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Volumn 47, Issue 8, 1999, Pages 3345-3351

Pesticide inactivation of peanut glutamate dehydrogenase: Biochemical basis of the enzyme's isomerization

Author keywords

Arachis hypogaea; Degradation; Glutamate dehydrogenase; Immunoanalysis; Isomerization; Pesticides

Indexed keywords

BENTAZON; CARBARIL; CHLOROTHALONIL; GLUTAMATE DEHYDROGENASE; PESTICIDE; PROTEINASE;

EID: 0032829928     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf980531v     Document Type: Article
Times cited : (6)

References (55)
  • 1
    • 0343905497 scopus 로고
    • Evidence for ammonium-dependent de novo synthesis of glutamate dehydrogenase in detached oat leaves
    • Barash, I.; Mor, H.; Sadon, T. Evidence for ammonium-dependent de novo synthesis of glutamate dehydrogenase in detached oat leaves. Plant Physiol. 1975, 56, 856-858.
    • (1975) Plant Physiol. , vol.56 , pp. 856-858
    • Barash, I.1    Mor, H.2    Sadon, T.3
  • 2
    • 0029989147 scopus 로고    scopus 로고
    • The central role of amino acids on nitrogen utilization and plant growth
    • Barneix, A. J.; Causin, H. F. The central role of amino acids on nitrogen utilization and plant growth. J. Plant Physiol. 1996, 149, 358-362.
    • (1996) J. Plant Physiol. , vol.149 , pp. 358-362
    • Barneix, A.J.1    Causin, H.F.2
  • 3
    • 0000104680 scopus 로고
    • Glutamine synthetase isoenzymes of Phaseolus vulgaris L.: Subunit composition in developing root nodules and plumules
    • Bennett, M. J.; Cullimore, J. V. Glutamine synthetase isoenzymes of Phaseolus vulgaris L.: subunit composition in developing root nodules and plumules. Planta 1989, 179, 433-440.
    • (1989) Planta , vol.179 , pp. 433-440
    • Bennett, M.J.1    Cullimore, J.V.2
  • 4
    • 0015818265 scopus 로고
    • Mechanism of inactivation of L-glutamate dehydrogenase by pyridoxal and pyridoxal phosphate
    • Brown, A.; Culver, J. M.; Fisher, H. F. Mechanism of inactivation of L-glutamate dehydrogenase by pyridoxal and pyridoxal phosphate. Biochemistry 1973, 12, 4367-4374.
    • (1973) Biochemistry , vol.12 , pp. 4367-4374
    • Brown, A.1    Culver, J.M.2    Fisher, H.F.3
  • 5
    • 0001031722 scopus 로고
    • A study of the role of glutamate dehydrogenase in the nitrogen metabolism of Arabidopsis thaliana
    • Cammaerts, D.; Jacobs, M. A study of the role of glutamate dehydrogenase in the nitrogen metabolism of Arabidopsis thaliana. Planta 1985, 163, 517-526.
    • (1985) Planta , vol.163 , pp. 517-526
    • Cammaerts, D.1    Jacobs, M.2
  • 6
    • 0015500319 scopus 로고
    • Ultraviolet spectrophotometric characterization of a glutamate dehydrogenase-reduced coenzyme-α-ketoglutarate complex
    • Cross, D. G. Ultraviolet spectrophotometric characterization of a glutamate dehydrogenase-reduced coenzyme-α-ketoglutarate complex. J. Biol. Chem. 1972, 247, 784-789.
