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Volumn 35, Issue 6, 1997, Pages 735-748

Lysine-ketoglutarate reductase and saccharopine dehydrogenase from Arabidopsis thaliana: Nucleotide sequence and characterization

Author keywords

Arabidopsis thaliana; Heterologous expression; Lysine catabolism; Lysine ketoglutarate reductase saccharopine dehydrogenase

Indexed keywords

COMPLEMENTARY DNA; MULTIENZYME COMPLEX; RECOMBINANT PROTEIN; SACCHAROPINE DEHYDROGENASE; SACCHAROPINE DEHYDROGENASE (NADP+, LYSINE FORMING); SACCHAROPINE DEHYDROGENASE (NADP+, LYSINE-FORMING); SIGNAL PEPTIDE; VEGETABLE PROTEIN;

EID: 0031458069     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005808923191     Document Type: Article
Times cited : (20)

References (34)
  • 1
    • 0000082872 scopus 로고
    • Lysine-ketoglutarate reductase activity in developing maize endosperm
    • Arruda P, Da Silva WJ: Lysine-ketoglutarate reductase activity in developing maize endosperm. Phytochemistry 22: 2687-2689 (1983).
    • (1983) Phytochemistry , vol.22 , pp. 2687-2689
    • Arruda, P.1    Da Silva, W.J.2
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M: A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254 (1976).
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 3
    • 0000690359 scopus 로고
    • Partial purification and characterization of lysine-ketoglutarate reductase in normal and opaque-2 maize endosperms
    • Brochetto-Braga M, Leite A, Arruda P: Partial purification and characterization of lysine-ketoglutarate reductase in normal and opaque-2 maize endosperms. Plant Physiol 98: 1139-1147 (1992).
    • (1992) Plant Physiol , vol.98 , pp. 1139-1147
    • Brochetto-Braga, M.1    Leite, A.2    Arruda, P.3
  • 5
    • 84941145308 scopus 로고
    • Advances in the biochemistry of amino acid biosynthesis
    • Miflin BJ, Lea PJ (eds) Intermediary Nitrogen Metabolism. Academic Press, New York
    • Bryan JK: Advances in the biochemistry of amino acid biosynthesis. In: Miflin BJ, Lea PJ (eds) Intermediary Nitrogen Metabolism, pp. 161-196. The Biochemistry of Plants, vol. 16. Academic Press, New York (1990).
    • (1990) The Biochemistry of Plants , vol.16 , pp. 161-196
    • Bryan, J.K.1
  • 6
    • 0000320052 scopus 로고
    • Synthesis of the aspartate family and branched-chain amino acids
    • Miflin BJ (ed) Amino Acids and Derivatives. Academic Press, New York
    • Bryan JK: Synthesis of the aspartate family and branched-chain amino acids. In: Miflin BJ (ed) Amino Acids and Derivatives, pp. 403-452. The Biochemistry of Plants, vol. 5. Academic Press, New York (1980).
    • (1980) The Biochemistry of Plants , vol.5 , pp. 403-452
    • Bryan, J.K.1
  • 7
    • 0025278259 scopus 로고
    • Weight matrix description of four eukaryotic RNA polymerase II promoter elements derived from 502 unrelated promoter sequences
    • Buchner P: Weight matrix description of four eukaryotic RNA polymerase II promoter elements derived from 502 unrelated promoter sequences. J Mol Biol 212: 563-578 (1990).
    • (1990) J Mol Biol , vol.212 , pp. 563-578
    • Buchner, P.1
  • 8
    • 0001619394 scopus 로고
    • Biosynthesis of threonine, lysine and methionine
    • Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (eds). American Society for Microbiology, Washington, DC
    • Cohen NG, Saint-Girons I: Biosynthesis of threonine, lysine and methionine. In: Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol I, pp. 429-444. American Society for Microbiology, Washington, DC (1987).
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , vol.1 , pp. 429-444
    • Cohen, N.G.1    Saint-Girons, I.2
  • 10
    • 0028041491 scopus 로고
    • Repression of the genes for lysine biosynthesis in Saccharomyces cerevisiae is caused by limitation of Lys14-dependent transcriptional activation
    • Feller A, Dubois E, Ramos F, Pierard A: Repression of the genes for lysine biosynthesis in Saccharomyces cerevisiae is caused by limitation of Lys14-dependent transcriptional activation. Mol Cell Biol 14: 6411-6418 (1994).
    • (1994) Mol Cell Biol , vol.14 , pp. 6411-6418
    • Feller, A.1    Dubois, E.2    Ramos, F.3    Pierard, A.4
  • 11
    • 0028119550 scopus 로고
    • Tissue-specific and temporal regulation of a β-conglycinin gene: Roles of the RY repeat and other cis-acting elements
