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Volumn 83, Issue , 2014, Pages 225-231

Glutamate dehydrogenase isoenzyme 3 (GDH3) of Arabidopsis thaliana is less thermostable than GDH1 and GDH2 isoenzymes

Author keywords

GDH; Glutamate dehydrogenase; Isoenzymes; Subunits; Thermal stability

Indexed keywords

ARABIDOPSIS PROTEIN; GLUTAMATE DEHYDROGENASE (NADP); ISOENZYME; PROTEIN SUBUNIT;

EID: 84907354412     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2014.08.003     Document Type: Article
Times cited : (13)

References (37)
  • 2
    • 77953008463 scopus 로고    scopus 로고
    • Natural variation of nitrate uptake and nitrogen use efficiency in Arabidopsis thaliana cultivated with limiting and ample nitrogen supply
    • Chardon F., Barthélémy J., Daniel-Vedele F., Masclaux-Daubresse C. Natural variation of nitrate uptake and nitrogen use efficiency in Arabidopsis thaliana cultivated with limiting and ample nitrogen supply. J.Exp. Bot. 2010, 61:2293-2302. 10.1093/jxb/erq059.
    • (2010) J.Exp. Bot. , vol.61 , pp. 2293-2302
    • Chardon, F.1    Barthélémy, J.2    Daniel-Vedele, F.3    Masclaux-Daubresse, C.4
  • 5
    • 33645700621 scopus 로고    scopus 로고
    • Control of the synthesis and subcellular targeting of the two GDH genes products in leaves and stems of Nicotiana plumbaginifolia and Arabidopsis thaliana
    • Fontaine J.-X., Saladino F., Agrimonti C., Bedu M., Tercé-Laforgue T., Tétu T., Hirel B., Restivo F.M., Dubois F. Control of the synthesis and subcellular targeting of the two GDH genes products in leaves and stems of Nicotiana plumbaginifolia and Arabidopsis thaliana. Plant Cell Physiol. 2006, 47:410-418. 10.1093/pcp/pcj008.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 410-418
    • Fontaine, J.-X.1    Saladino, F.2    Agrimonti, C.3    Bedu, M.4    Tercé-Laforgue, T.5    Tétu, T.6    Hirel, B.7    Restivo, F.M.8    Dubois, F.9
  • 8
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., Peitsch M. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997, 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.2
  • 10
    • 80052260152 scopus 로고    scopus 로고
    • Interaction between glutamate dehydrogenase (GDH) and L-leucine catabolic enzymes: intersecting metabolic pathways
    • Hutson S.M., Islam M.M., Zaganas I. Interaction between glutamate dehydrogenase (GDH) and L-leucine catabolic enzymes: intersecting metabolic pathways. Neurochem. Int. 2011, 59:518-524. 10.1016/j.neuint.2011.05.001.
    • (2011) Neurochem. Int. , vol.59 , pp. 518-524
    • Hutson, S.M.1    Islam, M.M.2    Zaganas, I.3
  • 11
    • 59449102490 scopus 로고    scopus 로고
    • Reproductive organs regulate leaf nitrogen metabolism mediated by cytokinin signal
    • Igarashi D., Izumi Y., Dokiya Y., Totsuka K., Fukusaki E., Ohsumi C. Reproductive organs regulate leaf nitrogen metabolism mediated by cytokinin signal. Planta 2009, 229:633-644. 10.1007/s00425-008-0858-2.
    • (2009) Planta , vol.229 , pp. 633-644
    • Igarashi, D.1    Izumi, Y.2    Dokiya, Y.3    Totsuka, K.4    Fukusaki, E.5    Ohsumi, C.6
  • 14
    • 84857804808 scopus 로고    scopus 로고
    • The structure and allosteric regulation of mammalian glutamate dehydrogenase
    • Li M., Li C., Allen A., Stanley C.a, Smith T.J. The structure and allosteric regulation of mammalian glutamate dehydrogenase. Arch. Biochem. Biophys. 2012, 519:69-80. 10.1016/j.abb.2011.10.015.
