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

Abbrev Name: glt

Synonyms: 1-amino-propane-1,3-dicarboxylic acid, glutacid, glutaminic acid, L-glutamic acid, α-aminoglutaric acid, E, glt, glu, glut, L-glu, 2-aminopentanedioic acid

Superclasses: an acidall carboxy acidsa carboxylatean amino acida glutamate
an acidall carboxy acidsa carboxylatean amino acida polar amino acida negatively-charged polar amino acid
an acidall carboxy acidsa carboxylatean amino acidan alpha amino acida standard alpha amino acid
an acidall carboxy acidsa carboxylatean amino acidan L-amino acid
an amino acid or its derivativean amino acida glutamate
an amino acid or its derivativean amino acida polar amino acida negatively-charged polar amino acid
an amino acid or its derivativean amino acidan alpha amino acida standard alpha amino acid
an amino acid or its derivativean amino acidan L-amino acid


Chemical Formula: C5H8NO4

Molecular Weight: 146.12 Daltons

Monoisotopic Molecular Weight: 148.0609828146 Daltons

L-glutamate compound structure

pKa 1: 2.19

pKa 2: 4.25

pKa 3: 9.67

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

InChI: InChI=1S/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10)/p-1/t3-/m0/s1

InChIKey: InChIKey=WHUUTDBJXJRKMK-VKHMYHEASA-M

Unification Links: CAS:56-86-0, ChEBI:29985, ChemSpider:4573882, HMDB:HMDB00148, IAF1260:33561, KEGG:C00025, KNApSAcK:C00001358, MetaboLights:MTBLC29985, PubChem:5460299

Standard Gibbs Free Energy of Formation (ΔfG in kcal/mol): -164.13

Reactions known to consume the compound:

folate polyglutamylation :
methylene-tetrahydropteroyl-[γ-Glu](n) + L-glutamate + ATP → methylene-tetrahydropteroyl-[γ-Glu](n+1) + ADP + phosphate
10-formyl-tetrahydropteroyl-[γ-Glu](n) + L-glutamate + ATP → 10-formyl-tetrahydropteroyl-[γ-Glu](n+1) + ADP + phosphate
tetrahydropteroyl-[γ-Glu](n) + L-glutamate + ATP → tetrahydropteroyl-[γ-Glu](n+1) + ADP + phosphate

glutathione biosynthesis :
L-cysteine + L-glutamate + ATP → γ-L-glutamyl-L-cysteine + ADP + phosphate + H+

L-glutamate degradation IX (via 4-aminobutanoate) :
L-glutamate + H+ → CO2 + 4-aminobutanoate

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

L-histidine biosynthesis :
imidazole acetol-phosphate + L-glutamate → L-histidinol-phosphate + 2-oxoglutarate

L-ornithine biosynthesis I :
N-acetyl-L-ornithine + 2-oxoglutarate ← N-acetyl-L-glutamate 5-semialdehyde + L-glutamate

L-proline biosynthesis I :
L-glutamate + ATP → γ-L-glutamyl 5-phosphate + ADP

putrescine degradation II :
putrescine + L-glutamate + ATP → γ-glutamyl-L-putrescine + ADP + phosphate + H+

tetrahydrofolate biosynthesis :
L-glutamate + 7,8-dihydropteroate + ATP → ADP + 7,8-dihydrofolate monoglutamate + phosphate + H+

tetrapyrrole biosynthesis I (from glutamate) , tRNA charging :
a tRNAglu + L-glutamate + ATP + H+ → an L-glutamyl-[tRNAGlu] + AMP + diphosphate

Not in pathways:
a [protein] C-terminal L-glutamate + L-glutamate + ATP → a [protein] with C-terminal α-L-glutamate-α-L-glutamate + ADP + phosphate + H+
queuosine at position 34 of a tRNAAsp + ATP + L-glutamate → glutamyl-queuosine at position 34 of a tRNAAsp + AMP + diphosphate + 2 H+

Reactions known to produce the compound:

5-aminoimidazole ribonucleotide biosynthesis I :
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-phospho-β-D-ribosylamine + L-glutamate + diphosphate ← 5-phospho-α-D-ribose 1-diphosphate + L-glutamine + H2O

5-aminoimidazole ribonucleotide biosynthesis II :
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-phospho-β-D-ribosylamine + L-glutamate + diphosphate ← 5-phospho-α-D-ribose 1-diphosphate + L-glutamine + H2O

