메뉴 건너뛰기




Volumn 53, Issue 5, 2005, Pages 1791-1798

Isolation and characterization of enzymes involved in lysine catabolism from sorghum seeds

Author keywords

Aspartate kinase; Lysine; Lysine 2 oxoglutarate reductase; Maize; Saccharopine dehydrogenase

Indexed keywords

2 OXOGLUTARATE REDUCTASE; ASPARTIC ACID; ESSENTIAL AMINO ACID; LYSINE; OXIDOREDUCTASE; SACCHAROPINE DEHYDROGENASE; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 14644390873     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf048525o     Document Type: Article
Times cited : (12)

References (46)
  • 1
    • 0031664235 scopus 로고    scopus 로고
    • Discovery of grain sorghum germplasm with high uncooked and cooked in vitro protein digestibilities
    • Weaver, A. C.; Hamaker, B. R.; Axtell, J. D. Discovery of grain sorghum germplasm with high uncooked and cooked in vitro protein digestibilities. Cereal Chem. 1998, 75, 665-670.
    • (1998) Cereal Chem. , vol.75 , pp. 665-670
    • Weaver, A.C.1    Hamaker, B.R.2    Axtell, J.D.3
  • 2
    • 0001492463 scopus 로고
    • High lysine mutant gene (hl) that improves protein quality and biological value of grain sorghum
    • Singh, R.; Axtell, J. D. High lysine mutant gene (hl) that improves protein quality and biological value of grain sorghum. Crop Sci. 1973, 13, 535-539.
    • (1973) Crop Sci. , vol.13 , pp. 535-539
    • Singh, R.1    Axtell, J.D.2
  • 3
    • 1442314010 scopus 로고    scopus 로고
    • The influence of nitrogen supply on antioxidant enzymes in plant roots
    • Medici, L. O.; Azevedo, R. A.; Smith, R. J.; Lea, P. J. The influence of nitrogen supply on antioxidant enzymes in plant roots. Funct. Plant Biol. 2004, 31, 1-9.
    • (2004) Funct. Plant Biol. , vol.31 , pp. 1-9
    • Medici, L.O.1    Azevedo, R.A.2    Smith, R.J.3    Lea, P.J.4
  • 4
    • 2542553368 scopus 로고    scopus 로고
    • Primary products: Amino acids
    • Thomas, B., Murphy, D. J., Murray, B. G., Eds.; Elsevier/Academic Press: New York
    • Lea, P. J.; Azevedo, R. A. Primary products: amino acids. In Encyclopedia of Applied Plant Sciences; Thomas, B., Murphy, D. J., Murray, B. G., Eds.; Elsevier/Academic Press: New York, 2003; pp 871-883.
    • (2003) Encyclopedia of Applied Plant Sciences , pp. 871-883
    • Lea, P.J.1    Azevedo, R.A.2
  • 5
    • 0031260404 scopus 로고    scopus 로고
    • The biosynthesis and metabolism of the aspartate derived amino acids in higher plants
    • Azevedo, R. A.; Arruda, P.; Turner, W. L.; Lea, P. J. The biosynthesis and metabolism of the aspartate derived amino acids in higher plants. Phytochemistry 1997, 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
  • 6
    • 0035094676 scopus 로고    scopus 로고
    • Lysine metabolism in higher plants
    • Azevedo, R. A.; Lea, P. J. Lysine metabolism in higher plants. Amino Acids 2001, 20, 261-279.
    • (2001) Amino Acids , vol.20 , pp. 261-279
    • Azevedo, R.A.1    Lea, P.J.2
  • 7
    • 0036331751 scopus 로고    scopus 로고
    • Metabolic engineering of amino acids and storage proteins in plants
    • Galili, G.; Hofgen, R. Metabolic engineering of amino acids and storage proteins in plants. Metabolic Eng. 2002, 4, 3-11.
    • (2002) Metabolic Eng. , vol.4 , pp. 3-11
    • Galili, G.1    Hofgen, R.2
  • 8
    • 0028795414 scopus 로고
    • Threonine accumulation in a mutant of Arabidopsis thaliana (L.) Heynt. with an altered aspartate kinase
    • Heremans, B.; Jacobs, M. Threonine accumulation in a mutant of Arabidopsis thaliana (L.) Heynt. with an altered aspartate kinase. J. Plant Physiol. 1995, 146, 249-257.
    • (1995) J. Plant Physiol. , vol.146 , pp. 249-257
    • Heremans, B.1    Jacobs, M.2
  • 9
    • 0032560569 scopus 로고    scopus 로고
    • The specific features of methionine biosynthesis and metabolism in plants
    • Ravanel, S.; Gakiere, B.; Job, D.; Douce, R. The specific features of methionine biosynthesis and metabolism in plants. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 7805-7812.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7805-7812
