메뉴 건너뛰기




Volumn 127, Issue 1, 2011, Pages 9-13

Glutamate synthase, but not GABA shunt enzymes, contributes to nitrogen metabolism of the sheep abomasal nematode parasites Haemonchus contortus and Teladorsagia circumcincta

Author keywords

Ammonia assimilation; Glutamate decarboxylase (E.C. 4.1.1.15); Glutamate synthase (E.C. 1.4.1.14); Haemonchus contortus; Succinic semialdehyde dehydrogenase (E.C. 1.2.1.24); Teladorsagia (Ostertagia) circumcincta

Indexed keywords

2 OXOGLUTARIC ACID; AMMONIA; AZASERINE; GLUTAMATE DECARBOXYLASE; GLUTAMATE SYNTHASE; GLUTAMINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NITROGEN; SUCCINATE SEMIALDEHYDE DEHYDROGENASE;

EID: 78650551463     PISSN: 00144894     EISSN: 10902449     Source Type: Journal    
DOI: 10.1016/j.exppara.2010.05.023     Document Type: Article
Times cited : (6)

References (38)
  • 1
    • 0014739411 scopus 로고
    • The operation of the gamma-aminobutyrate bypath of the tricarboxylic acid cycle in brain tissue in vitro
    • Balazs R., Machiyama Y., Hammond B.J., Julian T., Richter D. The operation of the gamma-aminobutyrate bypath of the tricarboxylic acid cycle in brain tissue in vitro. Biochemical Journal 1970, 116:445-446.
    • (1970) Biochemical Journal , vol.116 , pp. 445-446
    • Balazs, R.1    Machiyama, Y.2    Hammond, B.J.3    Julian, T.4    Richter, D.5
  • 2
    • 0017350794 scopus 로고
    • Assay and properties of 4-aminobutyric-2-oxoglutaric acid transaminase and succinic semialdehyde dehydrogenase in rat brain tissue
    • Boer T.D., Bruinvels J. Assay and properties of 4-aminobutyric-2-oxoglutaric acid transaminase and succinic semialdehyde dehydrogenase in rat brain tissue. Journal of Neurochemistry 1977, 28:471-478.
    • (1977) Journal of Neurochemistry , vol.28 , pp. 471-478
    • Boer, T.D.1    Bruinvels, J.2
  • 3
    • 0017703160 scopus 로고
    • Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules
    • Boland M.J., Benny A.G. Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules. European Journal of Biochemistry 1977, 79:355-362.
    • (1977) European Journal of Biochemistry , vol.79 , pp. 355-362
    • Boland, M.J.1    Benny, A.G.2
  • 4
    • 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. Analytical Biochemistry 1976, 72:248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0022510896 scopus 로고
    • Inactivation of glucosamine-6-phosphate synthetase from Salmonella typhimurium LT2 by fumaroyl diaminopropanoic acid derivatives, a novel group of glutamine analogs
    • Chmara H., Andruszkiewicz R., Borowski E. Inactivation of glucosamine-6-phosphate synthetase from Salmonella typhimurium LT2 by fumaroyl diaminopropanoic acid derivatives, a novel group of glutamine analogs. Biochimica et Biophysica Acta 1985, 870:357-366.
    • (1985) Biochimica et Biophysica Acta , vol.870 , pp. 357-366
    • Chmara, H.1    Andruszkiewicz, R.2    Borowski, E.3
  • 6
    • 0016737011 scopus 로고
    • Studies of regulatory metabolism in Moniezia expansa: glutamate, and absence of the γ-aminobutyrate pathway
    • Cornish R.A., Bryant C. Studies of regulatory metabolism in Moniezia expansa: glutamate, and absence of the γ-aminobutyrate pathway. International Journal for Parasitology 1975, 5:355-362.
    • (1975) International Journal for Parasitology , vol.5 , pp. 355-362
    • Cornish, R.A.1    Bryant, C.2
  • 7
    • 0007694934 scopus 로고
    • Occurrence of two forms of glutamate synthase in Chlamydomonas reinhardii
