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Escherichia coli K-12 substr. MG1655 Compound: L-glutamine

Abbrev Name: gln

Synonyms: Q, proglumide, glum, gln, glutamine, glumin, 2-aminoglutaramic acid, glutamic acid 5-amide, L-gln

Superclasses: an amino acid or its derivative an amino acid a neutral amino acid
an amino acid or its derivative an amino acid a polar amino acid an uncharged polar amino acid
an amino acid or its derivative an amino acid an alpha amino acid a standard alpha amino acid
an amino acid or its derivative an amino acid an L-amino acid

Chemical Formula: C5H10N2O3

Molecular Weight: 146.15 Daltons

Monoisotopic Molecular Weight: 146.0691421977 Daltons

pKa 1: 2.17

pKa 2: 9.13

SMILES: C(=O)(N)CCC([N+])C([O-])=O

InChI: InChI=1S/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)/t3-/m0/s1

InChIKey: InChIKey=ZDXPYRJPNDTMRX-VKHMYHEASA-N

Unification Links: CAS:56-85-9 , ChEBI:58359 , HMDB:HMDB00641 , IAF1260:33714 , KEGG:C00064 , MetaboLights:MTBLC58359 , PubChem:6992086

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -126.2

Reactions known to consume the compound:

5-aminoimidazole ribonucleotide biosynthesis I :
5-phospho-β-D-ribosylamine + L-glutamate + diphosphate ← 5-phospho-α-D-ribose 1-diphosphate + L-glutamine + H2O
ATP + N2-formyl-N1-(5-phospho-β-D-ribosyl)glycinamide + L-glutamine + H2O → ADP + 2-(formamido)-N1-(5-phospho-β-D-ribosyl)acetamidine + L-glutamate + phosphate + H+

5-aminoimidazole ribonucleotide biosynthesis II :
5-phospho-β-D-ribosylamine + L-glutamate + diphosphate ← 5-phospho-α-D-ribose 1-diphosphate + L-glutamine + H2O
ATP + N2-formyl-N1-(5-phospho-β-D-ribosyl)glycinamide + L-glutamine + H2O → ADP + 2-(formamido)-N1-(5-phospho-β-D-ribosyl)acetamidine + L-glutamate + phosphate + H+

arginine biosynthesis I (via L-ornithine) , UMP biosynthesis :
2 ATP + L-glutamine + hydrogen carbonate + H2O → carbamoyl-phosphate + L-glutamate + 2 ADP + phosphate + 2 H+

asparagine biosynthesis I :
L-glutamine + L-aspartate + ATP + H2O → L-glutamate + L-asparagine + AMP + diphosphate + H+

glutamate biosynthesis I :
2 L-glutamate + NADP+L-glutamine + 2-oxoglutarate + NADPH + H+

glutamine degradation I :
L-glutamine + H2O → L-glutamate + ammonium

guanosine ribonucleotides de novo biosynthesis :
L-glutamine + XMP + ATP + H2O → L-glutamate + GMP + AMP + diphosphate + 2 H+

histidine biosynthesis :
phosphoribulosylformimino-AICAR-P + L-glutamine → L-glutamate + D-erythro-imidazole-glycerol-phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide + H+

NAD biosynthesis I (from aspartate) , NAD salvage pathway I :
ATP + nicotinate adenine dinucleotide + L-glutamine + H2O → AMP + L-glutamate + NAD+ + diphosphate + H+

superpathway of 5-aminoimidazole ribonucleotide biosynthesis :
5-phospho-β-D-ribosylamine + L-glutamate + diphosphate ← 5-phospho-α-D-ribose 1-diphosphate + L-glutamine + H2O
ATP + N2-formyl-N1-(5-phospho-β-D-ribosyl)glycinamide + L-glutamine + H2O → ADP + 2-(formamido)-N1-(5-phospho-β-D-ribosyl)acetamidine + L-glutamate + phosphate + H+

tRNA charging :
tRNAgln + L-glutamine + ATP + H+ → L-glutaminyl-tRNAgln + AMP + diphosphate

tryptophan biosynthesis :
chorismate + L-glutamine → anthranilate + pyruvate + L-glutamate + H+

