| Identification | |||||||||||||||||||||||||||||||||||||
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| Name | L-Aspartic Acid | ||||||||||||||||||||||||||||||||||||
| Accession Number | DB00128 (EXPT01823, NUTR00016) | ||||||||||||||||||||||||||||||||||||
| Type | small molecule | ||||||||||||||||||||||||||||||||||||
| Groups | approved, nutraceutical | ||||||||||||||||||||||||||||||||||||
| Description | One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter. [PubChem] |
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| Structure |
Download: MOL | SDF | SMILES | InChI Display: 2D Structure | 3D Structure |
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| Synonyms |
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| Brand names |
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| Brand name mixtures | Not Available | ||||||||||||||||||||||||||||||||||||
| Categories |
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| CAS number | 56-84-8 | ||||||||||||||||||||||||||||||||||||
| Weight |
Average: 133.1027 Monoisotopic: 133.037507717 |
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| Chemical Formula | C4H7NO4 | ||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=CKLJMWTZIZZHCS-REOHCLBHSA-N | ||||||||||||||||||||||||||||||||||||
| InChI |
InChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m0/s1
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| IUPAC Name |
(2S)-2-aminobutanedioic acid
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| SMILES |
N[C@@H](CC(O)=O)C(O)=O
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| Mass Spec | show (3 KB) | ||||||||||||||||||||||||||||||||||||
| Taxonomy | |||||||||||||||||||||||||||||||||||||
| Kingdom | Organic | ||||||||||||||||||||||||||||||||||||
| Classes |
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| Substructures |
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| Pharmacology | |||||||||||||||||||||||||||||||||||||
| Indication | There is no support for the claim that aspartates are exercise performance enhancers, i.e. ergogenic aids. | ||||||||||||||||||||||||||||||||||||
| Pharmacodynamics | L-aspartate is considered a non-essential amino acid, meaning that, under normal physiological conditions, sufficient amounts of the amino acid are synthesized in the body to meet the body's requirements. L-aspartate is formed by the transamination of the Krebs cycle intermediate oxaloacetate. The amino acid serves as a precursor for synthesis of proteins, oligopeptides, purines, pyrimidines, nucleic acids and L-arginine. L-aspartate is a glycogenic amino acid, and it can also promote energy production via its metabolism in the Krebs cycle. These latter activities were the rationale for the claim that supplemental aspartate has an anti-fatigue effect on skeletal muscle, a claim that was never confirmed. | ||||||||||||||||||||||||||||||||||||
| Mechanism of action | There are also claims that L-aspartate has ergogenic effects, that it enhances performance in both prolonged exercise and short intensive exercise. It is hypothesized that L-aspartate, especially the potassium magnesium aspartate salt, spares stores of muscle glycogen and/or promotes a faster rate of glycogen resynthesis during exercise. It has also been hypothesized that L-aspartate can enhance short intensive exercise by serving as a substrate for energy production in the Krebs cycle and for stimulating the purine nucleotide cycle. | ||||||||||||||||||||||||||||||||||||
| Absorption | Absorbed from the small intestine by an active transport process | ||||||||||||||||||||||||||||||||||||
| Volume of distribution | Not Available | ||||||||||||||||||||||||||||||||||||
| Protein binding | Not Available | ||||||||||||||||||||||||||||||||||||
| Metabolism | |||||||||||||||||||||||||||||||||||||
| Route of elimination | Not Available | ||||||||||||||||||||||||||||||||||||
| Half life | Not Available | ||||||||||||||||||||||||||||||||||||
| Clearance | Not Available | ||||||||||||||||||||||||||||||||||||
| Toxicity | Mild gastrointestinal side effects including diarrhea. LD50 (rat) > 5,000 mg/kg. | ||||||||||||||||||||||||||||||||||||
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| Pathways | Not Available | ||||||||||||||||||||||||||||||||||||
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| Manufacturers | Not Available | ||||||||||||||||||||||||||||||||||||
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| Dosage forms | Not Available | ||||||||||||||||||||||||||||||||||||
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| Patents | Not Available | ||||||||||||||||||||||||||||||||||||
| Properties | |||||||||||||||||||||||||||||||||||||
| State | solid | ||||||||||||||||||||||||||||||||||||
| Melting point | 230 oC | ||||||||||||||||||||||||||||||||||||
| Experimental Properties |
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| Predicted Properties |
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| Synthesis Reference | Not Available | ||||||||||||||||||||||||||||||||||||
| General Reference | Not Available | ||||||||||||||||||||||||||||||||||||
| External Links |
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| ATC Codes |
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| AHFS Codes | Not Available | ||||||||||||||||||||||||||||||||||||
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| FDA label | Not Available | ||||||||||||||||||||||||||||||||||||
| MSDS | show (72.8 KB) | ||||||||||||||||||||||||||||||||||||
| Interactions | |||||||||||||||||||||||||||||||||||||
| Drug Interactions |
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| Food Interactions | Not Available | ||||||||||||||||||||||||||||||||||||
| Targets |
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Pharmacological action: unknown
Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA Organism class: humanUniProt ID: P07998 ![]() Gene: RNASE1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
2. Lysozyme C Pharmacological action: unknownOrganism class: human UniProt ID: P61626 ![]() Gene: LYZ SNPs: SNPJam Report ![]() References:
3. Calcium-binding mitochondrial carrier protein Aralar2 Pharmacological action: unknownCalcium-dependent mitochondrial aspartate and glutamate carrier. May have a function in the urea cycle Organism class: humanUniProt ID: Q9UJS0 ![]() Gene: SLC25A13 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
4. Aspartate aminotransferase, cytoplasmic Pharmacological action: unknownOrganism class: human UniProt ID: P17174 ![]() Gene: GOT1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
5. Mitochondrial aspartate-glutamate carrier protein Pharmacological action: unknownCalcium-dependent mitochondrial aspartate and glutamate carrier. May have a function in the urea cycle Organism class: humanUniProt ID: Q546F9 ![]() Gene: SLC25A13 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids Organism class: humanUniProt ID: P45381 ![]() Gene: ASPA ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
7. Asparagine synthetase [glutamine-hydrolyzing] Pharmacological action: unknownOrganism class: human UniProt ID: P08243 ![]() Gene: ASNS ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: P00966 ![]() Gene: ASS1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) Organism class: humanUniProt ID: Q03154 ![]() Gene: ACY1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
10. Aspartate aminotransferase, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: P00505 ![]() Gene: GOT2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
11. Aspartyl-tRNA synthetase, cytoplasmic Pharmacological action: unknownOrganism class: human UniProt ID: P14868 ![]() Gene: DARS ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
12. Calcium-binding mitochondrial carrier protein Aralar1 Pharmacological action: unknownCalcium-dependent mitochondrial aspartate and glutamate carrier. May have a function in the urea cycle Organism class: humanUniProt ID: O75746 ![]() Gene: SLC25A12 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
13. Aspartyl/asparaginyl beta-hydroxylase Pharmacological action: unknownSpecifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins Organism class: humanUniProt ID: Q12797 ![]() Gene: ASPH ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
14. Multifunctional protein ADE2 [Includes: Phosphoribosylaminoimidazole- succinocarboxamide synthase Pharmacological action: unknownATP + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate Organism class: humanUniProt ID: P22234 ![]() Gene: PAICS ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 15. CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase Pharmacological action: unknownThis protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase) Organism class: humanUniProt ID: P27708 ![]() Gene: CAD ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 16. Adenylosuccinate synthetase isozyme 2 Pharmacological action: unknownPlays an important role in the de novo pathway of purine nucleotide biosynthesis Organism class: humanUniProt ID: P30520 ![]() Gene: ADSS ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
17. Excitatory amino acid transporter 3 Pharmacological action: unknownTransports L-glutamate and also L- and D-aspartate. Essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic cleft. Acts as a symport by cotransporting sodium. Negatively regulated by ARL6IP5 Organism class: humanUniProt ID: P43005 ![]() Gene: SLC1A1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
18. Growth-inhibiting protein 18 Pharmacological action: unknownL-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate Organism class: humanUniProt ID: Q2TU84 ![]() Gene: GIG18 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 19. Adenylosuccinate synthetase Pharmacological action: unknownPlays an important role in the de novo pathway of purine nucleotide biosynthesis Organism class: humanUniProt ID: Q5SY84 ![]() Gene: ADSS ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
20. Argininosuccinate synthase Pharmacological action: unknownOrganism class: human UniProt ID: Q5T6L4 ![]() Gene: ASS1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
21. Aspartyl-tRNA synthetase, mitochondrial Pharmacological action: unknownATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp) Organism class: humanUniProt ID: Q6PI48 ![]() Gene: DARS2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
22. ASRGL1 protein Pharmacological action: unknownOrganism class: human UniProt ID: Q7L266 ![]() Gene: ASRGL1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 23. Adenylosuccinate synthetase isozyme 1 Pharmacological action: unknownPlays an important role in the de novo pathway of purine nucleotide biosynthesis Organism class: humanUniProt ID: Q8N142 ![]() Gene: ADSSL1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 24. Aspartoacylase-2 Pharmacological action: unknownN-acyl-L-aspartate + H(2)O = a carboxylate + L-aspartate Organism class: humanUniProt ID: Q96HD9 ![]() Gene: ACY3 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: |
| Transporters |
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1. Monocarboxylate transporter 10 Actions: inhibitorSodium-independent transporter that mediates the update of aromatic acid. Can function as a net efflux pathway for aromatic amino acids in the basosolateral epithelial cells (By similarity) UniProt ID: Q8TF71![]() Gene: SLC16A10 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
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| Comments |
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This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.