    • Ravanel, S.1    Gakiere, B.2    Job, D.3    Douce, R.4
  • 11
    • 0009019901 scopus 로고    scopus 로고
    • Increasing lysine in corn
    • Falco, S. C. Increasing lysine in corn. Amino Acids 2001, 21, 57-58.
    • (2001) Amino Acids , vol.21 , pp. 57-58
    • Falco, S.C.1
  • 12
    • 0034776257 scopus 로고    scopus 로고
    • Constitutive and seed-specific expression of a maize lysine-feedback- insensitive dihydrodipicolinate synthase gene leads to increased free lysine in rice seeds
    • Lee, S. I.; Kim, H. U.; Lee, Y. H.; Suh, S. C.; Lim, Y. P.; Lee, H. Y.; Kim, H. I. Constitutive and seed-specific expression of a maize lysine-feedback-insensitive dihydrodipicolinate synthase gene leads to increased free lysine in rice seeds. Mol. Breed. 2001, 8, 75-84.
    • (2001) Mol. Breed. , vol.8 , pp. 75-84
    • Lee, S.I.1    Kim, H.U.2    Lee, Y.H.3    Suh, S.C.4    Lim, Y.P.5    Lee, H.Y.6    Kim, H.I.7
  • 14
    • 0030612052 scopus 로고    scopus 로고
    • A mutant of (Arabidopsis thaliana L.) Heynh. with modified control of aspartate kinase by threonine
    • Heremans, B.; Jacobs, M. A mutant of (Arabidopsis thaliana L.) Heynh. with modified control of aspartate kinase by threonine. Biochem. Genet. 1997, 35, 139-153.
    • (1997) Biochem. Genet. , vol.35 , pp. 139-153
    • Heremans, B.1    Jacobs, M.2
  • 15
    • 0001593858 scopus 로고
    • Threonine overproduction in transgenic tobacco plants expressing a mutant desensitized aspartate kinase of Escherichia coli
    • Shaul, O.; Galili, G. Threonine overproduction in transgenic tobacco plants expressing a mutant desensitized aspartate kinase of Escherichia coli. Plant Physiol. 1992, 100, 1157-1163.
    • (1992) Plant Physiol. , vol.100 , pp. 1157-1163
    • Shaul, O.1    Galili, G.2
  • 16
    • 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. Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feedback-insensitive aspartate kinase and dihydrodipicolinate synthase. Plant Mol. Biol. 1993, 23, 759-768.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 759-768
    • Shaul, O.1    Galili, G.2
  • 17
    • 0030293719 scopus 로고    scopus 로고
    • Engineering of the aspartate family biosynthetic pathway in barley (Hordeum vulgare L.) by transformation with heterologous genes encoding feedback-insensitive aspartate kinase and dihydrodipicolinate synthase
    • Brinch-Pedersen, H.; Galili, G.; Knudsen, S.; Holm, P. B. Engineering of the aspartate family biosynthetic pathway in barley (Hordeum vulgare L.) by transformation with heterologous genes encoding feedback-insensitive aspartate kinase and dihydrodipicolinate synthase. Plant Mol. Biol. 1996, 32, 611-620.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 611-620
    • Brinch-Pedersen, H.1    Galili, G.2    Knudsen, S.3    Holm, P.B.4
  • 23
    • 0035989811 scopus 로고    scopus 로고
    • Analysis of the aspartic acid metabolic pathway using mutant genes
    • Azevedo, R. A. Analysis of the aspartic acid metabolic pathway using mutant genes. Amino Acids 2002, 22, 217-230.
    • (2002) Amino Acids , vol.22 , pp. 217-230
    • Azevedo, R.A.1
  • 24
    • 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.; Galili, G. 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 2003, 15, 845-853.
    • (2003) Plant Cell , vol.15 , pp. 845-853
    • Zhu, X.1    Galili, G.2
  • 26
    • 0001247558 scopus 로고
    • Lysine-ketoglutarate reductase activity in developing maize endosperm
    • Arruda, P.; Sodek, L.; Silva, W. J. Lysine-ketoglutarate reductase activity in developing maize endosperm. Plant Physiol. 1982, 69, 988-989.
    • (1982) Plant Physiol. , vol.69 , pp. 988-989
    • Arruda, P.1    Sodek, L.2    Silva, W.J.3
  • 27
    • 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. Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase saccharopine dehydrogenase from maize. Plant Physiol. 1996, 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
