메뉴 건너뛰기




Volumn 153, Issue 3-4, 1998, Pages 281-289

Isolation, partial purification and characterization of isoenzymes of aspartate kinase from rice seeds

Author keywords

Aspartate kinase; Aspartic acid pathway; Homoserine dehydrogenase; Lysine; Rice; Threonine

Indexed keywords

EMBRYOPHYTA; ORIZA; ORIZA SATIVA; ORYZA SATIVA;

EID: 0031760192     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0176-1617(98)80153-3     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 0001306027 scopus 로고
    • Threonine-sensitive aspartate kinase and homoserine dehydrogenase from Pisum sativum
    • H. Aarnes S.E. Rognes Threonine-sensitive aspartate kinase and homoserine dehydrogenase from Pisum sativum Phytochemistry 13 1974 2717 2724
    • (1974) Phytochemistry , vol.13 , pp. 2717-2724
    • Aarnes, H.1    Rognes, S.E.2
  • 2
    • 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
    • P. Arruda S.W.J. Bright J.S.H. Kueh P.J. Lea S.E. Rognes 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 1984 442
    • (1984) Plant Physiol. , vol.76 , pp. 442
    • Arruda, P.1    Bright, S.W.J.2    Kueh, J.S.H.3    Lea, P.J.4    Rognes, S.E.5
  • 3
    • 85119809491 scopus 로고
    • Isolation, purification and characterization of aspartate kinase isoenzymes from maize
    • R.A. Azevedo Isolation, purification and characterization of aspartate kinase isoenzymes from maize Ph. D. Thesis 1992 University of Lancaster UK
    • (1992)
    • Azevedo, R.A.1
  • 4
    • 0029110653 scopus 로고
    • Dominant and recessive mutants conferring resistance to S-2-aminoethyl-L-cysteine in maize
    • R.A. Azevedo P. Arruda Dominant and recessive mutants conferring resistance to S-2-aminoethyl-L-cysteine in maize J. Plant Physiol. 145 1995 321 326
    • (1995) J. Plant Physiol. , vol.145 , pp. 321-326
    • Azevedo, R.A.1    Arruda, P.2
  • 5
    • 0031260404 scopus 로고    scopus 로고
    • The biosynthesis and metabolism of the aspartate derived amino acids in higher plants
    • R.A. Azevedo P. Arruda W.J. Turner P.J. Lea The biosynthesis and metabolism of the aspartate derived amino acids in higher plants Phytochemistry 46 1997 395 419
    • (1997) Phytochemistry , vol.46 , pp. 395-419
    • Azevedo, R.A.1    Arruda, P.2    Turner, W.J.3    Lea, P.J.4
  • 7
    • 0001136267 scopus 로고
    • Aspartate kinase regulation in maize: evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase
    • R.A. Azevedo R.J. Smith P.J. Lea Aspartate kinase regulation in maize: evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase Phytochemistry 31 1992 3731 3734
    • (1992) Phytochemistry , vol.31 , pp. 3731-3734
    • Azevedo, R.A.1    Smith, R.J.2    Lea, P.J.3
  • 8
    • 0013569212 scopus 로고
    • Enzymes of lysine synthesis
    • P.J.R. Bonner P.J. Lea Enzymes of lysine synthesis P.J. Lea Methods in Plant Biochemistry Vol. 3 1990 Academic Press London 297 313
    • (1990) , pp. 297-313
    • Bonner, P.J.R.1    Lea, P.J.2
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0020038561 scopus 로고
    • Threonine accumulation in the seed of a barley mutant with an altered aspartate kinase
    • S.W.J. Bright B.J. Miflin S.E. Rognes Threonine accumulation in the seed of a barley mutant with an altered aspartate kinase Biochem. Genet. 20 1982 229 243
