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N Use By Plants
Nitrate Assimilation
Ammonia Assimilation
Glu, Gln, Asn, Gly, Ser
Aminotransferases
Asp, Ala, GABA
Val, Leu, Ileu, Thr, Lys
Pro, Arg, Orn
Polyamines
Non-protein AAs
Alkaloids
Sulfate Assimilation
Cys, Met, AdoMet, ACC
His, Phe, Tyr, Tryp
Secondary Products
Onium Compounds
Enzymes
Methods
Simulation
References
HORT640 - Metabolic Plant Physiology

References, glutamate dehydrogenase

Aalen N, Steen IH, Birkeland NK, Lien T. Purification and properties of an extremely thermostable NADP+-specific glutamate dehydrogenase from Archaeoglobus fulgidus. Arch. Microbiol. 168: 536-539 (1997).

Abd Rahman RN, Fujiwara S, Takagi M, Kanaya S, Imanaka T. Effect of heat treatment on proper oligomeric structure formation of thermostable glutamate dehydrogenase from a hyperthermophilic archaeon. Biochem. Biophys. Res. Commun. 241: 646-652 (1997).

Abell LM, Schloss JV. Oxygenase side reactions of acetolactate synthase and other carbanion-forming enzymes. Biochemistry 30: 7883-7887 (1991).

Abenavoli MR, Sorgona A, Sidari M, Badiani M, Fuggi A. Coumarin inhibits the growth of carrot (Daucus carota L. cv. Saint Valery) cells in suspension culture. J. Plant Physiol. 160: 227-237 (2003).

Abiko T, Obara M, Ushioda A, Hayakawa T, Hodges M, Yamaya T. Localization of NAD-isocitrate dehydrogenase and glutamate dehydrogenase in rice roots: candidates for providing carbon skeletons to NADH-glutamate synthase. Plant Cell Physiol. 46: 1724-1734 (2005).

Abraham DG, Cooper AJ. Glutamine transaminase K and cysteine S-conjugate beta-lyase activity stains. Anal. Biochem. 197: 421-427 (1991).

Abrahams GL, Abratt VR. The NADH-dependent glutamate dehydrogenase enzyme of Bacteroides fragilis Bf1 is induced by peptides in the growth medium. Microbiology 144: 1659-1667 (1998).

Aghajanian S, Engel PC. Use of protein engineering to explore subunit interactions in an allosteric enzyme: construction of inter-subunit hybrids in Clostridium symbiosum glutamate dehydrogenase. Protein Eng. 11: 569-575 (1998).

Aghajanian S, Hovsepyan M, Geoghegan KF, Chrunyk BA, Engel PC. Probing the stability of the tertiary structure of glutamate dehydrogenase by limited proteolysis. Biochem. Soc. Trans. 26: S26 (1998).

Aghajanian S, Walsh TP, Engel PC. Specificity of coenzyme analogues and fragments in promoting or impeding the refolding of clostridial glutamate dehydrogenase. Protein Sci. 8: 866-872 (1999).

Agnelli P, Dossena L, Colombi P, Mulazzi S, Morandi P, Tedeschi G, Negri A, Curti B, Vanoni MA. The unexpected structural role of glutamate synthase [4Fe-4S](+1,+2) clusters as demonstrated by site-directed mutagenesis of conserved C residues at the N-terminus of the enzyme beta subunit. Arch. Biochem. Biophys. 436: 355-366 (2005).

Ahmad I, Hellebust JA. A spectrophotometric procedure for measuring oxoglutarate and determining aminotransferase activities using nicotinamide adenine dinucleotide phosphate-linked glutamate dehydrogenase from algae. Anal. Biochem. 180: 99-104 (1989).

Ahn J, Choi S, Cho S. Identification of lysine residue involved in inactivation of brain glutamate dehydrogenase isoproteins by o-phthalaldehyde. Biochimie 81: 1123-1129 (1999).

