EC 6 - Ligases
EC 6.3 - Forming carbon-nitrogen bonds
EC 6.3.1 - Acid—ammonia (or amine) ligases (amide synthases)
EC 6.3.1.2 - Glutamine synthetase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 6.3.1.2
Names
Accepted name:
glutamine synthetase
Other
names:
glutamate—ammonia ligase
L-glutamine synthetase
glutamylhydroxamic synthetase
L-glutamine synthetase
glutamylhydroxamic synthetase
Systematic name:
L-glutamate:ammonia ligase (ADP-forming)
Reaction
- ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
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.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
NIST 74
,
UniPathway
Protein domains and families:
PROSITE:PDOC00162
Gene Ontology:
GO:0004356
CAS Registry Number:
9023-70-5
References
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Isolation of glutamine synthetase and glutamotransferase from green peas.J. Biol. Chem. 201 : 661-672 (1953). [PMID: 13061404]
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Glutamine synthesis by Micrococcus pyogenes var. aureus.Biochem. J. 59 : 579-589 (1955). [PMID: 14363150]
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Manganese-dependent glutamotransferase.J. Biol. Chem. 205 : 553-564 (1953). [PMID: 13129232]
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Glutamine synthesisIn: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes , 2nd ed. vol. 6 , Academic Press , New York , 1962 , 443-468
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Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli.Arch. Biochem. Biophys. 116 : 177-192 (1966). [PMID: 5336023]
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Evolution of the glutamine synthetase gene, one of the oldest existing and functioning genes.Proc. Natl. Acad. Sci. U.S.A. 90 : 3009-3013 (1993). [PMID: 8096645]
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The three-dimensional structure of an eukaryotic glutamine synthetase: functional implications of its oligomeric structure.J. Struct. Biol. 156 : 469-479 (2006). [PMID: 16884924]
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An octameric prokaryotic glutamine synthetase from the haloarchaeon Haloferax mediterranei.FEMS Microbiol. Lett. 264 : 110-116 (2006). [PMID: 17020556]
[EC 6.3.1.2 created 1961, modified 2016]