    • (2012) Arch. Biochem. Biophys. , vol.519 , pp. 69-80
    • Li, M.1    Li, C.2    Allen, A.3    Stanley, C.A.4    Smith, T.J.5
  • 15
    • 84907310146 scopus 로고    scopus 로고
    • Nitrogen metabolism in plants under low oxygen stress
    • Limami A.M., Diab H., Lothier J. Nitrogen metabolism in plants under low oxygen stress. Planta 2014, 239:531-541. 10.1007/s00425-013-2015-9.
    • (2014) Planta , vol.239 , pp. 531-541
    • Limami, A.M.1    Diab, H.2    Lothier, J.3
  • 16
    • 48649111185 scopus 로고    scopus 로고
    • Concerted modulation of alanine and glutamate metabolism in young Medicago truncatula seedlings under hypoxic stress
    • Limami A.M., Glévarec G., Ricoult C., Cliquet J.-B., Planchet E. Concerted modulation of alanine and glutamate metabolism in young Medicago truncatula seedlings under hypoxic stress. J.Exp. Bot. 2008, 59:2325-2335. 10.1093/jxb/ern102.
    • (2008) J.Exp. Bot. , vol.59 , pp. 2325-2335
    • Limami, A.M.1    Glévarec, G.2    Ricoult, C.3    Cliquet, J.-B.4    Planchet, E.5
  • 17
    • 0000639186 scopus 로고
    • Immunocharacterization of NADH-glutamate dehydrogenase from vitis vinifera L
    • Loulakakis C.A., Roubelakis-Angelakis K.A. Immunocharacterization of NADH-glutamate dehydrogenase from vitis vinifera L. Plant Physiol. 1990, 94:109-113.
    • (1990) Plant Physiol. , vol.94 , pp. 109-113
    • Loulakakis, C.A.1    Roubelakis-Angelakis, K.A.2
  • 18
    • 84887171238 scopus 로고    scopus 로고
    • Glutamate dehydrogenase isoenzyme 3 (GDH3) of Arabidopsis thaliana is regulated by a combined effect of nitrogen and cytokinin
    • Marchi L., Degola F., Polverini E., Tercé-Laforgue T., Dubois F., Hirel B. Glutamate dehydrogenase isoenzyme 3 (GDH3) of Arabidopsis thaliana is regulated by a combined effect of nitrogen and cytokinin. Plant Physiol. Biochem. 2013, 73:368-374.
    • (2013) Plant Physiol. Biochem. , vol.73 , pp. 368-374
    • Marchi, L.1    Degola, F.2    Polverini, E.3    Tercé-Laforgue, T.4    Dubois, F.5    Hirel, B.6
  • 19
    • 43149084126 scopus 로고    scopus 로고
    • NAD(H)-dependent glutamate dehydrogenase is essential for the survival of Arabidopsis thaliana during dark-induced carbon starvation
    • Miyashita Y., Good A.G. NAD(H)-dependent glutamate dehydrogenase is essential for the survival of Arabidopsis thaliana during dark-induced carbon starvation. J.Exp. Bot. 2008, 59:667-680. 10.1093/jxb/erm340.
    • (2008) J.Exp. Bot. , vol.59 , pp. 667-680
    • Miyashita, Y.1    Good, A.G.2
  • 20
    • 68149160193 scopus 로고    scopus 로고
    • Natural variation in Arabidopsis adaptation to growth at low nitrogen conditions
    • North K.A., Ehlting B., Koprivova A., Rennenberg H., Kopriva S. Natural variation in Arabidopsis adaptation to growth at low nitrogen conditions. Plant Physiol. Biochem. 2009, 47:912-918. 10.1016/j.plaphy.2009.06.009.
    • (2009) Plant Physiol. Biochem. , vol.47 , pp. 912-918
    • North, K.A.1    Ehlting, B.2    Koprivova, A.3    Rennenberg, H.4    Kopriva, S.5
  • 22
    • 0032829928 scopus 로고    scopus 로고
    • Pesticide inactivation of Peanut glutamate dehydrogenase: biochemical basis of the enzyme's isomerization
    • Osuji G.O., Braithwaite C., Pointer R., Reyes J. Pesticide inactivation of Peanut glutamate dehydrogenase: biochemical basis of the enzyme's isomerization. J.Agric. Food Chem. 1999, 47:3345-3351. 10.1021/jf980531v.
    • (1999) J.Agric. Food Chem. , vol.47 , pp. 3345-3351
