166-1172
    • Mills, W.R.1    Lea, P.J.2    Miflin, B.J.3
  • 67
    • 0014958494 scopus 로고
    • Gene for improved nutritional value in barley seed protein
    • Munck L, Karlsson KE, Hagberg A, Eggum BO (1970) Gene for improved nutritional value in barley seed protein. Science 168:985
    • (1970) Science , vol.168 , pp. 985
    • Munck, L.1    Karlsson, K.E.2    Hagberg, A.3    Eggum, B.O.4
  • 68
    • 0002378472 scopus 로고
    • Lysine overproducer mutants with an altered dihydrodipicolinate synthase from protoplast culture of Nicotiana sylvestris (Spegazzini and Comes)
    • Negrutiu I, Cattoir-Reynaerts A, Verbruggen I, Jacobs M (1984) Lysine overproducer mutants with an altered dihydrodipicolinate synthase from protoplast culture of Nicotiana sylvestris (Spegazzini and Comes). Theor Appl Genet 68:11-20
    • (1984) Theor Appl Genet , vol.68 , pp. 11-20
    • Negrutiu, I.1    Cattoir-Reynaerts, A.2    Verbruggen, I.3    Jacobs, M.4
  • 69
    • 0014213654 scopus 로고
    • Regulation by methionine of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K12
    • Patte JC, Lebras G, Cohen GN (1967) Regulation by methionine of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K12. Biochim Biophys Acta 136:245-257
    • (1967) Biochim Biophys Acta , vol.136 , pp. 245-257
    • Patte, J.C.1    Lebras, G.2    Cohen, G.N.3
  • 70
    • 0027130705 scopus 로고
    • Combining ability for yield and protein quality among modified-endosperm opaque-2 tropical maize inbreds
    • Pixley KV, Bjarnason MS (1993) Combining ability for yield and protein quality among modified-endosperm opaque-2 tropical maize inbreds. Crop Sci 33:1229-1234
    • (1993) Crop Sci , vol.33 , pp. 1229-1234
    • Pixley, K.V.1    Bjarnason, M.S.2
  • 72
    • 0002415484 scopus 로고
    • Feedback-insensitive aspartate kinase isoenzymes in barley mutants resistant to lysine plus threonine
    • Rognes SE, Bright SWJ, Miflin BJ (1983) Feedback-insensitive aspartate kinase isoenzymes in barley mutants resistant to lysine plus threonine. Planta 157:32-38
    • (1983) Planta , vol.157 , pp. 32-38
    • Rognes, S.E.1    Swj, B.2    Miflin, B.J.3
  • 73
    • 0023652835 scopus 로고
    • Transposon tagging and molecular analysis of the maize regulatory locus Opaque-2
    • Schmidt RJ, Burr FA, Burr B (1987) Transposon tagging and molecular analysis of the maize regulatory locus Opaque-2. Science 238:960-963
    • (1987) Science , vol.238 , pp. 960-963
    • Schmidt, R.J.1    Burr, F.A.2    Burr, B.3
  • 74
    • 0025169867 scopus 로고
    • Maize regulatory gene opaque-2 encodes a protein with a leucine-zipper motif that binds to zein DNA
    • Schmidt RJ, Burr FA, Aukerman MJ, Burr B (1990) Maize regulatory gene opaque-2 encodes a protein with a leucine-zipper motif that binds to zein DNA. Proc Natl Acad Sci USA 87:46-50
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 46-50
    • Schmidt, R.J.1    Burr, F.A.2    Aukerman, M.J.3    Burr, B.4
  • 75
    • 0026877588 scopus 로고
    • Opaque-2 is a transcriptional activator that recognizes a specific target site in 22-kd-zein genes
    • Schmidt RJ, Ketudat M, Aukerman MJ, Hoschek G (1992) Opaque-2 is a transcriptional activator that recognizes a specific target site in 22-kd-zein genes. Plant Cell 4:689-700
    • (1992) Plant Cell , vol.4 , pp. 689-700
    • Schmidt, R.J.1    Ketudat, M.2    Aukerman, M.J.3    Hoschek, G.4
  • 76
    • 0001593858 scopus 로고
    • Threonine overproduction in transgenic tobacco plants expressing a mutant desensitized aspartate kinase of Escherichia coli
    • Shaul O, Galili G (1992a) Threonine overproduction in transgenic tobacco plants expressing a mutant desensitized aspartate kinase of Escherichia coli. Plant Physiol 100:1157-1163
    • (1992) Plant Physiol , vol.100 , pp. 1157-1163
    • Shaul, O.1    Galili, G.2
  • 77
    • 0001188552 scopus 로고
    • Increased lysine synthesis in tobacco plants that express high levels of bacterial dihydrodipicolinate synthase in their chloroplasts
    • Shaul O, Galili G (1992b) Increased lysine synthesis in tobacco plants that express high levels of bacterial dihydrodipicolinate synthase in their chloroplasts. Plant J 2:203-209
    • (1992) Plant J , vol.2 , pp. 203-209
    • Shaul, O.1    Galili, G.2
  • 78
    • 0027691223 scopus 로고
    • Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feedback-insensitive aspartate kinase and dihydrodipicolinate synthase