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Ang HH, Chan KL, Mak JW. Electrophoretic variations of enzyme, GDH (NADP-dependent glutamate dehydrogenase) (EC. 1.4.1.4) in characterizing clones and isolates of Malaysian Plasmodium falciparum. Korean J. Parasitol. 34: 211-213 (1996).

Appenroth KJ, Teller S. Are NADP-dependent isocitrate dehydrogenases and ferredoxin-dependent glutamate synthase co-regulated by the same photoreceptors? Planta 218: 775-783 (2004).

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Araujo WL, Nunes-Nesi A, Trenkamp S, Bunik VI, Fernie AR. Inhibition of 2-oxoglutarate dehydrogenase in potato tuber suggests the enzyme is limiting for respiration and confirms its importance in nitrogen assimilation. Plant Physiol. 148: 1782-1796 (2008).

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Asakura Y, Kimura E, Usuda Y, Kawahara Y, Matsui K, Osumi T, Nakamatsu T. Altered metabolic flux due to deletion of odhA causes L-glutamate overproduction in Corynebacterium glutamicum. Appl. Environ. Microbiol. 73: 1308-1319 (2007).

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Astolfi S, Zuchi S, Passera C. Role of sulphur availability on cadmium-induced changes of nitrogen and sulphur metabolism in maize (Zea mays L.) leaves. J. Plant Physiol. 161: 795-802 (2004).

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Baggio L, Morrison M. The NAD(P)H-utilizing glutamate dehydrogenase of Bacteroides thetaiotaomicron belongs to enzyme family I, and its activity is affected by trans-acting gene(s) positioned downstream of gdhA. J. Bacteriol. 178: 7212-7220 (1996).

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Barsch A, Carvalho HG, Cullimore JV, Niehaus K. GC-MS based metabolite profiling implies three interdependent ways of ammonium assimilation in Medicago truncatula root nodules. J. Biotechnol. 127: 79-83 (2006).

Bartsch K, von Johnn-Marteville A, Schulz A. Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD). J. Bacteriol. 172: 7035-7042 (1990).

Basso LA, Engel PC, Walmsley AR. Cooperativity between trimers of the hexameric glutamate dehydrogenase from Clostridium symbiosum. Biochim. Biophys. Acta 1382: 345-350 (1998).

Batrel Y, Regnault M. Metabolic pathways of ammoniogenesis in the shrimp Crangon crangon L.: possible role of glutamate dehydrogenase. Comp. Biochem. Physiol. [B] 82: 217-222 (1985).

Beagle JM, Apgar GA, Jones KL, Griswold KE, Radcliffe JS, Qiu X, Lightfoot DA, Iqbal MJ. The digestive fate of Escherichia coli glutamate dehydrogenase deoxyribonucleic acid from transgenic corn in diets fed to weanling pigs. J. Anim. Sci. 84: 597-607 (2006).

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Belitsky BR, Sonenshein AL. An enhancer element located downstream of the major glutamate dehydrogenase gene of Bacillus subtilis. Proc. Natl. Acad. Sci. U.S.A. 96: 10290-10295 (1999).

Belitsky BR, Sonenshein AL. Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase. J. Bacteriol. 186: 3399-3407 (2004).

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Bender RA, Macaluso A, Magasanik B. Glutamate dehydrogenase: genetic mapping and isolation of regulatory mutants of Klebsiella aerogenes. J. Bacteriol. 127: 141-148 (1976).

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Bhuiya MW, Sakuraba H, Kujo C, Nunoura-Kominato N, Kawarabayasi Y, Kikuchi H, Ohshima T. Glutamate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1: enzymatic characterization, identification of the encoding gene, and phylogenetic implications. Extremophiles 4: 333-341 (2000).

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Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H. The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. J. Mol. Biol. 345: 325-337 (2005).

Bhuiya MW, Sakuraba H, Yoneda K, Ohshima T, Imagawa T, Katunuma N, Tsuge H. Crystallization and preliminary X-ray diffraction analysis of the hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. Acta Crystallogr. D. Biol. Crystallogr. 60: 715-717 (2004).

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