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

Abbrev Name: asp

Synonyms: L-aspartic acid, aspartic acid, D, aspartate, asp, L-asp

Superclasses: an acid all carboxy acids a carboxylate a dicarboxylate a C4-dicarboxylate
an amino acid or its derivative an amino acid a polar amino acid a negatively-charged 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: C4H6NO4

Molecular Weight: 132.1 Daltons

Monoisotopic Molecular Weight: 133.0375077183 Daltons

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

InChI: InChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/p-1/t2-/m0/s1

InChIKey: InChIKey=CKLJMWTZIZZHCS-REOHCLBHSA-M

Unification Links: CAS:56-84-8 , ChEBI:29991 , ChemSpider:4573879 , HMDB:HMDB00191 , IAF1260:33663 , KEGG:C00049 , MetaboLights:MTBLC29991 , PubChem:5460294

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -167.1

Reactions known to consume the compound:

adenosine ribonucleotides de novo biosynthesis :
L-aspartate + IMP + GTP → adenylo-succinate + GDP + phosphate + 2 H+

arginine biosynthesis I (via L-ornithine) :
L-aspartate + L-citrulline + ATP → L-arginino-succinate + AMP + diphosphate + H+

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

asparagine biosynthesis II :
L-aspartate + ammonium + ATP → L-asparagine + AMP + diphosphate + H+

β-alanine biosynthesis III :
L-aspartate + H+ → β-alanine + CO2

homoserine biosynthesis , lysine biosynthesis I :
L-aspartate + ATP → L-aspartyl-4-phosphate + ADP

inosine-5'-phosphate biosynthesis I :
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate → ADP + 5'-phosphoribosyl-4-(N-succinocarboxamide)-5-aminoimidazole + phosphate + H+

NAD biosynthesis I (from aspartate) :
L-aspartate + oxygen → hydrogen peroxide + α-iminosuccinate + H+

tRNA charging :
tRNAasp + L-aspartate + ATP + H+ → L-aspartyl-tRNAasp + AMP + diphosphate

UMP biosynthesis :
L-aspartate + carbamoyl-phosphate → N-carbamoyl-L-aspartate + phosphate + H+

Not in pathways:
L-aspartate + fumarate → α-iminosuccinate + succinate + H+

Reactions known to produce the compound:

asparagine degradation I , superpathway of aspartate and asparagine biosynthesis; interconversion of aspartate and asparagine :
L-asparagine + H2O → L-aspartate + ammonium

Not in pathways:
a dipetide with L-aspartate at the N-terminal + H2O → L-aspartate + a standard α amino acid
L-alanyl-L-aspartate + H2O → L-alanine + L-aspartate
glycyl-L-aspartate + H2O → glycine + L-aspartate
β-aspartyl dipeptide + H2O → L-aspartate + a standard α amino acid


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)
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 carboxylic ester + H2O → an alcohol + a carboxylate + H+
an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+
an acyl phosphate + H2O → a carboxylate + phosphate + H+
an acyl-CoA + H2O → a carboxylate + coenzyme A + H+
a 1-lysophosphatidylcholine + H2O → a carboxylate + sn-glycero-3-phosphocholine + H+


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

Reactions known to both consume and produce the compound:

aspartate biosynthesis :
L-aspartate + 2-oxoglutarate ↔ oxaloacetate + L-glutamate

glutamate degradation II :
L-aspartate ↔ ammonium + fumarate
L-aspartate + 2-oxoglutarate ↔ oxaloacetate + L-glutamate

Not in pathways:
pyridoxamine + oxaloacetate ↔ pyridoxal + L-aspartate

In Reactions of unknown directionality:

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


an aldehyde[periplasmic space] + FAD[periplasmic space] + H2O[periplasmic space] = a carboxylate[periplasmic space] + FADH2[periplasmic space]


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:
L-aspartate[periplasmic space] + 2 H+[periplasmic space]L-aspartate[cytosol] + 2 H+[cytosol] ,
succinate[cytosol] + L-aspartate[periplasmic space]L-aspartate[cytosol] + succinate[periplasmic space] ,
ATP + L-aspartate[periplasmic space] + H2O → L-aspartate[cytosol] + ADP + phosphate + H+ ,
L-aspartate[periplasmic space]L-aspartate[cytosol] ,
a C4-dicarboxylate[periplasmic space] + 2 H+[periplasmic space]a C4-dicarboxylate[cytosol] + 2 H+[cytosol] ,
a C4-dicarboxylate[periplasmic space] + 3 H+[periplasmic space]a C4-dicarboxylate[cytosol] + 3 H+[cytosol] ,
an L-amino acid[cytosol]an L-amino acid[periplasmic space]

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

Activator (Allosteric) of: malate dehydrogenase, NAD-requiring [Milne79]

Activator (Mechanism unknown) of: malate dehydrogenase [Bologna07] , aspartate ammonia-lyase [Ida85]

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

Inhibitor (Allosteric) of: phosphoenolpyruvate carboxylase [Izui81]

Inhibitor (Mechanism unknown) of: L-glutamate:NADP+ oxidoreductase (transaminating) [Miller72] , pyridoxamine-oxaloacetate transaminase [WADA62, Comment 1]

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


References

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

Ida85: Ida N, Tokushige M (1985). "L-Aspartate-induced activation of aspartase." J Biochem (Tokyo) 98(1);35-9. PMID: 3900058

Izui81: Izui K, Taguchi M, Morikawa M, Katsuki H (1981). "Regulation of Escherichia coli phosphoenolpyruvate carboxylase by multiple effectors in vivo. II. Kinetic studies with a reaction system containing physiological concentrations of ligands." J Biochem 90(5);1321-31. PMID: 7040354

Miller72: Miller RE, Stadtman ER (1972). "Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein." J Biol Chem 247(22);7407-19. PMID: 4565085

Milne79: Milne JA, Cook RA (1979). "Role of metal cofactors in enzyme regulation. Differences in the regulatory properties of the Escherichia coli nicotinamide adenine dinucleotide specific malic enzyme depending on whether Mg2+ or Mn2+ serves as divalent cation." Biochemistry 18(16);3604-10. PMID: 224913

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


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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 Thu Dec 18, 2014, biocyc14.