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targets (6) transporters (1)
for drugs
Identification
Name L-Asparagine
Accession Number DB00174 (NUTR00015)
Type small molecule
Groups approved, nutraceutical
Description

A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from aspartic acid and ammonia by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
Structure Thumb
Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure
Synonyms
(-)-Asparagine
(S)-2,4-Diamino-4-oxobutanoic acid
(S)-Asparagine
2-Aminosuccinamic acid
a-Aminosuccinamic acid
Asn
Asparagine
Asparagine acid
Asparamide
Aspartamic acid
Aspartic acid amide
Aspartic acid b-amide
L-2,4-Diamino-4-oxobutanoic acid
L-Aspartamine
L-b-Asparagine
First Prev Next Last
Salts Not Available
Brand names
Name Company
Agedoite
Altheine
Crystal VI
Brand mixtures Not Available
Categories
  • Dietary supplement
  • Micronutrient
  • Non-Essential Amino Acids
CAS number 70-47-3
Weight Average: 132.1179
Monoisotopic: 132.053492132
Chemical Formula C4H8N2O3
InChI Key InChIKey=DCXYFEDJOCDNAF-REOHCLBHSA-N
InChI
InChI=1S/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1
Plain Text
IUPAC Name
(2S)-2-amino-3-carbamoylpropanoic acid
SMILES
N[C@@H](CC(N)=O)C(O)=O
Plain Text
Mass Spec show (2.96 KB)
Taxonomy
Kingdom Organic
Classes
  • Amino Acids
  • Carboxylic Acids and Derivatives
  • Keto-Acids
Substructures
  • Amino Acids
  • Hydroxy Compounds
  • Acetates
  • Amino Ketones
  • Aliphatic and Aryl Amines
  • Carboxylic Acids and Derivatives
  • Carbamates and Derivatives
  • Carboxamides and Derivatives
  • Keto-Acids
Pharmacology
Indication Used for nutritional supplementation, also for treating dietary shortage or imbalance.
Pharmacodynamics A non-essential amino acid. Asparagine is critical for the production of the body's proteins, enzymes and muscle tissue. Supplements of this amino acid are claimed to balance nervous system function.
Mechanism of action Asparagine, a non-essential amino acid is important in the metabolism of toxic ammonia in the body through the action of asparagine synthase which attaches ammonia to aspartic acid in an amidation reaction. Asparagine is also used as a structural component in many proteins.
Absorption Not Available
Volume of distribution Not Available
Protein binding Not Available
Metabolism
Not Available
Route of elimination Not Available
Half life Not Available
Clearance Not Available
Toxicity Not Available
Affected organisms
  • Humans and other mammals
Pathways Not Available
Pharmacoeconomics
Manufacturers Not Available
Packagers Not Available
Dosage forms Not Available
Prices Not Available
Patents Not Available
Properties
State solid
Experimental Properties
Property Value Source
melting point 234-235 °C PhysProp
water solubility 2.94E+004 mg/L (at 25 °C) YALKOWSKY,SH & DANNENFELSER,RM (1992)
logP -3.82 CHMELIK,J ET AL. (1991)
logS -0.74 ADME Research, USCD
pKa 8.82 (at 18 °C) KORTUM,G ET AL (1961)
Predicted Properties
Property Value Source
water solubility 1.68e+02 g/l ALOGPS
logP -3.4 ALOGPS
logP -4.3 ChemAxon
logS 0.1 ALOGPS
pKa (strongest acidic) 2 ChemAxon
pKa (strongest basic) 8.43 ChemAxon
physiological charge 0 ChemAxon
hydrogen acceptor count 4 ChemAxon
hydrogen donor count 3 ChemAxon
polar surface area 106.41 ChemAxon
rotatable bond count 3 ChemAxon
refractivity 28.35 ChemAxon
polarizability 11.68 ChemAxon
References
Synthesis Reference Not Available
General Reference Not Available
External Links
Resource Link
KEGG Compound C00152 Link_out
PubChem Compound 6267 Link_out
PubChem Substance 46507804 Link_out
ChemSpider 6031 Link_out
ChEBI 17196 Link_out
ChEMBL 17196 Link_out
PharmGKB PA164776968 Link_out
HET ASN Link_out
ATC Codes Not Available
AHFS Codes Not Available
PDB Entries
FDA label Not Available
MSDS show (72.2 KB)
Interactions
Drug Interactions Not Available
Food Interactions Not Available
Targets

