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EC Tree
IUBMB Comments Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements.
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii The enzyme appears in selected viruses and cellular organisms
Synonyms
glutamine synthetase, gamma-glutamyl transferase, gs-ii, gsiii, taase, glna1, glna2, gln1;2, gln synthetase, gs(1),
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Clone lambda-GS28
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Clone lambda-GS31
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Gln isozyme alpha
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Gln isozyme gamma
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Glutamate--ammonia ligase
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glutamate-ammonia ligase
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Glutamine synthetase
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Glutamylhydroxamic synthetase
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L-Glutamine synthetase
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Synthetase, glutamine
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L-glutamate:ammonia ligase (ADP-forming)
Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements.
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ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + gamma-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than 3-aminopentanedioate (beta-glutamate) as a substrate
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ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
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Mg2+
assay in presence of 55 mM Mg2+
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58
L-glutamate
pH 7.0, 60°C
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40 - 70
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about 50% of maximal activity at 40°C and at 70°C
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SwissProt
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midpoint temperature of pure enzyme, none of the small molecules tested significantly stabilizes the enzyme. Stabilization by Escherichia coli GroEL or ribosomal protein L2. Protein-protein interactions appear to be the dominant factor in stabilizing the archael enzyme at the growth temperature (85°C)
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overexpression in Escherichia coli
expression in Escherichia coli
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Neelon, K.; Schreier, H.J.; Meekins, H.; Robinson, P.M.; Roberts, M.F.
Compatible solute effects on thermostability of glutamine synthetase and aspartate transcarbamoylase from Methanococcus jannaschii
Biochim. Biophys. Acta
1753
164-173
2005
Methanocaldococcus jannaschii
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Robinson, P.; Neelon, K.; Schreier, H.J.; Roberts, M.F.
beta-Glutamate as a substrate for glutamine synthetase
Appl. Environ. Microbiol.
67
4458-4463
2001
Methanohalophilus portucalensis, Archaeoglobus fulgidus (O29313), Archaeoglobus fulgidus, Methanocaldococcus jannaschii (Q60182), Methanocaldococcus jannaschii, Archaeoglobus fulgidus VC-16 (O29313)
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