    • (1972) J. Biol. Chem. , vol.247 , pp. 784-789
    • Cross, D.G.1
  • 7
    • 0014962169 scopus 로고
    • The mechanism of glutamate dehydrogenase reaction. III. The binding of ligands at multiple subsites and resulting kinetic effects
    • Cross, D. G.; Fisher, H. F. The mechanism of glutamate dehydrogenase reaction. III. The binding of ligands at multiple subsites and resulting kinetic effects. J. Biol. Chem. 1970, 245, 2612-2621.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2612-2621
    • Cross, D.G.1    Fisher, H.F.2
  • 8
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. General aspects
    • Davies, K. J. A. Protein damage and degradation by oxygen radicals. I. General aspects. J. Biol. Chem. 1987, 262, 9895-9901.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 9
    • 0023655449 scopus 로고
    • Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein
    • Davies, K. J. A.; Lin, S. W.; Pacifici, R. E. Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein. J. Biol. Chem. 1987, 262, 9914-9920.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9914-9920
    • Davies, K.J.A.1    Lin, S.W.2    Pacifici, R.E.3
  • 11
    • 0000037420 scopus 로고
    • Purification and characterization of zein-degrading proteases from endosperm of germinating maize seeds
    • De Barros, E. G.; Larkins, B. A. Purification and characterization of zein-degrading proteases from endosperm of germinating maize seeds. Plant Physiol. 1990, 94, 297-303.
    • (1990) Plant Physiol. , vol.94 , pp. 297-303
    • De Barros, E.G.1    Larkins, B.A.2
  • 12
    • 0001165153 scopus 로고    scopus 로고
    • Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley
    • Desimone, M.; Henke, A.; Wagner, E. Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley. Plant Physiol. 1996, 111, 789-796.
    • (1996) Plant Physiol. , vol.111 , pp. 789-796
    • Desimone, M.1    Henke, A.2    Wagner, E.3
  • 13
    • 0343320584 scopus 로고
    • Herbicide Metabolism
    • Huber, L. A., Bernhaut, K., Eds.; Prentice Hall: Englewood Cliffs, NJ
    • Devine, M. D.; Duke, S. O.; Fedtke, C. Herbicide Metabolism. In Physiology of Herbicide Action; Huber, L. A., Bernhaut, K., Eds.; Prentice Hall: Englewood Cliffs, NJ, 1993; pp 95-112.
    • (1993) Physiology of Herbicide Action , pp. 95-112
    • Devine, M.D.1    Duke, S.O.2    Fedtke, C.3
  • 15
    • 13044266477 scopus 로고
    • Interaction between mitochondrial cytochromes and linoleic acid hydroperoxide
    • Dupont, J.; Rustin, P.; Lance, C. Interaction between mitochondrial cytochromes and linoleic acid hydroperoxide. Plant Physiol. 1982, 69, 1308-1314.
    • (1982) Plant Physiol. , vol.69 , pp. 1308-1314
    • Dupont, J.1    Rustin, P.2    Lance, C.3
  • 16
    • 0037791627 scopus 로고
    • Glutamate dehydrogenase from Vicia faba
    • Fawole, M. O. Glutamate dehydrogenase from Vicia faba. Can. J. Bot. 1977, 55, 1850-1856.
    • (1977) Can. J. Bot. , vol.55 , pp. 1850-1856
    • Fawole, M.O.1
  • 18
    • 0001679509 scopus 로고
    • Lipid hydroperoxide reactivity with proteins and amino acids: A review
    • Gardner, H. W. Lipid hydroperoxide reactivity with proteins and amino acids: A review. J. Agric. Food Chem. 1979, 27, 220-229.
    • (1979) J. Agric. Food Chem. , vol.27 , pp. 220-229
    • Gardner, H.W.1
  • 20
    • 13044267828 scopus 로고
    • Endogenously and exogenously caused alteration of the isoenzyme pattern of NAD-specific glutamate dehydrogenase in shoots of Pisum sativum
    • Hartmann, T. Endogenously and exogenously caused alteration of the isoenzyme pattern of NAD-specific glutamate dehydrogenase in shoots of Pisum sativum. Planta 1973, 111, 129-136.