    • Cullimore J.V., Sims A.P. Occurrence of two forms of glutamate synthase in Chlamydomonas reinhardii. Phytochemistry 1981, 20:597-600.
    • (1981) Phytochemistry , vol.20 , pp. 597-600
    • Cullimore, J.V.1    Sims, A.P.2
  • 9
    • 0031666411 scopus 로고    scopus 로고
    • Tricarboxylic acid cycle and anaplerotic enzymes in rhizobia
    • Dunn M.F. Tricarboxylic acid cycle and anaplerotic enzymes in rhizobia. FEMS Microbiology Reviews 1998, 22:105-123.
    • (1998) FEMS Microbiology Reviews , vol.22 , pp. 105-123
    • Dunn, M.F.1
  • 11
    • 0025829437 scopus 로고
    • Purification and characterization of glutamate decarboxylase from Neurospora crassa conidia
    • Hao R., Schmit J.C. Purification and characterization of glutamate decarboxylase from Neurospora crassa conidia. Journal of Biological Chemistry 1991, 266:5135-5139.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 5135-5139
    • Hao, R.1    Schmit, J.C.2
  • 12
    • 84971783493 scopus 로고
    • Nitrogen metabolism in the ovine stomach 4. Nitrogenous components of the abomasal secretions
    • Harrop C.J.F. Nitrogen metabolism in the ovine stomach 4. Nitrogenous components of the abomasal secretions. Journal of Agricultural Science 1974, 83:249-257.
    • (1974) Journal of Agricultural Science , vol.83 , pp. 249-257
    • Harrop, C.J.F.1
  • 13
    • 84971713144 scopus 로고
    • Nitrogen metabolism in the ovine stomach 3. Urea in the abomasal secretions
    • Harrop C.J.F., Phillipson A.T. Nitrogen metabolism in the ovine stomach 3. Urea in the abomasal secretions. Journal of Agricultural Science 1974, 83:237-247.
    • (1974) Journal of Agricultural Science , vol.83 , pp. 237-247
    • Harrop, C.J.F.1    Phillipson, A.T.2
  • 14
    • 0028129875 scopus 로고
    • Why does Escherichia coli have two primary pathways for synthesis of glutamate?
    • Helling R.B. Why does Escherichia coli have two primary pathways for synthesis of glutamate?. Journal of Bacteriology 1994, 176:4664-4668.
    • (1994) Journal of Bacteriology , vol.176 , pp. 4664-4668
    • Helling, R.B.1
  • 15
    • 0036154795 scopus 로고    scopus 로고
    • Speed versus efficiency in microbial growth and the role of parallel pathways
    • Helling R.B. Speed versus efficiency in microbial growth and the role of parallel pathways. Journal of Bacteriology 2002, 184:1041-1045.
    • (2002) Journal of Bacteriology , vol.184 , pp. 1041-1045
    • Helling, R.B.1
  • 16
    • 0032127173 scopus 로고    scopus 로고
    • Purification and characterization of NADH-dependent glutamate synthase from the silkworm fat body (Bombyx mori)
    • Hirayama C., Saito H., Konno K., Shinbo H. Purification and characterization of NADH-dependent glutamate synthase from the silkworm fat body (Bombyx mori). Insect Biochemistry and Molecular Biology 1998, 28:473-482.
    • (1998) Insect Biochemistry and Molecular Biology , vol.28 , pp. 473-482
    • Hirayama, C.1    Saito, H.2    Konno, K.3    Shinbo, H.4
  • 18
    • 0142153893 scopus 로고    scopus 로고
    • Ammonia assimilation by Saccharomyces cerevisiae
    • Magasanik B. Ammonia assimilation by Saccharomyces cerevisiae. Eukaryotic Cell 2003, 2:827-829.
    • (2003) Eukaryotic Cell , vol.2 , pp. 827-829
    • Magasanik, B.1
  • 19
    • 0025834149 scopus 로고
    • Regulation of glutamine synthetase activity in the unicellular cyanobacterium Synechocystis sp. strain PCC 6803 by the nitrogen source: effect of ammonium
    • Mérida A., Candau P., Florencio F.J. Regulation of glutamine synthetase activity in the unicellular cyanobacterium Synechocystis sp. strain PCC 6803 by the nitrogen source: effect of ammonium. Journal of Bacteriology 1991, 173:4095-4100.