    • Osuji, G.O.1    Braithwaite, C.2    Pointer, R.3    Reyes, J.4
  • 23
    • 0031281306 scopus 로고    scopus 로고
    • Regulation of glutamate dehydrogenase by methionine sulphoximine
    • Osuji G.O., Wenceslau C., Madu C. Regulation of glutamate dehydrogenase by methionine sulphoximine. Phytochemistry 1997, 46:817-825.
    • (1997) Phytochemistry , vol.46 , pp. 817-825
    • Osuji, G.O.1    Wenceslau, C.2    Madu, C.3
  • 24
    • 0034076425 scopus 로고    scopus 로고
    • Cloning of two glutamate dehydrogenase cDNAs from Asparagus officinalis: sequence analysis and evolutionary implications
    • Pavesi A., Ficarelli A., Tassi F., Restivo F.M. Cloning of two glutamate dehydrogenase cDNAs from Asparagus officinalis: sequence analysis and evolutionary implications. Genome 2000, 43:306-316.
    • (2000) Genome , vol.43 , pp. 306-316
    • Pavesi, A.1    Ficarelli, A.2    Tassi, F.3    Restivo, F.M.4
  • 25
    • 0033788590 scopus 로고    scopus 로고
    • Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human glutamate dehydrogenases are regulated by distinct allosteric mechanisms: implications for biologic function
    • Plaitakis A., Metaxari M., Shashidharan P. Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human glutamate dehydrogenases are regulated by distinct allosteric mechanisms: implications for biologic function. J.Neurochem. 2000, 75:1862-1869.
    • (2000) J.Neurochem. , vol.75 , pp. 1862-1869
    • Plaitakis, A.1    Metaxari, M.2    Shashidharan, P.3
  • 26
    • 1542568235 scopus 로고    scopus 로고
    • Molecular cloning of glutamate dehydrogenase genes of Nicotiana plumbaginifolia: structure analysis and regulation of their expression by physiological and stress conditions
    • Restivo F.M. Molecular cloning of glutamate dehydrogenase genes of Nicotiana plumbaginifolia: structure analysis and regulation of their expression by physiological and stress conditions. Plant Sci. 2004, 166:971-982. 10.1016/j.plantsci.2003.12.011.
    • (2004) Plant Sci. , vol.166 , pp. 971-982
    • Restivo, F.M.1
  • 27
    • 0031003604 scopus 로고    scopus 로고
    • Nerve tissue-specific human glutamate dehydrogenase that is thermolabile and highly regulated by ADP
    • Shashidharan P., Clarke D.D., Ahmed N., Moschonas N., Plaitakis a Nerve tissue-specific human glutamate dehydrogenase that is thermolabile and highly regulated by ADP. J.Neurochem. 1997, 68:1804-1811.
    • (1997) J.Neurochem. , vol.68 , pp. 1804-1811
    • Shashidharan, P.1    Clarke, D.D.2    Ahmed, N.3    Moschonas, N.4    Plaitakis, A.5
  • 28
    • 84896719114 scopus 로고    scopus 로고
    • The discovery of human of GLUD2 glutamate dehydrogenase and its implications for cell function in health and disease
    • Shashidharan P., Plaitakis A. The discovery of human of GLUD2 glutamate dehydrogenase and its implications for cell function in health and disease. Neurochem. Res. 2014, 39:460-470. 10.1007/s11064-013-1227-5.
    • (2014) Neurochem. Res. , vol.39 , pp. 460-470
    • Shashidharan, P.1    Plaitakis, A.2
  • 29
    • 37249011264 scopus 로고    scopus 로고
    • The isoenzyme 7 of tobacco NAD(H)-dependent glutamate dehydrogenase exhibits high deaminating and low aminating activities invivo
    • Skopelitis D.S., Paranychianakis N.V., Kouvarakis A., Spyros A., Stephanou E.G., Roubelakis-Angelakis K.A. The isoenzyme 7 of tobacco NAD(H)-dependent glutamate dehydrogenase exhibits high deaminating and low aminating activities invivo. Plant Physiol. 2007, 145:1726-1734. 10.1104/pp.107.107813.
