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Gene Review

gdhA  -  glutamate dehydrogenase, NADP-specific

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1759, JW1750
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Disease relevance of gdhA


High impact information on gdhA

  • The glutamate dehydrogenase gene of Escherichia coli has been cloned into broad host-range plasmids and can complement glutamate synthase mutants of Methylophilus methylotrophus [5].
  • Assimilation of ammonia via glutamate dehydrogenase is more energy-efficient than via glutamate synthase, thus the recombinant organism converts more growth substrate, methanol, into cellular carbon [5].
  • In addition, they have glutamate synthase (EC and glutamate dehydrogenase (EC activities [6].
  • In agreement with this reasoning we find the kinetics of glutamate accumulation to be independent of the specific path of synthesis, whether by glutamate dehydrogenase or by glutamate synthase [7].
  • The nucleotide sequence of S. typhimurium gdhA was determined and the amino acid sequence derived [8].

Chemical compound and disease context of gdhA


Biological context of gdhA


Anatomical context of gdhA

  • These data suggest that the gdhA transgene began degradation in the stomach and was nondetectable in the large intestine [15].
  • The remaining 56 pigs were transitioned onto a corn-soybean meal diet and fed a diet containing 58% gdhA corn for approximately 1 wk; immediately thereafter, liver, 10th rib muscle, white blood cells, and plasma from the hepatic portal vein and ingesta from the stomach, distal ileum, and large intestine were collected [15].
  • A site-directed mutant of clostridial glutamate dehydrogenase in which Ala163 in the glutamate binding site is replaced by glycine displays a markedly sigmoid dependence of reaction rate on glutamate concentration (S0.5 = 200 mM), with a Hill coefficient of 3.4 when assayed at pH 10.5 with 1 mM NAD+ [16].
  • Blood samples were collected and analysed for hematology and total serum bile acids (S-BA), glutamate dehydrogenase (S-GLDH), calcium (S-Ca), iron (S-Fe), zinc (S-Zn) and a blood plasma metabolite (15-ketodihydro-PGF2a; P-PG) of prostaglandin F2a [17].

Associations of gdhA with chemical compounds

  • The gdhA gene encoding the NADP-dependent glutamate dehydrogenase activity from Penicillium chrysogenum has been isolated and characterized for its use in gene expression [14].
  • The gdhA1 mutational site has been identified by recombinational mapping, polymerase chain reaction (PCR) amplification and DNA sequencing, as an A to G transition at nucleotide 274 of the gdhA coding sequence, resulting in an amino acid change of lysine 92 to glutamic acid [18].
  • The higher state of GS is connected with a lower GDH activity and NH3 concentration [19].
  • Gene expression of GOGAT above a threshold value makes expression of GS under ammonium-limited conditions, and of GDH under glucose-limited conditions, sufficient for ammonium assimilation [20].
  • Cause and effect between gdhA expression, glutamate metabolism, and plant phenotypes was analyzed by (13) NH(4)(+) labeling of amino acid fractions, and by FT-ICR-MS analysis of metabolites [21].

Regulatory relationships of gdhA

  • Since no adenylation of the GS is detectable GS bistability seems to be regulated on the level of enzyme synthesis like GDH bistability [19].

Other interactions of gdhA

  • In wild-type bacteria there was only a weak inverse correlation between the activities of GS and glutamate dehydrogenase (GDH) during growth in various media [9].
  • The argP mutation, but not the glnE mutation, was associated with reduced glutamate dehydrogenase activity and a concomitant NH4+ assimilation defect in the gltBD strain [22].

