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:||Biosynthesis → Amino Acids Biosynthesis → Proteinogenic Amino Acids Biosynthesis → L-glutamate Biosynthesis|
|Biosynthesis → Amino Acids Biosynthesis → Proteinogenic Amino Acids Biosynthesis → L-glutamine Biosynthesis|
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
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].
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
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
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
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
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
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