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

hydrogen sulfide biosynthesis I :
2-oxoglutarate + L-cysteine → L-glutamate + 3-mercaptopyruvate

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

L-arginine degradation II (AST pathway) :
N2-succinylglutamate + H2O → succinate + L-glutamate

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

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

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

L-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+

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

muropeptide degradation :
L-alanyl-L-glutamate + H2O → L-alanine + L-glutamate

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

proline degradation :
L-glutamate-5-semialdehyde + NAD+ + H2O → L-glutamate + NADH + 2 H+

putrescine degradation I :
putrescine + 2-oxoglutarate → 4-aminobutanal + L-glutamate

putrescine degradation II :
4-(γ-L-glutamylamino)butanoate + H2O → 4-aminobutanoate + L-glutamate

superpathway of 5-aminoimidazole ribonucleotide biosynthesis :
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-phospho-β-D-ribosylamine + L-glutamate + diphosphate ← 5-phospho-α-D-ribose 1-diphosphate + L-glutamine + H2O

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

Not in pathways:
p-aminobenzoyl glutamate + H2O → 4-aminobenzoate + L-glutamate
glycyl-L-glutamate + H2O → glycine + L-glutamate
glutathione[periplasm] + H2O[periplasm] → L-cysteinyl-glycine[periplasm] + L-glutamate[periplasm]
(S)-1-pyrroline-5-carboxylate + NAD+ + 2 H2O → L-glutamate + NADH + H+

Reactions known to both consume and produce the compound:

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

4-aminobutanoate degradation I , 4-aminobutanoate degradation II :
2-oxoglutarate + 4-aminobutanoate ↔ L-glutamate + succinate semialdehyde

dTDP-N-acetylthomosamine biosynthesis :
dTDP-thomosamine + 2-oxoglutarate ↔ dTDP-4-dehydro-6-deoxy-α-D-glucopyranose + L-glutamate

L-alanine biosynthesis I , L-valine biosynthesis :
L-valine + 2-oxoglutarate ↔ 3-methyl-2-oxobutanoate + L-glutamate

L-alanine biosynthesis II :
2-oxoglutarate + L-alanine ↔ L-glutamate + pyruvate

L-arginine degradation II (AST pathway) :
N2-succinyl-L-ornithine + 2-oxoglutarate ↔ N2-succinyl-L-glutamate 5-semialdehyde + L-glutamate

L-aspartate biosynthesis , L-glutamate degradation II :
L-aspartate + 2-oxoglutarate ↔ oxaloacetate + L-glutamate

L-glutamate biosynthesis III :
L-glutamate + NADP+ + H2O ↔ ammonium + 2-oxoglutarate + NADPH + H+

L-isoleucine biosynthesis I (from threonine) :
L-isoleucine + 2-oxoglutarate ↔ (S)-3-methyl-2-oxopentanoate + L-glutamate

L-leucine biosynthesis :
L-leucine + 2-oxoglutarate ↔ 4-methyl-2-oxopentanoate + L-glutamate

L-lysine biosynthesis I :
2-oxoglutarate + N-succinyl-L,L-2,6-diaminopimelate ↔ L-glutamate + N-succinyl-2-amino-6-ketopimelate

L-ornithine biosynthesis I :
L-glutamate + acetyl-CoA ↔ N-acetyl-L-glutamate + coenzyme A + H+

L-phenylalanine biosynthesis I :
2-oxo-3-phenylpropanoate + L-glutamate ↔ L-phenylalanine + 2-oxoglutarate

L-serine biosynthesis :
3-phospho-L-serine + 2-oxoglutarate ↔ 3-phospho-hydroxypyruvate + L-glutamate

L-tyrosine biosynthesis I :
L-tyrosine + 2-oxoglutarate ↔ 4-hydroxyphenylpyruvate + L-glutamate

polymyxin resistance :
UDP-4-amino-4-deoxy-β-L-arabinopyranose + 2-oxoglutarate ↔ UDP-β-L-threo-pentapyranos-4-ulose + L-glutamate

pyridoxal 5'-phosphate biosynthesis I :
2-oxo-3-hydroxy-4-phosphobutanoate + L-glutamate ↔ 4-phospho-hydroxy-L-threonine + 2-oxoglutarate