Analytical, diagnostic and therapeutic context of gdhA


  1. Complete nucleotide sequence of the Escherichia coli gdhA gene. McPherson, M.J., Wootton, J.C. Nucleic Acids Res. (1983) [Pubmed]
  2. Cloning and characterization of gdhA, the structural gene for glutamate dehydrogenase of Salmonella typhimurium. Miller, E.S., Brenchley, J.E. J. Bacteriol. (1984) [Pubmed]
  3. Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase. Cleton-Jansen, A.M., Goosen, N., Fayet, O., van de Putte, P. J. Bacteriol. (1990) [Pubmed]
  4. Glutamate dehydrogenase: genetic mapping and isolation of regulatory mutants of Klebsiella aerogenes. Bender, R.A., Macaluso, A., Magasanik, B. J. Bacteriol. (1976) [Pubmed]
  5. Improved conversion of methanol to single-cell protein by Methylophilus methylotrophus. Windass, J.D., Worsey, M.J., Pioli, E.M., Pioli, D., Barth, P.T., Atherton, K.T., Dart, E.C., Byrom, D., Powell, K., Senior, P.J. Nature (1980) [Pubmed]
  6. The product of a newly identified gene, gInF, is required for synthesis of glutamine synthetase in Salmonella. Garcia, E., Bancroft, S., Rhee, S.G., Kustu, S. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  7. Interdependence of K+ and glutamate accumulation during osmotic adaptation of Escherichia coli. McLaggan, D., Naprstek, J., Buurman, E.T., Epstein, W. J. Biol. Chem. (1994) [Pubmed]
  8. Affinity labeling of a glutamyl peptide in the coenzyme binding site of NADP+-specific glutamate dehydrogenase of Salmonella typhimurium by 2-[(4-bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 2',5'-bisphosphate. Bansal, A., Dayton, M.A., Zalkin, H., Colman, R.F. J. Biol. Chem. (1989) [Pubmed]
  9. Lack of a regulatory function for glutamine synthetase protein in the synthesis of glutamate dehydrogenase and nitrite reductase in Escherichia coli K12. Newman, B.M., Cole, J.A. J. Gen. Microbiol. (1977) [Pubmed]
  10. Regulation of gamma-aminobutyric acid degradation in Escherichia coli by nitrogen metabolism enzymes. Zaboura, M., Halpern, Y.S. J. Bacteriol. (1978) [Pubmed]
  11. The glutamine synthetase of Prevotella bryantii B(1)4 is a family III enzyme (GlnN) and glutamine supports growth of mutants lacking glutamate dehydrogenase activity. Wen, Z.T., Peng, L., Morrison, M. FEMS Microbiol. Lett. (2003) [Pubmed]
  12. 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. Baggio, L., Morrison, M. J. Bacteriol. (1996) [Pubmed]
  13. Identification of a functional promoter for the Escherichia coli gdhA gene and its regulation. Riba, L., Becerril, B., Servín-González, L., Valle, F., Bolivar, F. Gene (1988) [Pubmed]
  14. The NADP-dependent glutamate dehydrogenase gene from Penicillium chrysogenum and the construction of expression vectors for filamentous fungi. Díez, B., Mellado, E., Rodríguez, M., Bernasconi, E., Barredo, J.L. Appl. Microbiol. Biotechnol. (1999) [Pubmed]
  15. The digestive fate of Escherichia coli glutamate dehydrogenase deoxyribonucleic acid from transgenic corn in diets fed to weanling pigs. Beagle, J.M., Apgar, G.A., Jones, K.L., Griswold, K.E., Radcliffe, J.S., Qiu, X., Lightfoot, D.A., Iqbal, M.J. J. Anim. Sci. (2006) [Pubmed]
  16. Positive cooperativity with Hill coefficients of up to 6 in the glutamate concentration dependence of steady-state reaction rates measured with clostridial glutamate dehydrogenase and the mutant A163G at high pH. Wang, X.G., Engel, P.C. Biochemistry (1995) [Pubmed]
  17. Reduced response to intravenous endotoxin injections following repeated oral administration of endotoxin in the pig. Holst, H., Edqvist, L.E., Kindahl, H. Acta Vet. Scand. (1993) [Pubmed]
  18. The gdhA1 point mutation in Escherichia coli K12 CLR207 alters a key lysine residue of glutamate dehydrogenase. Jones, K.M., McPherson, M.J., Baron, A.J., Mattaj, I.W., Riordan, C.L., Wootton, J.C. Mol. Gen. Genet. (1993) [Pubmed]
  19. Regulation of ammonia assimilation in ammonia-limited chemostat cultures of Escherichia coli ML 30: evidence of bistability. Müller, P.J., von Frommannshausen, B., Schütz, H. Z. Allg. Mikrobiol. (1981) [Pubmed]
  20. The multifarious short-term regulation of ammonium assimilation of Escherichia coli: dissection using an in silico replica. Bruggeman, F.J., Boogerd, F.C., Westerhoff, H.V. FEBS J. (2005) [Pubmed]
  21. Metabolite fingerprinting in transgenic Nicotiana tabacum altered by the Escherichia coli glutamate dehydrogenase gene. Mungur, R., Glass, A.D., Goodenow, D.B., Lightfoot, D.A. J. Biomed. Biotechnol. (2005) [Pubmed]
  22. Osmosensitivity associated with insertions in argP (iciA) or glnE in glutamate synthase-deficient mutants of Escherichia coli. Nandineni, M.R., Laishram, R.S., Gowrishankar, J. J. Bacteriol. (2004) [Pubmed]
  23. 'Integron'-bearing vectors: a method suitable for stable chromosomal integration in highly restrictive corynebacteria. Reyes, O., Guyonvarch, A., Bonamy, C., Salti, V., David, F., Leblon, G. Gene (1991) [Pubmed]
  24. Crystallization of the NADP(+)-dependent glutamate dehydrogenase from Escherichia coli. Korber, F.C., Rizkallah, P.J., Attwood, T.K., Wootton, J.C., McPherson, M.J., North, A.C., Geddes, A.J., Abeysinghe, I.S., Baker, P.J., Dean, J.L. J. Mol. Biol. (1993) [Pubmed]
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