메뉴 건너뛰기




Volumn 24, Issue 3, 2002, Pages 279-283

Effect of selected compounds on the activity of glutamate dehydrogenase from triticale roots

Author keywords

Activators; Divalent metal ions; Glutamate dehydrogenase; Inhibitors; Triticale

Indexed keywords

TRITICOSECALE;

EID: 0036408436     PISSN: 01375881     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11738-002-0052-2     Document Type: Article
Times cited : (2)

References (23)
  • 1
    • 0033428609 scopus 로고    scopus 로고
    • Identification of lysine residue involved in inactivation of brain glutamate dehydrogenase isoproteins by o-phthalaldehyde
    • Ahn J.-Y, Choi S., Cho S.-W. 1999. Identification of lysine residue involved in inactivation of brain glutamate dehydrogenase isoproteins by o-phthalaldehyde. Biochimie 81: 1123-1129.
    • (1999) Biochimie , vol.81 , pp. 1123-1129
    • Ahn, J.-Y.1    Choi, S.2    Cho, S.-W.3
  • 2
    • 0031473278 scopus 로고    scopus 로고
    • Regulation of glutamate dehydrogenase activity by manipulation of nucleotide supply in Daucus carota suspension cultures
    • Athwal G.S., Pearson J., Laurie S. 1997. Regulation of glutamate dehydrogenase activity by manipulation of nucleotide supply in Daucus carota suspension cultures. Physiol. Plant. 101: 503-509.
    • (1997) Physiol. Plant. , vol.101 , pp. 503-509
    • Athwal, G.S.1    Pearson, J.2    Laurie, S.3
  • 3
    • 0015900367 scopus 로고
    • Induction of a specific isoenzyme of glutamate dehydrogenase by ammonia in oat leaves
    • Barash I., Sadon T., Mor H. 1973. Induction of a specific isoenzyme of glutamate dehydrogenase by ammonia in oat leaves. Nature New Biol. 244: 150-152.
    • (1973) Nature New Biol. , vol.244 , pp. 150-152
    • Barash, I.1    Sadon, T.2    Mor, H.3
  • 4
    • 0033677874 scopus 로고    scopus 로고
    • Glutamine synthetase and glutamate dehydrogenase isoforms in maize leaves: Localization, relative proportion and their role in ammonium assimilation or nitrogen transport
    • Becker T.W., Carrayol E., Hirel B. 2000. Glutamine synthetase and glutamate dehydrogenase isoforms in maize leaves: localization, relative proportion and their role in ammonium assimilation or nitrogen transport. Planta 211: 800-806.
    • (2000) Planta , vol.211 , pp. 800-806
    • Becker, T.W.1    Carrayol, E.2    Hirel, B.3
  • 5
    • 0000395059 scopus 로고
    • Regulation of NADH-glutamate dehydrogenase activity by phytochrome, calcium and calmodulin in Zea mays
    • Das R., Sharma A. K., Sopory S.K. 1989. Regulation of NADH-glutamate dehydrogenase activity by phytochrome, calcium and calmodulin in Zea mays. Plant Cell. Physiol. 30: 317-323.
    • (1989) Plant Cell. Physiol. , vol.30 , pp. 317-323
    • Das, R.1    Sharma, A.K.2    Sopory, S.K.3
  • 6
    • 0035081796 scopus 로고    scopus 로고
    • Construction, separation and properties of hybrid hexamers of glutamate dehydrogenase in which five of the six subunits are contributed by the catalically inert D165S
    • Hayden B.M., Engel P.C. 2001. Construction, separation and properties of hybrid hexamers of glutamate dehydrogenase in which five of the six subunits are contributed by the catalically inert D165S. Eur. J. Biochem. 268: 1173-1180.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1173-1180
    • Hayden, B.M.1    Engel, P.C.2
  • 7
    • 0027333040 scopus 로고
