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MetaCyc Reaction: 6.3.1.2

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 6.3.1.2

Enzymes and Genes:

Arabidopsis thaliana col:
Escherichia coli K-12 substr. MG1655: glutamine synthetaseInferred from experiment: glnA
Haloferax mediterranei: glutamine synthetase, type IVInferred from experiment
Homo sapiens: glutamine synthetase, type IIInferred from experiment: GLUL
Neurospora crassa:
Ruminococcus albus 8: glutamine synthetase, type IIIInferred from experiment: gluN
Saccharomyces cerevisiae: glutamine synthetase, type IIInferred from experiment: GLN1
Solanum lycopersicum: cytosolic glutamine synthetaseInferred from experiment: GS1
Synechococcus elongatus PCC 7942:

In Pathway: nitrate reduction II (assimilatory), L-glutamine biosynthesis III, L-glutamine biosynthesis I, ammonia assimilation cycle II, nitrate reduction VI (assimilatory), nitrate reduction V (assimilatory), ammonia assimilation cycle I

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: glutamate—ammonia ligase

Enzyme Commission Synonyms: glutamine synthetase, glutamylhydroxamic synthetase, L-glutamine synthetase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -6.7717896Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Also acts, more slowly, on 4-methylene-L-glutamate (cf. EC 6.3.1.7 4-methyleneglutamate—ammonia ligase).

Citations: [Woolfolk66, LAJTHA53, FRY55, ELLIOTT53]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R00253, Rhea:16169

Relationship Links: BRENDA:EC:6.3.1.2, ENZYME:EC:6.3.1.2, IUBMB-ExplorEnz:EC:6.3.1.2, UniProt:RELATED-TO:O04998, UniProt:RELATED-TO:O04999, UniProt:RELATED-TO:O22504, UniProt:RELATED-TO:O22505, UniProt:RELATED-TO:O22506, UniProt:RELATED-TO:O66514, UniProt:RELATED-TO:O75014, UniProt:RELATED-TO:P00964, UniProt:RELATED-TO:P00965, UniProt:RELATED-TO:P04078, UniProt:RELATED-TO:P04770, UniProt:RELATED-TO:P04771, UniProt:RELATED-TO:P04772, UniProt:RELATED-TO:P05457, UniProt:RELATED-TO:P07694, UniProt:RELATED-TO:P07804, UniProt:RELATED-TO:P08281, UniProt:RELATED-TO:P08282, UniProt:RELATED-TO:P09606, UniProt:RELATED-TO:P09826, UniProt:RELATED-TO:P0A1P6, UniProt:RELATED-TO:P0A9C5, UniProt:RELATED-TO:P0A040, UniProt:RELATED-TO:P10583, UniProt:RELATED-TO:P10656, UniProt:RELATED-TO:P11600, UniProt:RELATED-TO:P12424, UniProt:RELATED-TO:P12425, UniProt:RELATED-TO:P13564, UniProt:RELATED-TO:P14636, UniProt:RELATED-TO:P14654, UniProt:RELATED-TO:P14655, UniProt:RELATED-TO:P14656, UniProt:RELATED-TO:P15102, UniProt:RELATED-TO:P15103, UniProt:RELATED-TO:P15105, UniProt:RELATED-TO:P15106, UniProt:RELATED-TO:P15124, UniProt:RELATED-TO:P15623, UniProt:RELATED-TO:P16580, UniProt:RELATED-TO:P19064, UniProt:RELATED-TO:P19432, UniProt:RELATED-TO:P19904, UniProt:RELATED-TO:P20479, UniProt:RELATED-TO:P21154, UniProt:RELATED-TO:P22248, UniProt:RELATED-TO:P22878, UniProt:RELATED-TO:P23712, UniProt:RELATED-TO:P23794, UniProt:RELATED-TO:P24099, UniProt:RELATED-TO:P25462, UniProt:RELATED-TO:P28786, UniProt:RELATED-TO:P31592, UniProt:RELATED-TO:P32288, UniProt:RELATED-TO:P38559, UniProt:RELATED-TO:P38560, UniProt:RELATED-TO:P38561, UniProt:RELATED-TO:P38562, UniProt:RELATED-TO:P38563, UniProt:RELATED-TO:P43386, UniProt:RELATED-TO:P43518, UniProt:RELATED-TO:P43794, UniProt:RELATED-TO:P45627, UniProt:RELATED-TO:P46410, UniProt:RELATED-TO:P51118, UniProt:RELATED-TO:P51119, UniProt:RELATED-TO:P52783, UniProt:RELATED-TO:Q7M314, UniProt:RELATED-TO:Q8X7G0, UniProt:RELATED-TO:Q9C8C7, UniProt:RELATED-TO:Q9CDL9, UniProt:RELATED-TO:Q9FHR0, UniProt:RELATED-TO:Q9JSU6, UniProt:RELATED-TO:Q9PPK8, UniProt:RELATED-TO:Q9RDW7, UniProt:RELATED-TO:Q9UWN1, UniProt:RELATED-TO:Q02154, UniProt:RELATED-TO:Q04831, UniProt:RELATED-TO:Q05542, UniProt:RELATED-TO:Q05650, UniProt:RELATED-TO:Q07939, UniProt:RELATED-TO:Q27747, UniProt:RELATED-TO:Q42623, UniProt:RELATED-TO:Q42624, UniProt:RELATED-TO:Q42625, UniProt:RELATED-TO:Q42688, UniProt:RELATED-TO:Q42689, UniProt:RELATED-TO:Q42802, UniProt:RELATED-TO:Q42950, UniProt:RELATED-TO:Q42951, UniProt:RELATED-TO:Q43066, UniProt:RELATED-TO:Q43127, UniProt:RELATED-TO:Q43759, UniProt:RELATED-TO:Q43760, UniProt:RELATED-TO:Q53045, UniProt:RELATED-TO:Q59195, UniProt:RELATED-TO:Q59972, UniProt:RELATED-TO:Q59982, UniProt:RELATED-TO:Q60182


References

ELLIOTT53: ELLIOTT WH (1953). "Isolation of glutamine synthetase and glutamotransferase from green peas." J Biol Chem 201(2);661-72. PMID: 13061404

FRY55: FRY BA (1955). "Glutamine synthesis by Micrococcus pyogenes var. aureus." Biochem J 59(4);579-89. PMID: 14363150

LAJTHA53: LAJTHA A, MELA P, WAELSCH H (1953). "Manganese-dependent glutamotransferase." J Biol Chem 205(2);553-64. PMID: 13129232

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Woolfolk66: Woolfolk CA, Shapiro B, Stadtman ER (1966). "Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli." Arch Biochem Biophys 116(1);177-92. PMID: 5336023


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
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