    • (1973) Planta , vol.111 , pp. 129-136
    • Hartmann, T.1
  • 21
    • 0010273348 scopus 로고
    • Organ specific multiple forms of glutamate dehydrogenase in Medicago sativa
    • Hartmann, T.; Nagel, M.; Ilert, H.-I. Organ specific multiple forms of glutamate dehydrogenase in Medicago sativa. Planta 1973, 111, 119-128.
    • (1973) Planta , vol.111 , pp. 119-128
    • Hartmann, T.1    Nagel, M.2    Ilert, H.-I.3
  • 22
    • 0001107410 scopus 로고
    • Glutamine synthetase genes are regulated by ammonia provided externally or symbiotic nitrogen fixation
    • Hirel, B.; Bouet, C.; King, B.; Layzell, D.; Jacobs, F.; Verma, D. P. S. Glutamine synthetase genes are regulated by ammonia provided externally or symbiotic nitrogen fixation. EMBO J. 1987, 6, 1167-1171.
    • (1987) EMBO J. , vol.6 , pp. 1167-1171
    • Hirel, B.1    Bouet, C.2    King, B.3    Layzell, D.4    Jacobs, F.5    Verma, D.P.S.6
  • 23
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser, M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 1995, 7, 215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 24
    • 84981632688 scopus 로고
    • Inducible formation of glutamate dehydrogenase in rice plant roots by the addition of ammonia to the media
    • Kanamori, T.; Konishi, S.; Takahashi, E. Inducible formation of glutamate dehydrogenase in rice plant roots by the addition of ammonia to the media. Physiol. Plant. 1972, 26, 1-6.
    • (1972) Physiol. Plant. , vol.26 , pp. 1-6
    • Kanamori, T.1    Konishi, S.2    Takahashi, E.3
  • 25
    • 84989763142 scopus 로고
    • Activity profiles of enzymes involved in glutamine and glutamate metabolism in the apple during autumnal senescence
    • Rang, S. M.; Titus, J. S. Activity profiles of enzymes involved in glutamine and glutamate metabolism in the apple during autumnal senescence. Physiol. Plant. 1980, 50, 291-297.
    • (1980) Physiol. Plant. , vol.50 , pp. 291-297
    • Rang, S.M.1    Titus, J.S.2
  • 26
    • 0003127788 scopus 로고
    • Changes in the activities of enzymes involved in amino acid metabolism during the senescence of detached wheat leaves
    • Kar, M.; Feierabend, J. Changes in the activities of enzymes involved in amino acid metabolism during the senescence of detached wheat leaves. Plant Physiol. 1984, 62, 39-44.
    • (1984) Plant Physiol. , vol.62 , pp. 39-44
    • Kar, M.1    Feierabend, J.2
  • 27
    • 0002539435 scopus 로고
    • Herbicide-induced radical damage and antioxidative systems
    • Boger, P., Sandmann, G., Eds.; CRC Press: Boca Raton, FL, Chapter 3
    • Kunert, K. J.; Dodge, A. D. Herbicide-induced radical damage and antioxidative systems. In Target Sites of Herbicide Action; Boger, P., Sandmann, G., Eds.; CRC Press: Boca Raton, FL, 1989; Chapter 3.
    • (1989) Target Sites of Herbicide Action
    • Kunert, K.J.1    Dodge, A.D.2
  • 28
    • 85032068659 scopus 로고
    • Identification of the ammonium dependent isoenzyme of glutamate dehydrogenase as the form induced by senescence or darkness stress in the first leaf of wheat
    • Lauriere, C.; Daussant, J. Identification of the ammonium dependent isoenzyme of glutamate dehydrogenase as the form induced by senescence or darkness stress in the first leaf of wheat. Physiol. Plant. 1983, 58, 89-92.
    • (1983) Physiol. Plant. , vol.58 , pp. 89-92
    • Lauriere, C.1    Daussant, J.2
  • 29
    • 0842293215 scopus 로고
    • Glutamate dehydrogenase in the first leaf of wheat. I. Antigenic polymorphism
    • Lauriere, C.; Weisman, N.; Daussant, J. Glutamate dehydrogenase in the first leaf of wheat. I. Antigenic polymorphism. Physiol. Plant. 1981, 52, 146-150.