    • L-glutamate dehydrogenases: Distribution, properties and mechanism
    • Hudson R. C., Daniel R.M. 1993. L-Glutamate dehydrogenases: distribution, properties and mechanism. Comp. Biochem. Physiol. 106B: 767-792.
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 767-792
    • Hudson, R.C.1    Daniel, R.M.2
  • 8
    • 0011069061 scopus 로고
    • Effects of calcium on NAD(H)-glutamate dehydrogenase from turnip (Brassica rapa L.) mitochondria
    • Itagaki T., Dry, I. B., Wiskich J. T.1990. Effects of calcium on NAD(H)- glutamate dehydrogenase from turnip (Brassica rapa L.) mitochondria. Plant Cell Physiol. 31: 993-997.
    • (1990) Plant Cell Physiol. , vol.31 , pp. 993-997
    • Itagaki, T.1    Dry, I.B.2    Wiskich, J.T.3
  • 9
    • 38249032379 scopus 로고
    • Purification and properties of NAD-glutamate dehydrogenase from turnip mitochondria
    • Itagaki T., Dry I.B., Wiskich J.T. 1988. Purification and properties of NAD-glutamate dehydrogenase from turnip mitochondria. Phytochemistry 27: 3373-3378.
    • (1988) Phytochemistry , vol.27 , pp. 3373-3378
    • Itagaki, T.1    Dry, I.B.2    Wiskich, J.T.3
  • 10
    • 0011130210 scopus 로고
    • Control of glutamate dehydrogenase from Pisum sativum roots
    • Joy K. W. 1973. Control of glutamate dehydrogenase from Pisum sativum roots. Phytochemistry 12: 1031 - 1040.
    • (1973) Phytochemistry , vol.12 , pp. 1031-1040
    • Joy, K.W.1
  • 11
    • 0035689191 scopus 로고    scopus 로고
    • Purification and characteristics of glutamate dehydrogenase (GDH) from triticale roots
    • Kwinta J., Bartoszewicz K., Bielawski W. 2001. Purification and characteristics of glutamate dehydrogenase (GDH) from triticale roots. Acta Physiol. Plant.23: 399-405.
    • (2001) Acta Physiol. Plant. , vol.23 , pp. 399-405
    • Kwinta, J.1    Bartoszewicz, K.2    Bielawski, W.3
  • 12
    • 0033926907 scopus 로고    scopus 로고
    • Enzyme redundancy and the importance of 2-oxoglutarate in higher plant ammonium assimilation
    • Lancien, M., Gadal, P., Hodges, M.2000. Enzyme redundancy and the importance of 2-oxoglutarate in higher plant ammonium assimilation. lant Physiol. 123: 817-824.
    • (2000) Lant Physiol. , vol.123 , pp. 817-824
    • Lancien, M.1    Gadal, P.2    Hodges, M.3
  • 13
    • 0000837713 scopus 로고
    • Intracellular localization and properties of NADH-glutamate dehydrogenase from Vitis vinifera L.: Purification and characterization of the major leaf isoenzyme
    • Loulakakis K.A., Roubelakis-Angelakis K.A. 1990. Intracellular localization and properties of NADH-glutamate dehydrogenase from Vitis vinifera L.: Purification and characterization of the major leaf isoenzyme. J. Exp. Bot. 41: 1223-1230.
    • (1990) J. Exp. Bot. , vol.41 , pp. 1223-1230
    • Loulakakis, K.A.1    Roubelakis-Angelakis, K.A.2
  • 14
    • 0026505663 scopus 로고
    • Purification and properties of three NAD(P) isozymes of L-glutamate dehydrogenase of Chlamydomonas reinhardtii
    • Moyano E., Cardenas J., Munoz-Blanco J. 1992. Purification and properties of three NAD(P) isozymes of L-glutamate dehydrogenase of Chlamydomonas reinhardtii. Biochim. Biophys. Acta 1119: 63-68.
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 63-68
    • Moyano, E.1    Cardenas, J.2    Munoz-Blanco, J.3
  • 15
    • 0029981769 scopus 로고    scopus 로고
