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MetaCyc Chimeric Pathway: L-glutamate and L-glutamine biosynthesis

Enzyme View:

Pathway diagram: L-glutamate and L-glutamine biosynthesis

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: BiosynthesisAmino Acids BiosynthesisProteinogenic Amino Acids BiosynthesisL-glutamate Biosynthesis
BiosynthesisAmino Acids BiosynthesisProteinogenic Amino Acids BiosynthesisL-glutamine Biosynthesis
Metabolic Clusters

Some taxa known to possess parts of the pathway include : Arabidopsis thaliana col, Escherichia coli K-12 substr. MG1655, Haloferax mediterranei, Homo sapiens, Lupinus angustifolius, Ruminococcus albus 8, Saccharomyces cerevisiae

Expected Taxonomic Range: Archaea, Bacteria , Eukaryota

Note: This is a chimeric pathway, comprising reactions from multiple organisms, and typically will not occur in its entirety in a single organism. The taxa listed here are likely to catalyze only subsets of the reactions depicted in this pathway.

Please note: This collection of reactions does not represent the metabolism of a single organism. Rather, it is assembled from a variety of organisms. Its purpose is to provide an overview of the ways that organisms can biosynthesize glutamate and glutamine.

The amino acid glutamate is a both constituent of proteins and a biosynthetic precursor. Many pathways and reactions involving glutamate as a precursor are shown on the MetaCyc compound page for L-glutamate. Glutamine is also a constituent of proteins and is the amino group donor for many biosynthetic reactions, as shown on the MetaCyc compound page for L-glutamine. It also serves as a storage form of ammonia.

In microorganisms, glutamate dehydrogenase, glutamine synthetase (GS), and glutamate synthase (glutamine α-oxoglutarate amidotransferase, GOGAT) are used for ammonia assimilation. Some of these organisms may use only glutamate dehydrogenase, or only glutamine synthetase/glutamate synthase (GS/GOGAT), while others use either route, depending upon growth conditions ( [Gottschalk86] and in [MartinezEspinos06, Magasanik03]). Mammals use glutamate dehydrogenase and glutamine synthetase in nitrogen metabolism. In plants, GS/GOGAT functions in ammonia assimilation. A role for glutamate dehydrogenase in glutamate biosynthesis in plants is unclear [Purnell07].

Subpathways: L-glutamine biosynthesis I, L-glutamate biosynthesis V, L-glutamate biosynthesis IV, L-glutamate biosynthesis I, L-glutamate biosynthesis III, L-glutamate biosynthesis II

Variants: L-arginine degradation I (arginase pathway), L-glutamine biosynthesis III

Created 11-Apr-2007 by Fulcher CA, SRI International


Gottschalk86: Gottschalk, G "Bacterial Metabolism, Second Edition." Springer-Verlag, New York. 1986.

Magasanik03: Magasanik B (2003). "Ammonia assimilation by Saccharomyces cerevisiae." Eukaryot Cell 2(5);827-9. PMID: 14555464

MartinezEspinos06: Martinez-Espinosa RM, Esclapez J, Bautista V, Bonete MJ (2006). "An octameric prokaryotic glutamine synthetase from the haloarchaeon Haloferax mediterranei." FEMS Microbiol Lett 264(1);110-6. PMID: 17020556

Purnell07: Purnell MP, Botella JR (2007). "Tobacco isoenzyme 1 of NAD(H)-dependent glutamate dehydrogenase catabolizes glutamate in vivo." Plant Physiol 143(1);530-9. PMID: 17114271

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Alibhai94: Alibhai M, Villafranca JJ (1994). "Kinetic and mutagenic studies of the role of the active site residues Asp-50 and Glu-327 of Escherichia coli glutamine synthetase." Biochemistry 33(3);682-6. PMID: 7904829

Amaya05: Amaya KR, Kocherginskaya SA, Mackie RI, Cann IK (2005). "Biochemical and mutational analysis of glutamine synthetase type III from the rumen anaerobe Ruminococcus albus 8." J Bacteriol 187(21);7481-91. PMID: 16237031