    • (1982) Biochem. Genet. , vol.20 , pp. 229-243
    • Bright, S.W.J.1    Miflin, B.J.2    Rognes, S.E.3
  • 12
    • 0000361183 scopus 로고
    • Differential regulation of maize homoserine dehydrogenase under physiological conditions
    • J.K. Bryan Differential regulation of maize homoserine dehydrogenase under physiological conditions Plant Physiol. 92 1990 785 791
    • (1990) Plant Physiol. , vol.92 , pp. 785-791
    • Bryan, J.K.1
  • 13
    • 0342636259 scopus 로고
    • The control of lysine biosynthesis in maize
    • R.M. Cheshire B.J. Miflin The control of lysine biosynthesis in maize Phytochemistry 14 1975 695 698
    • (1975) Phytochemistry , vol.14 , pp. 695-698
    • Cheshire, R.M.1    Miflin, B.J.2
  • 14
    • 84931975752 scopus 로고
    • Regulation of amino acid biosynthesis in carrot tissue cultures
    • H.M. Davies Regulation of amino acid biosynthesis in carrot tissue cultures Ph. D. Thesis 1977 University of London UK
    • (1977)
    • Davies, H.M.1
  • 15
    • 0042444742 scopus 로고
    • Aspartate kinase from carrot cell suspension culture
    • H.M. Davies B.J. Miflin Aspartate kinase from carrot cell suspension culture Plant Sci. Lett. 9 1977 323 332
    • (1977) Plant Sci. Lett. , vol.9 , pp. 323-332
    • Davies, H.M.1    Miflin, B.J.2
  • 16
    • 0041442518 scopus 로고
    • Regulatory isoenzymes of aspartate kinase and the control of lysine and threonine biosynthesis in carrot cell suspension culture
    • H.M. Davies B.J. Miflin Regulatory isoenzymes of aspartate kinase and the control of lysine and threonine biosynthesis in carrot cell suspension culture Plant Physiol. 62 1978 536 541
    • (1978) Plant Physiol. , vol.62 , pp. 536-541
    • Davies, H.M.1    Miflin, B.J.2
  • 17
    • 0001432042 scopus 로고
    • Purification and characterization of lysine-sensitive aspartate kinase from maize cell suspension cultures
    • S.B. Dotson D.A. Somers B.G. Gengenbach Purification and characterization of lysine-sensitive aspartate kinase from maize cell suspension cultures Plant Physiol. 91 1989 1602 1608
    • (1989) Plant Physiol. , vol.91 , pp. 1602-1608
    • Dotson, S.B.1    Somers, D.A.2    Gengenbach, B.G.3
  • 18
    • 0031148690 scopus 로고    scopus 로고
    • Molecular characterization of an Arabidopsis thaliana cDNA coding for a monofunctional aspartate kinase
    • V. Frankard M. Vauterin M. Jacobs Molecular characterization of an Arabidopsis thaliana cDNA coding for a monofunctional aspartate kinase Plant Mol. Biol. 34 1997 233 242
    • (1997) Plant Mol. Biol. , vol.34 , pp. 233-242
    • Frankard, V.1    Vauterin, M.2    Jacobs, M.3
  • 19
    • 0005725378 scopus 로고    scopus 로고
    • Lysine biosynthesis and degradation in rice developing seeds. Enzyme isolation and regulation
    • S.A. Gaziola C.M.G. Teixeira A. Ando L. Sodek R.A. Azevedo Lysine biosynthesis and degradation in rice developing seeds. Enzyme isolation and regulation Int. Rice. Res. Notes 21 1996 27 28
    • (1996) Int. Rice. Res. Notes , vol.21 , pp. 27-28
    • Gaziola, S.A.1    Teixeira, C.M.G.2    Ando, A.3    Sodek, L.4    Azevedo, R.A.5
  • 20
    • 0030758692 scopus 로고    scopus 로고