    • Shaul O, Galili G (1993) Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feedback-insensitive aspartate kinase and dihydrodipicolinate synthase. Plant Mol Biol 23:759-768
    • (1993) Plant Mol Biol , vol.23 , pp. 759-768
    • Shaul, O.1    Galili, G.2
  • 79
    • 0345210412 scopus 로고
    • Evidence for the genetic-control of lysine catabolism in maize endosperm
    • Silva WJ, Arruda P (1979) Evidence for the genetic-control of lysine catabolism in maize endosperm. Phytochemistry 18:1803-1805
    • (1979) Phytochemistry , vol.18 , pp. 1803-1805
    • Silva, W.J.1    Arruda, P.2
  • 80
    • 0014848363 scopus 로고
    • Incorporation of leucine-C14 into protein in the developing of normal and opaque-2 corn
    • Sodek L, Wilson CM (1970) Incorporation of leucine-C14 into protein in the developing of normal and opaque-2 corn. Arch Biochem Biophys 140:29-38
    • (1970) Arch Biochem Biophys , vol.140 , pp. 29-38
    • Sodek, L.1    Wilson, C.M.2
  • 81
    • 32644458045 scopus 로고
    • Comparison of effect of shrunken-4, opaque-2, opaque-7, and floury-2 genes on zein content of maize during endosperm development
    • Tsai CY, Dalby A (1974) Comparison of effect of shrunken-4, opaque-2, opaque-7, and floury-2 genes on zein content of maize during endosperm development. Cereal Chem 51:825-829
    • (1974) Cereal Chem , vol.51 , pp. 825-829
    • Tsai, C.Y.1    Dalby, A.2
  • 82
    • 38549144582 scopus 로고    scopus 로고
    • Lysine biosynthesis and nitrogen metabolism in quinoa (Chenopodium quinoa): Study of enzymes and nitrogen-containing compounds
    • Varisi VA, Camargos LS, Aguiar LF, Christofoleti RM, Medici LO, Azevedo RA (2008) Lysine biosynthesis and nitrogen metabolism in quinoa (Chenopodium quinoa): study of enzymes and nitrogen-containing compounds. Plant Physiol Biochem 46:11-18
    • (2008) Plant Physiol Biochem , vol.46 , pp. 11-18
    • Varisi, V.A.1    Camargos, L.S.2    Aguiar, L.F.3    Christofoleti, R.M.4    Medici, L.O.5    Azevedo, R.A.6
  • 83
    • 0002139233 scopus 로고
    • High quality protein corn
    • Hallawer AR (ed), CRC Press, Boca Raton
    • Vasal SK (1994) High quality protein corn. In: Hallawer AR (ed) Specialty corns. CRC Press, Boca Raton, pp 79-120
    • (1994) Specialty Corns , pp. 79-120
    • Vasal, S.K.1
  • 85
    • 11944254685 scopus 로고
    • New methods for extraction and quantitation of zeins reveal a high content of gamma-zein in modified opaque-2 maize
    • Wallace JC, Lopes MA, Paiva E, Larkins BA (1990) New methods for extraction and quantitation of zeins reveal a high content of gamma-zein in modified opaque-2 maize. Plant Physiol 92:191-196
    • (1990) Plant Physiol , vol.92 , pp. 191-196
    • Wallace, J.C.1    Lopes, M.A.2    Paiva, E.3    Larkins, B.A.4
  • 86
    • 34548456805 scopus 로고    scopus 로고
    • Characterization of monofunctional aspartate kinase genes in maize and their relationship with free amino acid content in the endosperm
    • Wang XL, Lopez-Valenzuela JA, Gibbon BC (2007) Characterization of monofunctional aspartate kinase genes in maize and their relationship with free amino acid content in the endosperm. J Exp Bot 58:2653-2660
    • (2007) J Exp Bot , vol.58 , pp. 2653-2660
    • Wang, X.L.1    Lopez-Valenzuela, J.A.2    Gibbon, B.C.3
  • 87
    • 0014215411 scopus 로고
    • Ribonuclease activity in normal and opaque-2 mutant endosperm of maize
    • Wilson CM, Alexander DE (1967) Ribonuclease activity in normal and opaque-2 mutant endosperm of maize. Science 155:1575-1576
    • (1967) Science , vol.155 , pp. 1575-1576
    • Wilson, C.M.1    Alexander, D.E.2
  • 88
    • 0000469671 scopus 로고
    • Bifunctional protein in carrot contains both aspartokinase and homoserine dehydrogenase activities
    • Wilson BJ, Gray AC, Matthews BF (1991) Bifunctional protein in carrot contains both aspartokinase and homoserine dehydrogenase activities. Plant Physiol 97:1323-1328
    • (1991) Plant Physiol , vol.97 , pp. 1323-1328
    • Wilson, B.J.1    Gray, A.C.2    Matthews, B.F.3
  • 89
    • 2442644300 scopus 로고    scopus 로고
    • Lysine metabolism is concurrently regulated by synthesis and catabolism in both reproductive and vegetative tissues
    • Zhu XH, Galili G (2004) Lysine metabolism is concurrently regulated by synthesis and catabolism in both reproductive and vegetative tissues. Plant Physiol 135:129-136
    • (2004) Plant Physiol , vol.135 , pp. 129-136
    • Zhu, X.H.1    Galili, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.