    • (1981) Physiol. Plant. , vol.52 , pp. 146-150
    • Lauriere, C.1    Weisman, N.2    Daussant, J.3
  • 30
    • 0016313599 scopus 로고
    • Alternate route for nitrogen assimilation in higher plants
    • Lea, P. J.; Miflin, B. J. Alternate route for nitrogen assimilation in higher plants. Nature 1974, 251, 614-616.
    • (1974) Nature , vol.251 , pp. 614-616
    • Lea, P.J.1    Miflin, B.J.2
  • 31
    • 13044256504 scopus 로고
    • Glutamate dehydrogenase isoenzymes in Ricinus communis seedlings
    • Lee, D. W. Glutamate dehydrogenase isoenzymes in Ricinus communis seedlings. Phytochemistry 1973, 12, 2631-2634.
    • (1973) Phytochemistry , vol.12 , pp. 2631-2634
    • Lee, D.W.1
  • 32
    • 0001446787 scopus 로고
    • Plant NADH-glutamate dehydrogenase consists of two subunit polypeptides and their participation in the seven isoenzymes occurs in an ordered ratio
    • Loulakakis, K. A.; Roubelakis-Angelakis, K. A. Plant NADH-glutamate dehydrogenase consists of two subunit polypeptides and their participation in the seven isoenzymes occurs in an ordered ratio. Plant Physiol. 1991, 97, 104-111.
    • (1991) Plant Physiol. , vol.97 , pp. 104-111
    • Loulakakis, K.A.1    Roubelakis-Angelakis, K.A.2
  • 35
    • 13044264575 scopus 로고
    • Glutamate dehydrogenase characteristics in the organs and root nodules of Lupinus luteus L.
    • Mazurowa, H.; Ratajezak, W.; Ratajczak, L. Glutamate dehydrogenase characteristics in the organs and root nodules of Lupinus luteus L. Acta Physiol. Plant. 1980, 2, 167-177.
    • (1980) Acta Physiol. Plant. , vol.2 , pp. 167-177
    • Mazurowa, H.1    Ratajezak, W.2    Ratajczak, L.3
  • 36
    • 0030029406 scopus 로고    scopus 로고
    • Arabidopsis mutant analysis and gene regulation define nonredundant role for glutamate dehydrogenase in nitrogen assimilation
    • Melo-Oliveira, R.; Oliveira, I. C.; Coruzzi, G. M. Arabidopsis mutant analysis and gene regulation define nonredundant role for glutamate dehydrogenase in nitrogen assimilation. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 4718-4723.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4718-4723
    • Melo-Oliveira, R.1    Oliveira, I.C.2    Coruzzi, G.M.3
  • 37
    • 0542358704 scopus 로고    scopus 로고
    • Peanut glutamate dehydrogenase: A target site of herbicide action
    • Ando, T., Fujita, K., Mae, T., Matsumoto, H., Mon, S., Sekiya, J., Eds.; Kluwer Academic Press: London
    • Osuji, G. O. Peanut glutamate dehydrogenase: A target site of herbicide action. In Plant nutrition for sustainable food production and environment; Ando, T., Fujita, K., Mae, T., Matsumoto, H., Mon, S., Sekiya, J., Eds.; Kluwer Academic Press: London, 1997; pp 845-850.
    • (1997) Plant Nutrition for Sustainable Food Production and Environment , pp. 845-850
    • Osuji, G.O.1
  • 38
    • 0032882817 scopus 로고    scopus 로고
    • Signaling by glutamate dehydrogenase in response to pesticide and fertilizer nitrogen treatments of peanut (Arachis hypogaea L.)