    • The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate/saccharopine dehydrogenase bifunctional polypetide
    • S.A. Gaziola C.M.G. Teixeira J. Lugli L. Sodek R.A. Azevedo The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate/saccharopine dehydrogenase bifunctional polypetide Eur. J. Biochem. 247 1997 364 371
    • (1997) Eur. J. Biochem. , vol.247 , pp. 364-371
    • Gaziola, S.A.1    Teixeira, C.M.G.2    Lugli, J.3    Sodek, L.4    Azevedo, R.A.5
  • 21
    • 0028385754 scopus 로고
    • Molecular analysis of the aspartate kinase — homoserine dehydrogenase from Arabidopsis thaliana
    • M. Ghislain V. Frankard D. Vandenbossche B.F. Matthews M. Jacobs Molecular analysis of the aspartate kinase — homoserine dehydrogenase from Arabidopsis thaliana Plant Mol. Biol. 24 1994 835 851
    • (1994) Plant Mol. Biol. , vol.24 , pp. 835-851
    • Ghislain, M.1    Frankard, V.2    Vandenbossche, D.3    Matthews, B.F.4    Jacobs, M.5
  • 22
    • 0030042427 scopus 로고    scopus 로고
    • Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize
    • M. Gonçalves-Butruille P. Szajner E. Torigoi A. Leite P. Arruda Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize Plant Physiol. 110 1996 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
  • 23
    • 0022701727 scopus 로고
    • Use of monoclonal antibodies for the purification and characterization of the threonine-sensitive isozyme of maize homoserine dehydrogenase
    • S. Krishnaswamy J.K. Bryan Use of monoclonal antibodies for the purification and characterization of the threonine-sensitive isozyme of maize homoserine dehydrogenase Arch. Biochem. Biophys. 246 1986 250 262
    • (1986) Arch. Biochem. Biophys. , vol.246 , pp. 250-262
    • Krishnaswamy, S.1    Bryan, J.K.2
  • 24
    • 0000971260 scopus 로고
    • Analysis of barley metabolism using mutant genes
    • P.J. Lea R.D. Blackwell R.A. Azevedo Analysis of barley metabolism using mutant genes P.R. Shewry Barley: Genetics, Molecular Biology and Biotechnology 1992 CAB International Oxford 181 208
    • (1992) , pp. 181-208
    • Lea, P.J.1    Blackwell, R.D.2    Azevedo, R.A.3
  • 25
    • 0018437786 scopus 로고
    • The isolation of a lysinesensitive aspartate kinase from pea leaves and its involvement in homoserine biosynthesis in isolated chloroplasts
    • P.J. Lea W.R. Mills B.J. Miflin The isolation of a lysinesensitive aspartate kinase from pea leaves and its involvement in homoserine biosynthesis in isolated chloroplasts FEBS Lett. 98 1979 165 168
    • (1979) FEBS Lett. , vol.98 , pp. 165-168
    • Lea, P.J.1    Mills, W.R.2    Miflin, B.J.3
  • 26
    • 0005656775 scopus 로고
    • Isolation of aspartate kinase from Coix lacryma-jobi
    • J. Lugli R.A. Azevedo Isolation of aspartate kinase from Coix lacryma-jobi Maize Newsletters 68 1994 75 77
    • (1994) Maize Newsletters , vol.68 , pp. 75-77
    • Lugli, J.1    Azevedo, R.A.2
  • 27
    • 85051584923 scopus 로고
    • Cloning and analysis of cDNAs encoding bifunctional aspartate kinase homoserine dehydrogenase activities in carrot and soybean
    • B.F. Matthews J.M. Weisemann K.M. Lewin G.J. Wadsworth J.S. Gebhardt Cloning and analysis of cDNAs encoding bifunctional aspartate kinase homoserine dehydrogenase activities in carrot and soybean B.K. Singh H.E. Flores J.C. Shannon Biosynthesis and Molecular Regulation of Amino Acids in Plants Vol. 7 1992 American Society of Plant Physiologists Rockville 294 295
