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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 acid all carboxy acids a carboxylate an amino acid a polar amino acid a negatively-charged polar amino acid
an acid all carboxy acids a carboxylate an amino acid an alpha amino acid a standard alpha amino acid
an acid all carboxy acids a carboxylate an amino acid an L-amino acid
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

L-aspartate compound structure

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+

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

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+

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

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

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

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

NAD biosynthesis I (from aspartate) :
L-aspartate + oxygen → hydrogen peroxide + 2-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 → 2-iminosuccinate + succinate + H+

Reactions known to produce the compound:

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

Not in pathways:
a dipetide with an N-terminal L-aspartate + 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

Not in pathways:
a peptide with an N-terminal X-L-proline + H2O → a standard α amino acid + a peptide with an N-terminal L-proline + H+
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
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

Not in pathways:
a polypeptide + H2O → a polypeptide + an L-amino acid

Not in pathways:
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-acyl 2-lyso-phosphatidylcholine + H2O → a carboxylate + sn-glycero-3-phosphocholine + H+

Reactions known to both consume and produce the compound:

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

L-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

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

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

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 (Competitive) of: asparaginase [Jayaram86]

Inhibitor (Allosteric) of: phosphoenolpyruvate carboxylase [Izui81]

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

This compound has been characterized as an alternative substrate of the following enzymes: tyrosine aminotransferase , phenylalanine aminotransferase

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

Jayaram86: Jayaram HN, Cooney DA, Huang CY (1986). "Interaction between L-aspartic acid and L-asparaginase from Escherichia coli: binding and inhibition studies." J Enzyme Inhib 1(2);151-61. PMID: 3334241

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 19.0 on Sat Jul 4, 2015, biocyc12.