UTP and CTP de novo biosynthesis :
ATP + UTP + L-glutamine + H2O → ADP + CTP + L-glutamate + phosphate + 2 H+

Reactions known to produce the compound:

glutamine biosynthesis I , Nitrogen Regulation Two-Component System :
ammonium + L-glutamate + ATP → L-glutamine + ADP + phosphate + H+

Not in pathways:
L-alanyl-L-glutamine + H2O → L-alanine + L-glutamine
glycyl-L-glutamine + H2O → glycine + L-glutamine


a peptide + H2O → a standard α amino acid + a peptide
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a standard α amino acid + a peptide
amino acids(n) + H2O → a standard α amino acid + amino acids(n-1)
β-aspartyl dipeptide + H2O → L-aspartate + a standard α amino acid
a dipetide with L-aspartate at the N-terminal + H2O → L-aspartate + a standard α amino acid
a tripeptide + H2O → a dipeptide + a standard α amino acid
a dipeptide with proline at the C-terminal + H2O → L-proline + a standard α amino acid
a dipeptide + H2O → 2 a standard α amino acid


a polypeptide + H2O → a polypeptide + an L-amino acid

Reactions known to both consume and produce the compound:

4-aminobenzoate biosynthesis :
L-glutamine + chorismate ↔ 4-amino-4-deoxychorismate + L-glutamate

UDP-N-acetyl-D-glucosamine biosynthesis I :
β-D-fructofuranose 6-phosphate + L-glutamine ↔ D-glucosamine 6-phosphate + L-glutamate

In Reactions of unknown directionality:

Not in pathways:
L-methionine + a 2-oxo carboxylate = 2-oxo-4-methylthiobutanoate + a standard α amino acid


a 5-L-glutamyl-[peptide][periplasmic space] + an amino acid[periplasmic space] = a 5-L-glutamyl-amino acid[periplasmic space] + a peptide[periplasmic space]

In Transport reactions:
ATP + L-glutamine[periplasmic space] + H2O → ADP + L-glutamine[cytosol] + phosphate + H+ ,
an L-amino acid[cytosol]an L-amino acid[periplasmic space]

Enzymes activated by L-glutamine, sorted by the type of activation, are:

Activator (Mechanism unknown) of: glutamine synthetase adenylyltransferase [Kingdon67]

Enzymes inhibited by L-glutamine, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: glutamate dehydrogenase [Sakamoto75]

Inhibitor (Mechanism unknown) of: glutamine synthetase deadenylase [Shapiro69, Shapiro68] , [protein-PII] uridylyltransferase [Adler75, Atkinson94a, Kamberov95]

In Growth Media: Neidhardt EZ rich defined medium , Gutnick minimal salts medium base + gln , PMA nitrogen source test + gln , PMA carbon source test + gln


References

Adler75: Adler SP, Purich D, Stadtman ER (1975). "Cascade control of Escherichia coli glutamine synthetase. Properties of the PII regulatory protein and the uridylyltransferase-uridylyl-removing enzyme." J Biol Chem 1975;250(16);6264-72. PMID: 239942

Atkinson94a: Atkinson MR, Kamberov ES, Weiss RL, Ninfa AJ (1994). "Reversible uridylylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator I (NRI or NtrC)." J Biol Chem 1994;269(45);28288-93. PMID: 7961766

Kamberov95: Kamberov ES, Atkinson MR, Ninfa AJ (1995). "The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP." J Biol Chem 1995;270(30);17797-807. PMID: 7629080

Kingdon67: Kingdon HS, Shapiro BM, Stadtman ER (1967). "Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase." Proc Natl Acad Sci U S A 1967;58(4);1703-10. PMID: 4867671

Sakamoto75: Sakamoto N, Kotre AM, Savageau MA (1975). "Glutamate dehydrogenase from Escherichia coli: purification and properties." J Bacteriol 1975;124(2);775-83. PMID: 241744

Shapiro68: Shapiro BM, Stadtman ER (1968). "Glutamine synthetase deadenylylating enzyme." Biochem Biophys Res Commun 1968;30(1);32-7. PMID: 4866293

Shapiro69: Shapiro BM (1969). "The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements." Biochemistry 8(2);659-70. PMID: 4893578


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Nov 24, 2014, BIOCYC14B.