    • (1992) , pp. 294-295
    • Matthews, B.F.1    Weisemann, J.M.2    Lewin, K.M.3    Wadsworth, G.J.4    Gebhardt, J.S.5
  • 28
    • 0001432043 scopus 로고
    • Purification and interconversion of homoserine dehydrogenase from Daucus carota cell-suspension cultures
    • B.F. Matthews M.J. Farrar A.C. Gray Purification and interconversion of homoserine dehydrogenase from Daucus carota cell-suspension cultures Plant Physiol. 91 1989 1569 1574
    • (1989) Plant Physiol. , vol.91 , pp. 1569-1574
    • Matthews, B.F.1    Farrar, M.J.2    Gray, A.C.3
  • 29
    • 0011491433 scopus 로고
    • Regulation of homoserine dehydrogenase in developing organs of soybean seedlings
    • B.F. Matthews J.M. Widholm Regulation of homoserine dehydrogenase in developing organs of soybean seedlings Phytochemistry 18 1979 395 400
    • (1979) Phytochemistry , vol.18 , pp. 395-400
    • Matthews, B.F.1    Widholm, J.M.2
  • 30
    • 0028675928 scopus 로고
    • Molecular genetics of the maize (Zea mays L.) aspartate kinase-homoserine dehydrogenase gene family
    • G.J. Muehlbauer D.A. Somers B.F. Matthews B.G. Gengenbach Molecular genetics of the maize ( Zea mays L.) aspartate kinase-homoserine dehydrogenase gene family Plant Physiol. 106 1994 1303 1312
    • (1994) Plant Physiol. , vol.106 , pp. 1303-1312
    • Muehlbauer, G.J.1    Somers, D.A.2    Matthews, B.F.3    Gengenbach, B.G.4
  • 31
    • 0014213654 scopus 로고
    • Regulation by methionine of the synthesis of a third aspartate kinase and a second homoserine dehydrogenase in Escherichia coli K12
    • J.C. Patte G. Le-Bras G.N. Cohen Regulation by methionine of the synthesis of a third aspartate kinase and a second homoserine dehydrogenase in Escherichia coli K12 Biochim. Biophys. Acta 136 1967 245 257
    • (1967) Biochim. Biophys. Acta , vol.136 , pp. 245-257
    • Patte, J.C.1    Le-Bras, G.2    Cohen, G.N.3
  • 32
    • 0002638086 scopus 로고
    • Physical and kinetic properties of lysine-sensitive aspartate kinase purified from carrot cell suspension culture
    • J.M. Relton P.L.R. Bonner R.M. Wallsgrove P.J. Lea Physical and kinetic properties of lysine-sensitive aspartate kinase purified from carrot cell suspension culture Biochim. Biophys. Acta 953 1988 48 60
    • (1988) Biochim. Biophys. Acta , vol.953 , pp. 48-60
    • Relton, J.M.1    Bonner, P.L.R.2    Wallsgrove, R.M.3    Lea, P.J.4
  • 33
    • 0001535884 scopus 로고
    • Threonine biosynthesis
    • S.E. Rognes Threonine biosynthesis P.J. Lea Methods in Plant Biochemistry — Enzymes of the Primary Metabolism Vol. 3 1990 Academic Press London 315 324
    • (1990) , pp. 315-324
    • Rognes, S.E.1
  • 34
    • 0018948321 scopus 로고
    • S-adenosylmethionine: a novel regulator of aspartate kinase (EC 2.7.2.4)
    • S.E. Rognes P.J. Lea B.J. Miflin S-adenosylmethionine: a novel regulator of aspartate kinase (EC 2.7.2.4) Nature 287 1980 357 359
    • (1980) Nature , vol.287 , pp. 357-359
    • Rognes, S.E.1    Lea, P.J.2    Miflin, B.J.3
  • 35
    • 0013247091 scopus 로고