    • (1991) Journal of Bacteriology , vol.173 , pp. 4095-4100
    • Mérida, A.1    Candau, P.2    Florencio, F.J.3
  • 20
    • 0036010144 scopus 로고    scopus 로고
    • The role of glutamine synthetase and glutamate dehydrogenase in nitrogen assimilation and possibilities for improvement in the nitrogen utilization of crops
    • Miflin B.J., Habash D.Z. The role of glutamine synthetase and glutamate dehydrogenase in nitrogen assimilation and possibilities for improvement in the nitrogen utilization of crops. Journal of Experimental Botany 2002, 53:979-987.
    • (2002) Journal of Experimental Botany , vol.53 , pp. 979-987
    • Miflin, B.J.1    Habash, D.Z.2
  • 22
    • 37049064296 scopus 로고
    • L-Glutamate-1-carboxylase in intestinal parasites
    • Monteoliva M., Rasero F.S., Gorgé J.L., Mayor F. l-Glutamate-1-carboxylase in intestinal parasites. Nature 1965, 205:1111-1112.
    • (1965) Nature , vol.205 , pp. 1111-1112
    • Monteoliva, M.1    Rasero, F.S.2    Gorgé, J.L.3    Mayor, F.4
  • 27
    • 46549092935 scopus 로고
    • Glutamine synthetase and glutamate synthase from Sclerotinia sclerotiorum
    • Rachim M.A., Nicholas D.J.D. Glutamine synthetase and glutamate synthase from Sclerotinia sclerotiorum. Phytochemistry 1985, 24:2541-2548.
    • (1985) Phytochemistry , vol.24 , pp. 2541-2548
    • Rachim, M.A.1    Nicholas, D.J.D.2
  • 32
    • 0033074893 scopus 로고    scopus 로고
    • Abomasal secretion in sheep receiving adult Ostertagia circumcincta that are prevented from contact with the mucosa
    • Simpson H.V., Simpson B.H., Simcock D.C., Reynolds G.W., Pomroy W.E. Abomasal secretion in sheep receiving adult Ostertagia circumcincta that are prevented from contact with the mucosa. New Zealand Veterinary Journal 1999, 47:20-24.
    • (1999) New Zealand Veterinary Journal , vol.47 , pp. 20-24
    • Simpson, H.V.1    Simpson, B.H.2    Simcock, D.C.3    Reynolds, G.W.4    Pomroy, W.E.5
  • 35
  • 36
    • 0026001607 scopus 로고
    • Pyridoxal 5′-phosphate dependent enzymes in the nematode Nippostrongylus brasiliensis
    • Walker J., Barrett J. Pyridoxal 5′-phosphate dependent enzymes in the nematode Nippostrongylus brasiliensis. International Journal for Parasitology 1991, 21:641-649.
    • (1991) International Journal for Parasitology , vol.21 , pp. 641-649
    • Walker, J.1    Barrett, J.2
  • 37
    • 0021007587 scopus 로고
    • Application of a quick, simple and direct radiometric assay for 4-aminobutyrate: 2-oxoglutarate aminotransferase to studies of the parasitic nematode Nippostrongylus brasiliensis
    • B
    • Watts S.D.M., Atkins A.M. Application of a quick, simple and direct radiometric assay for 4-aminobutyrate: 2-oxoglutarate aminotransferase to studies of the parasitic nematode Nippostrongylus brasiliensis. Comparative Biochemistry and Physiology 1983, 76B:899-906.
    • (1983) Comparative Biochemistry and Physiology , vol.76 , pp. 899-906
    • Watts, S.D.M.1    Atkins, A.M.2
  • 38
    • 0021443531 scopus 로고
    • Kinetics of 4-aminobutyrate:2-oxoglutarate aminotransferase from Nippostrongylus brasiliensis
    • Watts S.D.M., Atkins A.M. Kinetics of 4-aminobutyrate:2-oxoglutarate aminotransferase from Nippostrongylus brasiliensis. Molecular and Biochemical Parasitology 1984, 12:207-216.
    • (1984) Molecular and Biochemical Parasitology , vol.12 , pp. 207-216
    • Watts, S.D.M.1    Atkins, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.