    • Fujiwara T, Beachy RN: Tissue-specific and temporal regulation of a β-conglycinin gene: roles of the RY repeat and other cis-acting elements. Plant Mol Biol 24: 261-272 (1994).
    • (1994) Plant Mol Biol , vol.24 , pp. 261-272
    • Fujiwara, T.1    Beachy, R.N.2
  • 12
    • 0027993014 scopus 로고
    • Molecular and functional analysis of the LYS1 gene of Candida albicans
    • Garrad R, Schmidt TM, Bhattacharjee JK: Molecular and functional analysis of the LYS1 gene of Candida albicans. Infect Immun 62: 5027-5031 (1994).
    • (1994) Infect Immun , vol.62 , pp. 5027-5031
    • Garrad, R.1    Schmidt, T.M.2    Bhattacharjee, J.K.3
  • 13
    • 0001693369 scopus 로고
    • Dihydropicolinate synthase of Nicotiana sylvestris, a chloroplast-localized enzyme of the lysine pathway
    • Ghislain MV, Frankard V, Jacobs M: Dihydropicolinate synthase of Nicotiana sylvestris, a chloroplast-localized enzyme of the lysine pathway. Planta 180: 480-486 (1990).
    • (1990) Planta , vol.180 , pp. 480-486
    • Ghislain, M.V.1    Frankard, V.2    Jacobs, M.3
  • 14
    • 0028385754 scopus 로고
    • Molecular analysis of the aspartate kinase-homoserine dehydrogenase gene from Arabidopsis thaliana
    • Ghislain M, Frankard V, Vandenbossche D, Matthews F, Jacobs M: Molecular analysis of the aspartate kinase-homoserine dehydrogenase gene from Arabidopsis thaliana. Plant Mol Biol 24: 835-851 (1994).
    • (1994) Plant Mol Biol , vol.24 , pp. 835-851
    • Ghislain, M.1    Frankard, V.2    Vandenbossche, D.3    Matthews, F.4    Jacobs, M.5
  • 15
    • 0030042427 scopus 로고    scopus 로고
    • Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize
    • Goncalves-butruille M, Szajner P, Torigoi E, Leite A, Arruda P: Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize. Plant Physiol 110: 765-771 (1996).
    • (1996) Plant Physiol , vol.110 , pp. 765-771
    • Goncalves-butruille, M.1    Szajner, P.2    Torigoi, E.3    Leite, A.4    Arruda, P.5
  • 16
    • 0023650367 scopus 로고
    • Putative polyadenylation signals in nuclear genes of higher plants: A compilation and analysis
    • Joshi CP: Putative polyadenylation signals in nuclear genes of higher plants: a compilation and analysis. Nucl Acids Res 15: 9627-9640 (1987).
    • (1987) Nucl Acids Res , vol.15 , pp. 9627-9640
    • Joshi, C.P.1
  • 17
    • 0025167552 scopus 로고
    • Molecular cloning of wheat dihydropicolinate synthase
    • Kaneko T, Hashimoto T, Kumpaisal R, Yamada Y: Molecular cloning of wheat dihydropicolinate synthase. J Biol Chem 265: 17451-17455 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 17451-17455
    • Kaneko, T.1    Hashimoto, T.2    Kumpaisal, R.3    Yamada, Y.4
  • 18
    • 0029411732 scopus 로고
    • The lysine-dependent stimulation of lysine catabolism in tobacco seed requires calcium and protein phosphorylation
    • Karchi H, Miron D, Ben-Yaacov S, Galili G: The lysine-dependent stimulation of lysine catabolism in tobacco seed requires calcium and protein phosphorylation. Plant Cell 7: 1963-1970 (1995).
    • (1995) Plant Cell , vol.7 , pp. 1963-1970
    • Karchi, H.1    Miron, D.2    Ben-Yaacov, S.3    Galili, G.4
  • 19
    • 0028331761 scopus 로고
    • Lysine synthesis and catabolism are coordinately regulated during tobacco seed development
    • Karchi H, Shaul O, Galili G: Lysine synthesis and catabolism are coordinately regulated during tobacco seed development. Proc Natl Acad Sci USA 91: 2577-2581 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2577-2581
    • Karchi, H.1    Shaul, O.2    Galili, G.3
  • 20
    • 0026532613 scopus 로고
    • Plant transcription factors: Present knowledge and future challenges
    • Katagiri F, Chua NH: Plant transcription factors: present knowledge and future challenges. Trends Genet 8: 22-27 (1992).
    • (1992) Trends Genet , vol.8 , pp. 22-27
    • Katagiri, F.1    Chua, N.H.2
  • 21
    • 0000808158 scopus 로고
    • Chloroplastic precursors and their transport across the envelope membranes
    • Keegstra K, Olsen LJ, Theg SM: Chloroplastic precursors and their transport across the envelope membranes. Plant Mol Biol 40: 471-501 (1989).
    • (1989) Plant Mol Biol , vol.40 , pp. 471-501
    • Keegstra, K.1    Olsen, L.J.2    Theg, S.M.3
  • 22
    • 0028914004 scopus 로고
    • Adherence to the first-AUG rule when a second AUG codon follows closely upon the first