    • Localisation and characterization of homoserine dehydrogenase isolated from barley and pea leaves
    • J.K. Sainis R.G. Mayne R.M. Wallsgrove P.J. Lea B.J. Miflin Localisation and characterization of homoserine dehydrogenase isolated from barley and pea leaves Planta 152 1981 491 496
    • (1981) Planta , vol.152 , pp. 491-496
    • Sainis, J.K.1    Mayne, R.G.2    Wallsgrove, R.M.3    Lea, P.J.4    Miflin, B.J.5
  • 36
    • 0017852107 scopus 로고
    • Fine structure analysis of the threonine operon in Escherichia coli K12
    • I. Saint-Girons D. Margarita Fine structure analysis of the threonine operon in Escherichia coli K12 Mol. Gen. Genet. 162 1978 101 108
    • (1978) Mol. Gen. Genet. , vol.162 , pp. 101-108
    • Saint-Girons, I.1    Margarita, D.2
  • 37
    • 0042945599 scopus 로고
    • Change in the proportion of two aspartokinases in carrot root tissue in response to in vitro culture
    • K. Sakano A. Komamine Change in the proportion of two aspartokinases in carrot root tissue in response to in vitro culture Plant Physiol. 61 1978 115 118
    • (1978) Plant Physiol. , vol.61 , pp. 115-118
    • Sakano, K.1    Komamine, A.2
  • 38
    • 0001593858 scopus 로고
    • Threonine overproduction in transgenic tobacco plants expressing a mutant desensitized aspartate kinase of Escherichia coli
    • O. Shaul G. Galili Threonine overproduction in transgenic tobacco plants expressing a mutant desensitized aspartate kinase of Escherichia coli Plant Physiol. 100 1992 1157 1163
    • (1992) Plant Physiol. , vol.100 , pp. 1157-1163
    • Shaul, O.1    Galili, G.2
  • 39
    • 0027691223 scopus 로고
    • Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feed-back-insensitive aspartate kinase and dihydrodipicolinate synthase
    • O. Shaul G. Galili Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feed-back-insensitive aspartate kinase and dihydrodipicolinate synthase Plant Mol. Biol. 23 1993 759 768
    • (1993) Plant Mol. Biol. , vol.23 , pp. 759-768
    • Shaul, O.1    Galili, G.2
  • 40
    • 84921070666 scopus 로고
    • Regulation and properties of rice (Oryza sativa cultivar Shingchu) aspartokinase (EC 2.7.2.4)
    • J.F. Shaw C.Y. Ku Regulation and properties of rice ( Oryza sativa cultivar Shingchu) aspartokinase (EC 2.7.2.4) Bot. Bull. Acad. Sin. 25 1984 45 58
    • (1984) Bot. Bull. Acad. Sin. , vol.25 , pp. 45-58
    • Shaw, J.F.1    Ku, C.Y.2
  • 41
    • 0343592279 scopus 로고
    • Properties and regulation of aspartate kinase from barley seedlings
    • P.R. Shewry B.J. Miflin Properties and regulation of aspartate kinase from barley seedlings Plant Physiol. 59 1977 69 73
    • (1977) Plant Physiol. , vol.59 , pp. 69-73
    • Shewry, P.R.1    Miflin, B.J.2
  • 42
    • 0000234488 scopus 로고
    • Feedback inhibition and repression of aspartokinase activity in Escherichia coli and Saccharomyces cerovisiae
    • E.R. Stadtman G.N. Cohen G. Le-Bras H. Robinson-Szulmajster Feedback inhibition and repression of aspartokinase activity in Escherichia coli and Saccharomyces cerovisiae J. Biol. Chem. 236 1961 2033 2038
    • (1961) J. Biol. Chem. , vol.236 , pp. 2033-2038
    • Stadtman, E.R.1    Cohen, G.N.2    Le-Bras, G.3    Robinson-Szulmajster, H.4
  • 43
    • 0031149180 scopus 로고    scopus 로고