    • (2007) Plant Physiol. , vol.145 , pp. 1726-1734
    • Skopelitis, D.S.1    Paranychianakis, N.V.2    Kouvarakis, A.3    Spyros, A.4    Stephanou, E.G.5    Roubelakis-Angelakis, K.A.6
  • 30
    • 0030070662 scopus 로고    scopus 로고
    • The amino-acid sequence similarity of plant glutamate dehydrogenase to the extremophilic archaeal enzyme conforms to its stress-related function
    • Syntichaki K.M., Loulakakis K.A., Roubelakis-Angelakis K.A. The amino-acid sequence similarity of plant glutamate dehydrogenase to the extremophilic archaeal enzyme conforms to its stress-related function. Gene 1996, 168:87-92.
    • (1996) Gene , vol.168 , pp. 87-92
    • Syntichaki, K.M.1    Loulakakis, K.A.2    Roubelakis-Angelakis, K.A.3
  • 31
    • 78650043632 scopus 로고    scopus 로고
    • Hetero-oligomeric glutamate dehydrogenase from Thermus thermophilus
    • Tomita T., Miyazaki T., Miyazaki J., Kuzuyama T., Nishiyama M. Hetero-oligomeric glutamate dehydrogenase from Thermus thermophilus. Microbiology 2010, 156:3801-3813. 10.1099/mic.0.042721-0.
    • (2010) Microbiology , vol.156 , pp. 3801-3813
    • Tomita, T.1    Miyazaki, T.2    Miyazaki, J.3    Kuzuyama, T.4    Nishiyama, M.5
  • 32
    • 0031127224 scopus 로고    scopus 로고
    • Characterization and expression of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis
    • Turano F.J., Thakkar S.S., Fang T., Weisemann J.M. Characterization and expression of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis. Plant Physiol. 1997, 113:1329-1341.
    • (1997) Plant Physiol. , vol.113 , pp. 1329-1341
    • Turano, F.J.1    Thakkar, S.S.2    Fang, T.3    Weisemann, J.M.4
  • 34
    • 34247632051 scopus 로고    scopus 로고
    • Redox and translational regulation of glutamate dehydrogenase α subunits in Brassica napus under wounding stress
    • Watanabe M., Itho Y., Jo Y., Yasuda K., Kamachi K., Watanabe Y. Redox and translational regulation of glutamate dehydrogenase α subunits in Brassica napus under wounding stress. Plant Sci. 2007, 172:1182-1192. 10.1016/j.plantsci.2007.01.007.
    • (2007) Plant Sci. , vol.172 , pp. 1182-1192
    • Watanabe, M.1    Itho, Y.2    Jo, Y.3    Yasuda, K.4    Kamachi, K.5    Watanabe, Y.6
  • 36
    • 1642304692 scopus 로고    scopus 로고
    • Important role of Ser443 in different thermal stability of human glutamate dehydrogenase isozymes
    • Yang S.-J., Huh J.-W., Hong H.-N., Kim T.U., Cho S.-W. Important role of Ser443 in different thermal stability of human glutamate dehydrogenase isozymes. FEBS Lett. 2004, 562:59-64. 10.1016/S0014-5793(04)00183-8.
    • (2004) FEBS Lett. , vol.562 , pp. 59-64
    • Yang, S.-J.1    Huh, J.-W.2    Hong, H.-N.3    Kim, T.U.4    Cho, S.-W.5
  • 37
    • 0037195942 scopus 로고    scopus 로고
    • Substitution of Ser for Arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and L-leucine
    • Zaganas I., Spanaki C., Karpusas M., Plaitakis A. Substitution of Ser for Arg-443 in the regulatory domain of human housekeeping (GLUD1) glutamate dehydrogenase virtually abolishes basal activity and markedly alters the activation of the enzyme by ADP and L-leucine. J.Biol. Chem. 2002, 277:46552-46558. 10.1074/jbc.M208596200.
    • (2002) J.Biol. Chem. , vol.277 , pp. 46552-46558
    • Zaganas, I.1    Spanaki, C.2    Karpusas, M.3    Plaitakis, A.4


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