    • Kozak M: Adherence to the first-AUG rule when a second AUG codon follows closely upon the first. Proc Natl Acad Sci USA 92: 2662-2666 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2662-2666
    • Kozak, M.1
  • 23
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak M: The scanning model for translation: an update. J Cell Biol 108: 229-235 (1989).
    • (1989) J Cell Biol , vol.108 , pp. 229-235
    • Kozak, M.1
  • 24
    • 0025980693 scopus 로고
    • The maize regulatory locus Opaque-2 encodes a DNA-binding protein which activates the transcription of the b-32 gene
    • Lohmer S, Maddaloni M, Motto M, Di Fonzo N, Hartings H, Salamini F, Thompson RD: The maize regulatory locus Opaque-2 encodes a DNA-binding protein which activates the transcription of the b-32 gene. EMBO J 10: 617-624 (1991).
    • (1991) EMBO J , vol.10 , pp. 617-624
    • Lohmer, S.1    Maddaloni, M.2    Motto, M.3    Di Fonzo, N.4    Hartings, H.5    Salamini, F.6    Thompson, R.D.7
  • 25
    • 0021199211 scopus 로고
    • Familial hyperlysinemias: Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with LKR and SDH activities
    • Markovitz PJ, Chuang DT: Familial hyperlysinemias: purification and characterization of the bifunctional aminoadipic semialdehyde synthase with LKR and SDH activities. J Biol Chem 259: 11643-11646 (1984).
    • (1984) J Biol Chem , vol.259 , pp. 11643-11646
    • Markovitz, P.J.1    Chuang, D.T.2
  • 26
    • 0001210633 scopus 로고
    • Amino acid metabolism
    • Miflin BJ (ed) Amino Acids and Derivatives. Academic Press, New York
    • Mazelis M. Amino acid metabolism. In: Miflin BJ (ed) Amino Acids and Derivatives, pp. 541-567. The Biochemistry of Plants, vol. 5. Academic Press, New York (1980).
    • (1980) The Biochemistry of Plants , vol.5 , pp. 541-567
    • Mazelis, M.1
  • 27
    • 0006914596 scopus 로고
    • Photosynthetic formation of the aspartate family of amino acids in isolated chloroplasts
    • Mills WR, Lea PJ, Miflin BJ: Photosynthetic formation of the aspartate family of amino acids in isolated chloroplasts. Plant Physiol 65: 1166-1172 (1980).
    • (1980) Plant Physiol , vol.65 , pp. 1166-1172
    • Mills, W.R.1    Lea, P.J.2    Miflin, B.J.3
  • 28
    • 0017886563 scopus 로고
    • Purification and characterization of saccharopine dehydrogenase from baker's yeast
    • Ogawa H, Fujioka M: Purification and characterization of saccharopine dehydrogenase from baker's yeast. Biol Chem 253: 3666-3670 (1978).
    • (1978) Biol Chem , vol.253 , pp. 3666-3670
    • Ogawa, H.1    Fujioka, M.2
  • 30
    • 0030293564 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a gene that encodes a MYC-related protein in Arabidopsis
    • Urao T, Yamaguchi-Shinozaki K, Mitsukawa N, Shibata D, Shinozaki K: Molecular cloning and characterization of a gene that encodes a MYC-related protein in Arabidopsis. Plant Mol Biol 32: 571-576 (1996).
    • (1996) Plant Mol Biol , vol.32 , pp. 571-576
    • Urao, T.1    Yamaguchi-Shinozaki, K.2    Mitsukawa, N.3    Shibata, D.4    Shinozaki, K.5
  • 31
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • Von Heijne G, Steppuhn J, Hermann RG: Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180: 535-545 (1989).
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Hermann, R.G.3
  • 32
    • 0027598473 scopus 로고
    • Identification and expression of a cDNA from Daucus carota encoding a bifunctional aspartokinase-homoserine dehydrogenase
    • Weisemann JM, Matthews BF: Identification and expression of a cDNA from Daucus carota encoding a bifunctional aspartokinase-homoserine dehydrogenase. Plant Mol Biol 22: 301-312 (1993).
    • (1993) Plant Mol Biol , vol.22 , pp. 301-312
    • Weisemann, J.M.1    Matthews, B.F.2
  • 33
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga RK, Terpstra P, Hol WMG: Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J Mol Biol 187: 101-107 (1986).
    • (1986) J Mol Biol , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.M.G.3
  • 34
    • 0025073498 scopus 로고
    • Overlapping reading frames in the LYS5 locus in the yeast Yarrowia lipolytica
    • Yuan J-W, Fournier P, Declerck N, Chasles M, Gaillardin C: Overlapping reading frames in the LYS5 locus in the yeast Yarrowia lipolytica. Mol Cell Biol 10: 4795-4806 (1990).
    • (1990) Mol Cell Biol , vol.10 , pp. 4795-4806
    • Yuan, J.-W.1    Fournier, P.2    Declerck, N.3    Chasles, M.4    Gaillardin, C.5


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