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Atkins92: Atkins WM, Villafranca JJ (1992). "Time-resolved fluorescence studies of tryptophan mutants of Escherichia coli glutamine synthetase: conformational analysis of intermediates and transition-state complexes." Protein Sci 1(3);342-55. PMID: 1363912

Atkins94: Atkins WM (1994). "Supramolecular self-assembly of Escherichia coli glutamine synthetase: effects of pressure and adenylylation state on dodecamer stacking." Biochemistry 33(50);14965-73. PMID: 7999752

Avendano97: Avendano A, Deluna A, Olivera H, Valenzuela L, Gonzalez A (1997). "GDH3 encodes a glutamate dehydrogenase isozyme, a previously unrecognized route for glutamate biosynthesis in Saccharomyces cerevisiae." J Bacteriol 179(17);5594-7. PMID: 9287019

Balakrishnan78: Balakrishnan MS, Villafranca JJ (1978). "Distance determinations between the metal ion sites of Escherichia coli glutamine synthetase by electron paramagnetic resonance using Cr(III)--nucleotides as paramagnetic substrate analogues." Biochemistry 17(17);3531-8. PMID: 28753

Becerril85: Becerril B, Valle F, Merino E, Riba L, Bolivar F (1985). "Repetitive extragenic palindromic (REP) sequences in the Escherichia coli gdhA gene." Gene 37(1-3);53-62. PMID: 3902576

Bender77: Bender RA, Janssen KA, Resnick AD, Blumenberg M, Foor F, Magasanik B (1977). "Biochemical parameters of glutamine synthetase from Klebsiella aerogenes." J Bacteriol 129(2);1001-9. PMID: 14104

Benjamin89: Benjamin PM, Wu JI, Mitchell AP, Magasanik B (1989). "Three regulatory systems control expression of glutamine synthetase in Saccharomyces cerevisiae at the level of transcription." Mol Gen Genet 217(2-3);370-7. PMID: 2570348

Bennett09: Bennett BD, Kimball EH, Gao M, Osterhout R, Van Dien SJ, Rabinowitz JD (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5(8);593-9. PMID: 19561621

Berberich72: Berberich MA (1972). "A glutamate-dependent phenotype in E. coli K12: the result of two mutations." Biochem Biophys Res Commun 47(6);1498-503. PMID: 4402696

Blumenthal73: Blumenthal KM, Smith EL (1973). "Nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase of Neurospora. I. Isolation, subunits, amino acid composition, sulfhydryl groups, and identification of a lysine residue reactive with pyridoxal phosphate and N-ethylmaleimide." J Biol Chem 248(17);6002-8. PMID: 4146914

Boland77: Boland MJ, Benny AG (1977). "Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules." Eur J Biochem 79(2);355-62. PMID: 21790

Bonete90: Bonete MJ, Camacho ML, Cadenas E (1990). "Analysis of the kinetic mechanism of halophilic NADP-dependent glutamate dehydrogenase." Biochim Biophys Acta 1990;1041(3);305-10. PMID: 1980084

Bower83: Bower S, Zalkin H (1983). "Chemical modification and ligand binding studies with Escherichia coli glutamate synthase." Biochemistry 22(7);1613-20. PMID: 6342664

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Bruggeman05: Bruggeman FJ, Boogerd FC, Westerhoff HV (2005). "The multifarious short-term regulation of ammonium assimilation of Escherichia coli: dissection using an in silico replica." FEBS J 272(8);1965-85. PMID: 15819889

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Bywater75: Bywater RP, Carlisle CH, Jackson RB, Mackay AL, Timmins PA (1975). "Crystals of glutamine synthetase from Escherichia coli." J Mol Biol 91(3);293-300. PMID: 241853

Showing only 20 references. To show more, press the button "Show all references".

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sat Apr 30, 2016, biocyc11.