  • 28
    • 0034047474 scopus 로고    scopus 로고
    • Purification and characterization of bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase from developing soybean seeds
    • Miron, D.; Ben-Yaacov, S.; Reches, D.; Schupper, A.; Galili, G. Purification and characterization of bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase from developing soybean seeds. Plant Physiol. 2000, 123, 665-663.
    • (2000) Plant Physiol. , vol.123 , pp. 665-663
    • Miron, D.1    Ben-Yaacov, S.2    Reches, D.3    Schupper, A.4    Galili, G.5
  • 29
    • 0036739759 scopus 로고    scopus 로고
    • The bifunctional LKRISDH locus of plants also encodes a highly active monofunctional lysine-ketoglutarate reductase using a polyadenylation signal located within an intron
    • Tang, G.; Zhu, X.; Gakiere, B.; Levanony, H.; Kahana, A.; Galili, G. The bifunctional LKRISDH locus of plants also encodes a highly active monofunctional lysine-ketoglutarate reductase using a polyadenylation signal located within an intron. Plant Physiol. 2002, 130, 147-154.
    • (2002) Plant Physiol. , vol.130 , pp. 147-154
    • Tang, G.1    Zhu, X.2    Gakiere, B.3    Levanony, H.4    Kahana, A.5    Galili, G.6
  • 30
    • 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 polypeptide
    • Gaziola, S. A.; Teixeira, C. M. G.; Lugli, J.; Sodek, L.; Azevedo, R. A. The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate/saccharopine dehydrogenase bifunctional polypeptide. Eur. J. Biochem. 1997, 247, 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
  • 32
    • 0031467950 scopus 로고    scopus 로고
    • In vitro dephosphorylation inhibits the activity of soybean lysine-oxoglutarate reductase in a lysine-regulated manner
    • Miron, D.; Ben-Yaacov, S.; Karchi, H.; Galili, G. In vitro dephosphorylation inhibits the activity of soybean lysine-oxoglutarate reductase in a lysine-regulated manner. Plant J. 1997, 12, 1453-1458.
    • (1997) Plant J. , vol.12 , pp. 1453-1458
    • Miron, D.1    Ben-Yaacov, S.2    Karchi, H.3    Galili, G.4
  • 33
    • 0032079778 scopus 로고    scopus 로고
    • Structure and regulation of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase in maize
    • Kemper, E. L.; Cord-Neto, G.; Capella, A. N.; Gonçalves-Butruille, M.; Azevedo, R. A.; Arruda, P. Structure and regulation of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase in maize. Eur. J. Biochem. 1998, 253, 720-729.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 720-729
    • Kemper, E.L.1    Cord-Neto, G.2    Capella, A.N.3    Gonçalves-Butruille, M.4    Azevedo, R.A.5    Arruda, P.6
  • 34
    • 0033819985 scopus 로고    scopus 로고
    • Degradation of lysine in rice seeds, effect of calcium, ionic strength, S-adenosylmethionine, and S-2-aminoethyl-L-cysteine on the lysine 2-oxoglutarate reductase-saccharopine dehydrogenase bifunctional enzyme
    • Gaziola, S. A.; Sodek, L.; Arruda, P.; Lea, P. J.; Azevedo, R. A. Degradation of lysine in rice seeds, effect of calcium, ionic strength, S-adenosylmethionine, and S-2-aminoethyl-L-cysteine on the lysine 2-oxoglutarate reductase-saccharopine dehydrogenase bifunctional enzyme. Physiol. Plant. 2000, 110, 164-171.
    • (2000) Physiol. Plant. , vol.110 , pp. 164-171
    • Gaziola, S.A.1    Sodek, L.2    Arruda, P.3    Lea, P.J.4    Azevedo, R.A.5
  • 35
    • 0035043361 scopus 로고    scopus 로고
    • Lysine catabolism: A stress and development super-regulated metabolic pathway
    • Galili, G.; Tang, G.; Zhu, X.; Gakiere, B. Lysine catabolism: a stress and development super-regulated metabolic pathway. Curr. Opin. Plant Biol. 2001, 4, 261-266.
    • (2001) Curr. Opin. Plant Biol. , vol.4 , pp. 261-266
    • Galili, G.1    Tang, G.2    Zhu, X.3    Gakiere, B.4
  • 36
    • 0037147307 scopus 로고    scopus 로고
    • The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains
    • Zhu, X. H.; Tang, G. L.; Galili, G. The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains. J. Biol. Chem. 2002, 277, 49655-49661.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49655-49661
    • Zhu, X.H.1    Tang, G.L.2    Galili, G.3
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 0013968749 scopus 로고
    • Separation and estimation of amino acids in crude plant extracts by thin-layer electrophoresis and chromatography
    • Bieleski, R. L.; Turner, N. Separation and estimation of amino acids in crude plant extracts by thin-layer electrophoresis and chromatography. Anal. Biochem. 1966, 17, 278-293.
    • (1966) Anal. Biochem. , vol.17 , pp. 278-293
    • Bieleski, R.L.1    Turner, N.2
  • 40
    • 37049046128 scopus 로고
    • Estimation of amino acids by ninhydrin
    • Yemm, E. M.; Cocking, E. C. Estimation of amino acids by ninhydrin. Analyst 1955, 80, 209-213.
    • (1955) Analyst , vol.80 , pp. 209-213
    • Yemm, E.M.1    Cocking, E.C.2
  • 41
    • 12444280061 scopus 로고    scopus 로고
    • Isolation of the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase
    • Lima, S. T. C.; Azevedo, R. A.; Santoro, L. G.; Gaziola, S. A.; Lea, P. J. Isolation of the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase. Amino Acids 2003, 24, 179-186.
    • (2003) Amino Acids , vol.24 , pp. 179-186
    • Lima, S.T.C.1    Azevedo, R.A.2    Santoro, L.G.3    Gaziola, S.A.4    Lea, P.J.5
  • 42
    • 0346829881 scopus 로고    scopus 로고
    • Improved procedures for extraction of lysine 2-oxoglutarate reductase/saccharopine dehydrogenase (LOR/SDH) enzyme from Phaseolus vulgaris cultivars
    • Lima, S. T. C.; Azevedo, R. A.; Santoro, L. G. Improved procedures for extraction of lysine 2-oxoglutarate reductase/ saccharopine dehydrogenase (LOR/SDH) enzyme from Phaseolus vulgaris cultivars. New Zeal. J. Crop Hort. Sci. 2003, 31, 261-268.
    • (2003) New Zeal. J. Crop Hort. Sci. , vol.31 , pp. 261-268
    • Lima, S.T.C.1    Azevedo, R.A.2    Santoro, L.G.3
  • 43
    • 0000690359 scopus 로고
    • Partial purification and characterization of lysine-ketoglutarate reductase in normal and opaque-2 maize endosperm
    • Brochetto-Braga, M. R.; Leite, A.; Arruda, P. Partial purification and characterization of lysine-ketoglutarate reductase in normal and opaque-2 maize endosperm. Plant Physiol. 1992, 98, 1139-1147.
    • (1992) Plant Physiol. , vol.98 , pp. 1139-1147
    • Brochetto-Braga, M.R.1    Leite, A.2    Arruda, P.3
  • 44
    • 0030880203 scopus 로고    scopus 로고
    • Electrophoretic profiles and amino acid composition of rice endosperm proteins of a mutant with enhanced lysine and total protein after backcrosses for germplasm improvements
    • Schaeffer, G. W.; Sharpe, F. T. Electrophoretic profiles and amino acid composition of rice endosperm proteins of a mutant with enhanced lysine and total protein after backcrosses for germplasm improvements. Theor. Appl. Genet. 1997, 95, 230-235.
    • (1997) Theor. Appl. Genet. , vol.95 , pp. 230-235
    • Schaeffer, G.W.1    Sharpe, F.T.2
  • 45
    • 14644407066 scopus 로고
    • Barley seed proteins
    • Inglett, G. E., Ed.; The AVI Publishing Company, Inc.: Westport, CT
    • Munck, L. Barley Seed Proteins. In Symposium: Seed Proteins; Inglett, G. E., Ed.; The AVI Publishing Company, Inc.: Westport, CT, 1972, p 144-164.
    • (1972) Symposium: Seed Proteins , pp. 144-164
    • Munck, L.1
  • 46
    • 9944265796 scopus 로고    scopus 로고
    • Hull-less barley varieties: Storage proteins and amino acid distribution in relation to nutritional quality
    • Helm, C. V.; De Francisco, A.; Gaziola, S. A.; Fornazier, R. F.; Pompeu, G. B.; Azevedo, R. A. Hull-less barley varieties: storage proteins and amino acid distribution in relation to nutritional quality. Food Biotechnol. 2004, 18, 327-341.
    • (2004) Food Biotechnol. , vol.18 , pp. 327-341
    • Helm, C.V.1    De Francisco, A.2    Gaziola, S.A.3    Fornazier, R.F.4    Pompeu, G.B.5    Azevedo, R.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.