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

UDP-N-acetylmuramoyl-pentapeptide biosynthesis I (meso-diaminopimelate containing) :
L-glutamate ↔ D-glutamate

Not in pathways:
an aliphatic α,ω-diamine + 2-oxoglutarate ↔ an aliphatic ω-aminoaldehyde + L-glutamate
an aromatic amino acid + 2-oxoglutarate ↔ an aromatic oxo-acid + L-glutamate
L-kynurenine + 2-oxoglutarate ↔ L-glutamate + 4-(2-aminophenyl)-2,4-dioxobutanoate
putrescine + 2-oxoglutarate ↔ L-glutamate + 1-pyrroline + H2O

In Reactions of unknown directionality:

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

Not in pathways:
a 5-L-glutamyl-[peptide][periplasm] + an amino acid[periplasm] = a 5-L-glutamyl-amino acid[periplasm] + a peptide[periplasm]

Not in pathways:
a 2-acyl 1-lyso-phosphatidylcholine + H2O = a carboxylate + sn-glycero-3-phosphocholine + H+
an aldehyde[periplasm] + FAD[periplasm] + H2O[periplasm] = a carboxylate[periplasm] + FADH2[periplasm]

In Transport reactions:
4-aminobutanoate[cytosol] + L-glutamate[periplasm]L-glutamate[cytosol] + 4-aminobutanoate[periplasm],
2 Na+[periplasm] + L-glutamate[periplasm] → 2 Na+[cytosol] + L-glutamate[cytosol],
L-glutamate[periplasm] + 2 H+[periplasm]L-glutamate[cytosol] + 2 H+[cytosol],
ATP + L-glutamate[periplasm] + H2O → ADP + L-glutamate[cytosol] + phosphate + H+,
an amino acid[periplasm]an amino acid[extracellular space]

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

Activator (Allosteric) of: glutaminase B [Prusiner76, Prusiner76a] Activator (Mechanism unknown) of: malate dehydrogenase [Bologna07]

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

Inhibitor (Competitive) of: diaminopimelate decarboxylase [White65], glutaminase B [Prusiner76, Comment 1], L-glutamine:D-fructose-6-phosphate aminotransferase [Badet88, Isupov96, Comment 2], glutaminase [Hartman68] Inhibitor (Mechanism unknown) of: pyridoxamine-oxaloacetate transaminase [WADA62, Comment 3]

This compound has been characterized as an alternative substrate of the following enzymes: valine-pyruvate aminotransferase

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


References

Badet88: Badet B, Vermoote P, Le Goffic F (1988). "Glucosamine synthetase from Escherichia coli: kinetic mechanism and inhibition by N3-fumaroyl-L-2,3-diaminopropionic derivatives." Biochemistry 1988;27(7);2282-7. PMID: 3132968

Bologna07: Bologna FP, Andreo CS, Drincovich MF (2007). "Escherichia coli malic enzymes: two isoforms with substantial differences in kinetic properties, metabolic regulation, and structure." J Bacteriol 189(16);5937-46. PMID: 17557829

Hartman68: Hartman SC (1968). "Glutaminase of Escherichia coli. I. Purification and general catalytic properties." J Biol Chem 1968;243(5);853-63. PMID: 4966660

Isupov96: Isupov MN, Obmolova G, Butterworth S, Badet-Denisot MA, Badet B, Polikarpov I, Littlechild JA, Teplyakov A (1996). "Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 A crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase." Structure 4(7);801-10. PMID: 8805567

Prusiner76: Prusiner S, Stadtman ER (1976). "Regulation of glutaminase B in Escherichia coli. II. Modulaltion of activity by carbosylate and borate ions." J Biol Chem 1976;251(11);3457-62. PMID: 776969

Prusiner76a: Prusiner S, Stadtman ER (1976). "Regulation of glutaminase B in Escherichia coli. III. Control by nucleotides and divalent cations." J Biol Chem 1976;251(11);3463-9. PMID: 776970

WADA62: WADA H, SNELL EE (1962). "Enzymatic transamination of pyridoxamine. I. With oxaloacetate and alpha-ketoglutarate." J Biol Chem 237;127-32. PMID: 14004226

White65: White PJ, Kelly B (1965). "Purification and properties of diaminopimelate decarboxylase from Escherichia coli." Biochem J 96;75-84. PMID: 14343156


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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