    • Osuji, G. O.; Braithwaite, C. Signaling by glutamate dehydrogenase in response to pesticide and fertilizer nitrogen treatments of peanut (Arachis hypogaea L.). J. Agric. Food Chem. 1999, 47, 3332-3344.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 3332-3344
    • Osuji, G.O.1    Braithwaite, C.2
  • 39
    • 0011353622 scopus 로고
    • Effects of α-ketoglutarate on the activities of glutamate synthase, glutamate dehydrogenase, and aspartate transaminase of sweet potato, yam tuber, and cream pea
    • Osuji, G. O.; Cuero, R. G. Effects of α-ketoglutarate on the activities of glutamate synthase, glutamate dehydrogenase, and aspartate transaminase of sweet potato, yam tuber, and cream pea. J. Agric. Food Chem. 1991, 39, 1590-1596.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 1590-1596
    • Osuji, G.O.1    Cuero, R.G.2
  • 40
    • 0027046418 scopus 로고
    • Carboxymethylchitosan enhancement of the storage protein contents of maize seeds (Zea mays L.)
    • Osuji, G. O.; Cuero, R. G. N-Carboxymethylchitosan enhancement of the storage protein contents of maize seeds (Zea mays L.). Food Biotechnol. 1992, 6, 597-610.
    • (1992) Food Biotechnol. , vol.6 , pp. 597-610
    • Osuji, G.O.1    Cuero, R.G.N.2
  • 41
    • 0028896108 scopus 로고
    • Ammonium ion-dependent isomerization of glutamate dehydrogenase in relation to glutamate synthesis in maize
    • Osuji, G. O.; Madu, W. C. Ammonium ion-dependent isomerization of glutamate dehydrogenase in relation to glutamate synthesis in maize. Phytochemistry 1995, 39, 495-503.
    • (1995) Phytochemistry , vol.39 , pp. 495-503
    • Osuji, G.O.1    Madu, W.C.2
  • 42
    • 0030207717 scopus 로고    scopus 로고
    • Ammonium ion salvage by glutamate dehydrogenase during defence response in maize
    • Osuji G. O.; Madu, W. C. Ammonium ion salvage by glutamate dehydrogenase during defence response in maize. Phytochemistry 1996, 42, 1491-1498.
    • (1996) Phytochemistry , vol.42 , pp. 1491-1498
    • Osuji, G.O.1    Madu, W.C.2
  • 43
    • 0031281306 scopus 로고    scopus 로고
    • Regulation of peanut glutamate dehydrogenase by methionine sulphoximine
    • Osuji, G. O.; Madu, W. C. Regulation of peanut glutamate dehydrogenase by methionine sulphoximine. Phytochemistry 1997a, 46, 817-825.
    • (1997) Phytochemistry , vol.46 , pp. 817-825
    • Osuji, G.O.1    Madu, W.C.2
  • 44
    • 0030847637 scopus 로고    scopus 로고
    • Regulation of sweetpotato growth and differentiation by glutamate dehydrogenase
    • Osuji, G. O.; Madu, W. C. Regulation of sweetpotato growth and differentiation by glutamate dehydrogenase. Can. J. Bot. 1997b, 75, 1070-1078.
    • (1997) Can. J. Bot. , vol.75 , pp. 1070-1078
    • Osuji, G.O.1    Madu, W.C.2
  • 45
    • 0007051453 scopus 로고    scopus 로고
    • Glutamate dehydrogenase isomerization: A simple method for diagnosing nitrogen, phosphorus, and potassium sufficiency in maize (Zea mays L)
    • Osuji, G. O.; Reyes, J. C.; Mangaroo, A. S. Glutamate dehydrogenase isomerization: A simple method for diagnosing nitrogen, phosphorus, and potassium sufficiency in maize (Zea mays L). J. Agric. Food Chem. 1998, 46, 2395-2401.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 2395-2401
    • Osuji, G.O.1    Reyes, J.C.2    Mangaroo, A.S.3
  • 46
    • 0018990321 scopus 로고
    • Plant NAD-dependent glutamate dehydrogenase, purification, molecular properties, and metal ion activation of the enzymes from Lemnar minor and Pisum sativum
    • Scheid, H.-W.; Ehmke, A.; Hartmann, T. Plant NAD-dependent glutamate dehydrogenase, purification, molecular properties, and metal ion activation of the enzymes from Lemnar minor and Pisum sativum. Z. Naturforsch. 1980, 35c, 213-221.