    • Cloning and expression of an Arabidopsis thaliana cDNA encoding a monofunctional aspartate kinase homologous to the lysine-sensitive enzyme of Escherichia coli
    • G.L. Tang J.X. Zhu-Shimoni R. Amir I.B.T. Zchori G. Galili Cloning and expression of an Arabidopsis thaliana cDNA encoding a monofunctional aspartate kinase homologous to the lysine-sensitive enzyme of Escherichia coli Plant Mol. Biol. 34 1997 287 293
    • (1997) Plant Mol. Biol. , vol.34 , pp. 287-293
    • Tang, G.L.1    Zhu-Shimoni, J.X.2    Amir, R.3    Zchori, I.B.T.4    Galili, G.5
  • 44
    • 0000087176 scopus 로고
    • Intracellular localization of aspartate kinase (EC 2.7.2.4) and the enzymes of threonine and methionine biosynthesis in green leaves
    • R.M. Wallsgrove P.J. Lea B.J. Miflin Intracellular localization of aspartate kinase (EC 2.7.2.4) and the enzymes of threonine and methionine biosynthesis in green leaves Plant Physiol. 71 1983 780 784
    • (1983) Plant Physiol. , vol.71 , pp. 780-784
    • Wallsgrove, R.M.1    Lea, P.J.2    Miflin, B.J.3
  • 45
    • 0018800326 scopus 로고
    • Isolation and characterization of two homoserine dehydrogenase from maize suspension cultures
    • T.J. Walter J.A. Connelly B.G. Gengenbach F. Wold Isolation and characterization of two homoserine dehydrogenase from maize suspension cultures J. Biol. Chem. 254 1979 1349 1355
    • (1979) J. Biol. Chem. , vol.254 , pp. 1349-1355
    • Walter, T.J.1    Connelly, J.A.2    Gengenbach, B.G.3    Wold, F.4
  • 46
    • 0027598473 scopus 로고
    • Identification and expression of a cDNA from Dauern carota encoding a bifunctional aspartokinase-homoserine dehydrogenase
    • J.M. Weisemann B.F. Matthews Identification and expression of a cDNA from Dauern carota encoding a bifunctional aspartokinase-homoserine dehydrogenase Plant Mol. Biol. 22 1993 301 312
    • (1993) Plant Mol. Biol. , vol.22 , pp. 301-312
    • Weisemann, J.M.1    Matthews, B.F.2
  • 47
    • 0000469671 scopus 로고
    • Bifunctional protein in carrot contains both aspartokinase and homoserine dehydrogenase activities
    • B.J. Wilson A.C. Gray B.F. Matthews Bifunctional protein in carrot contains both aspartokinase and homoserine dehydrogenase activities Plant Physiol. 97 1991 1323 1328
    • (1991) Plant Physiol. , vol.97 , pp. 1323-1328
    • Wilson, B.J.1    Gray, A.C.2    Matthews, B.F.3
  • 48
    • 0020567509 scopus 로고
    • Nucleotide sequence of the met 1 gene of Escherichia coli. Its product, the bifunctional aspartokinase II (EC 2.7.2.4) — homoserin dehydrogenase II (EC 1.1.1.3) and the bifunctional product of the thrA gene, aspartokinase I — homoserine dehydrogenase I, derive from a common ancestor
    • M.M. Zakin N. Duchange P. Ferrara G.N. Cohen Nucleotide sequence of the met 1 gene of Escherichia coli . Its product, the bifunctional aspartokinase II (EC 2.7.2.4) — homoserin dehydrogenase II (EC 1.1.1.3) and the bifunctional product of the thrA gene, aspartokinase I — homoserine dehydrogenase I, derive from a common ancestor J. Biol. Chem. 258 1983 3028 3031
    • (1983) J. Biol. Chem. , vol.258 , pp. 3028-3031
    • Zakin, M.M.1    Duchange, N.2    Ferrara, P.3    Cohen, G.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.