    • Identification of cysteine and lysine residues present at the active site of beef liver glutamate dehydrogenase by o-phthalaldehyde
    • Pandey A., Sheikh S., Katiyar S.S. 1996. Identification of cysteine and lysine residues present at the active site of beef liver glutamate dehydrogenase by o-phthalaldehyde. Biochim. Biophys. Acta 1293: 122-128.
    • (1996) Biochim. Biophys. Acta , vol.1293 , pp. 122-128
    • Pandey, A.1    Sheikh, S.2    Katiyar, S.S.3
  • 16
    • 0033565447 scopus 로고    scopus 로고
    • The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery
    • Peterson P.E., Smith T. S. 1999. The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery. Structure 7: 769-782.
    • (1999) Structure , vol.7 , pp. 769-782
    • Peterson, P.E.1    Smith, T.S.2
  • 17
    • 0011067275 scopus 로고
    • Sensitivity to DTNB of NADH-glutamate dehydrogenase from the leaves of bean seedlings
    • Puranik R.M., Srivastava H.S. 1986. Sensitivity to DTNB of NADH-glutamate dehydrogenase from the leaves of bean seedlings. Phytochemistry 25: 803-805, 1986.
    • (1986) Phytochemistry , vol.25 , pp. 803-805
    • Puranik, R.M.1    Srivastava, H.S.2
  • 19
    • 0029328567 scopus 로고
    • Isolation and characterisation of a cDNA that encodes maize glutamate dehydrogenase
    • Sakakibara H., Fujii K., Sugiyama T. 1995. Isolation and characterisation of a cDNA that encodes maize glutamate dehydrogenase. Plant. Cell Physiol. 36: 789-797.
    • (1995) Plant. Cell Physiol. , vol.36 , pp. 789-797
    • Sakakibara, H.1    Fujii, K.2    Sugiyama, T.3
  • 20
    • 0030070662 scopus 로고    scopus 로고
    • The amino acid sequence similarity of plant glutamate dehydrogenase to the extermophilic archaeal enzyme conforms to it stress-related function
    • Syntichaki K.M., Loulakakis K.A., Roubelakis- Angelakis K. A. 1996. The amino acid sequence similarity of plant glutamate dehydrogenase to the extermophilic archaeal enzyme conforms to it stress-related function. Gene 168: 87-92.
    • (1996) Gene , vol.168 , pp. 87-92
    • Syntichaki, K.M.1    Loulakakis, K.A.2    Roubelakis-Angelakis, K.A.3
  • 21
    • 0032407967 scopus 로고    scopus 로고
    • Characterization of mitochondrial glutamate dehydrogenase from dark-grown soybean seedlings
    • Turano F. 1998. Characterization of mitochondrial glutamate dehydrogenase from dark-grown soybean seedlings. Physiol. Plant. 104: 337-344.
    • (1998) Physiol. Plant. , vol.104 , pp. 337-344
    • Turano, F.1
  • 22
    • 0031127224 scopus 로고    scopus 로고
    • Characterization and expresion of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis
    • Turano F.J., Thakkar S.S., Tung Fang, Weiseman J. M. 1997. Characterization and expresion of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis. Plant. Physiol. 113: 1329-1341.
    • (1997) Plant. Physiol. , vol.113 , pp. 1329-1341
    • Turano, F.J.1    Thakkar, S.S.2    Tung, F.3    Weiseman, J.M.4
  • 23
    • 84950014120 scopus 로고
    • Characteristics of glutamate dehydrogenase prepared from corn shoots
    • Yamaya T., Oaks A., Matsumoto H. 1984. Characteristics of glutamate dehydrogenase prepared from corn shoots. Plant. Physiol. 76: 1009-1013.
    • (1984) Plant. Physiol. , vol.76 , pp. 1009-1013
    • Yamaya, T.1    Oaks, A.2    Matsumoto, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.