    • (1980) Z. Naturforsch. , vol.35 C , pp. 213-221
    • Scheid, H.-W.1    Ehmke, A.2    Hartmann, T.3
  • 48
    • 0000771331 scopus 로고
    • Nitrogen redistribution during grain growth in wheat (Triticum aestivum L.). III. Enzymology and transport of amino acids from senescing flag leaves
    • Simpson, R. J.; Bailing, M. J. Nitrogen redistribution during grain growth in wheat (Triticum aestivum L.). III. Enzymology and transport of amino acids from senescing flag leaves. Planta 1981, 157, 447-456.
    • (1981) Planta , vol.157 , pp. 447-456
    • Simpson, R.J.1    Bailing, M.J.2
  • 49
    • 0348023685 scopus 로고
    • Regulation of glutamate dehydrogenase activity by amino acids in maize seedlings
    • Singh, R. P.; Srivastava, H. S. Regulation of glutamate dehydrogenase activity by amino acids in maize seedlings. Physiol. Plant. 1983, 57, 549-554.
    • (1983) Physiol. Plant. , vol.57 , pp. 549-554
    • Singh, R.P.1    Srivastava, H.S.2
  • 50
    • 0000790558 scopus 로고
    • Glutamate dehydrogenase
    • Boyer, P. D., Ed.; Academic Press: New York, Chapter 5
    • Smith, E. L.; Austen, B. M.; Blumenthal, K. M.; Nyc, J. F. Glutamate dehydrogenase. In Enzymes; Boyer, P. D., Ed.; Academic Press: New York, 1975; Vol. 2, Chapter 5.
    • (1975) Enzymes , vol.2
    • Smith, E.L.1    Austen, B.M.2    Blumenthal, K.M.3    Nyc, J.F.4
  • 51
    • 0001141677 scopus 로고
    • Role and regulation of L-glutamate dehydrogenase activity in higher plants
    • Srivastava, H. S.; Singh, R. P. Role and regulation of L-glutamate dehydrogenase activity in higher plants. Phytochemistry 1987, 26, 597-610.
    • (1987) Phytochemistry , vol.26 , pp. 597-610
    • Srivastava, H.S.1    Singh, R.P.2
  • 52
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman, E. R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 1993, 62, 797-410.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-1410
    • Stadtman, E.R.1
  • 53
    • 0001461290 scopus 로고
    • Enzymes of nitrogen mobilization in detached leaves of Lolium temulentum during senescence
    • Thomas, H. Enzymes of nitrogen mobilization in detached leaves of Lolium temulentum during senescence. Planta 1978, 142, 161-169.
    • (1978) Planta , vol.142 , pp. 161-169
    • Thomas, H.1
  • 54
    • 78651007343 scopus 로고
    • The use of azoalbumin as a substrate in the colorimetric determination of peptic and tryptic activity
    • Tomarelli, R. M.; Charney, J.; Harding, M. L. The use of azoalbumin as a substrate in the colorimetric determination of peptic and tryptic activity. J. Lab. Clin. Med. 1949, 34, 428-433.
    • (1949) J. Lab. Clin. Med. , vol.34 , pp. 428-433
    • Tomarelli, R.M.1    Charney, J.2    Harding, M.L.3
  • 55
    • 0344730413 scopus 로고
    • Isoenzymes of glutamate dehydrogenase in plants
    • Yue, S. B. Isoenzymes of glutamate dehydrogenase in plants. Plant Physiol. 1969, 44, 453-457.
    • (1969) Plant Physiol. , vol.44 , pp. 453-457
    • Yue, S.B.1


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