1. Neutral amino acid transporter B(0)

Pharmacological action: unknown

Has a broad substrate specificity, a preference for zwitterionic amino acids, and a sodium-dependence. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated amino acids, anionic amino acids, and cationic amino acids. Act as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses

Organism class: human
UniProt ID: Q15758 Link_out
Gene: SLC1A5 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Dun Y, Mysona B, Itagaki S, Martin-Studdard A, Ganapathy V, Smith SB: Functional and molecular analysis of D-serine transport in retinal Muller cells. Exp Eye Res. 2007 Jan;84(1):191-9. Epub 2006 Nov 13. Pubmed
  2. Oppedisano F, Pochini L, Galluccio M, Cavarelli M, Indiveri C: Reconstitution into liposomes of the glutamine/amino acid transporter from renal cell plasma membrane: functional characterization, kinetics and activation by nucleotides. Biochim Biophys Acta. 2004 Dec 15;1667(2):122-31. Pubmed

2. ASRGL1 protein

Pharmacological action: unknown
Organism class: human
UniProt ID: Q7L266 Link_out
Gene: ASRGL1 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed

3. Probable asparaginyl-tRNA synthetase, mitochondrial

Pharmacological action: unknown

ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)

Organism class: human
UniProt ID: Q96I59 Link_out
Gene: NARS2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Iwasaki W, Sekine S, Kuroishi C, Kuramitsu S, Shirouzu M, Yokoyama S: Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase. J Mol Biol. 2006 Jul 7;360(2):329-42. Epub 2006 May 15. Pubmed
  2. Roy H, Becker HD, Reinbolt J, Kern D: When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism. Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9837-42. Epub 2003 Jul 21. Pubmed

4. System N amino acid transporter 1

Pharmacological action: unknown

Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission

Organism class: human
UniProt ID: Q99624 Link_out
Gene: SLC38A3 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed

5. Asparagine synthetase [glutamine-hydrolyzing]

Pharmacological action: unknown
Organism class: human
UniProt ID: P08243 Link_out
Gene: ASNS Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Tesson AR, Soper TS, Ciustea M, Richards NG: Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli. Arch Biochem Biophys. 2003 May 1;413(1):23-31. Pubmed
  2. Fresquet V, Thoden JB, Holden HM, Raushel FM: Kinetic mechanism of asparagine synthetase from Vibrio cholerae. Bioorg Chem. 2004 Apr;32(2):63-75. Pubmed
  3. Chaffei C, Pageau K, Suzuki A, Gouia H, Ghorbel MH, Masclaux-Daubresse C: Cadmium toxicity induced changes in nitrogen management in Lycopersicon esculentum leading to a metabolic safeguard through an amino acid storage strategy. Plant Cell Physiol. 2004 Nov;45(11):1681-93. Pubmed
  4. Al Sarraj J, Vinson C, Thiel G: Regulation of asparagine synthetase gene transcription by the basic region leucine zipper transcription factors ATF5 and CHOP. Biol Chem. 2005 Sep;386(9):873-9. Pubmed
  5. Iwamoto S, Mihara K, Downing JR, Pui CH, Campana D: Mesenchymal cells regulate the response of acute lymphoblastic leukemia cells to asparaginase. J Clin Invest. 2007 Apr;117(4):1049-57. Epub 2007 Mar 22. Pubmed

6. Asparaginyl-tRNA synthetase, cytoplasmic

Pharmacological action: unknown
Organism class: human
UniProt ID: O43776 Link_out
Gene: NARS Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Iwasaki W, Sekine S, Kuroishi C, Kuramitsu S, Shirouzu M, Yokoyama S: Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase. J Mol Biol. 2006 Jul 7;360(2):329-42. Epub 2006 May 15. Pubmed
  2. Iwamoto S, Mihara K, Downing JR, Pui CH, Campana D: Mesenchymal cells regulate the response of acute lymphoblastic leukemia cells to asparaginase. J Clin Invest. 2007 Apr;117(4):1049-57. Epub 2007 Mar 22. Pubmed
Transporters

1. Monocarboxylate transporter 10

Actions: inhibitor

Sodium-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 Link_out
Gene: SLC16A10 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Kim DK, Kanai Y, Chairoungdua A, Matsuo H, Cha SH, Endou H: Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters. J Biol Chem. 2001 May 18;276(20):17221-8. Epub 2001 Feb 20. Pubmed
Comments
Drug created on June 13, 2005 07:24 / Updated on February 08, 2013 16:19