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Overview and history Synthesis and Metabolism References
L-Asparagine structure
Chemical Name:
ASN;L-Asn;Agedoite;H-ASN-OH;Altheine;L-Asn-OH;-Asparag;ASPARAGINE;Asparamide;Crystal VI
Molecular Formula:
Formula Weight:
MOL File:

L-Asparagine Properties

Melting point:
235 °C (dec.) (lit.)
34.5 º (c=10, 2N HCl)
Boiling point:
244.01°C (rough estimate)
refractive index 
1.4880 (estimate)
storage temp. 
Keep in dark place,Inert atmosphere,Room temperature
H2O: 0.1 M at 20 °C, clear, colorless
2.17(at 20℃)
sltly sweet taste
Water Solubility 
20 g/L (20 ºC)
Stable, but may be moisture-sensitive. Incompatible with strong oxidizing agents.
CAS DataBase Reference
70-47-3(CAS DataBase Reference)
Substances Added to Food (formerly EAFUS)
NIST Chemistry Reference
EPA Substance Registry System
L-Asparagine (70-47-3)
  • Risk and Safety Statements
Hazard Codes  Xn
Risk Statements  20/21/22-36/37/38
Safety Statements  24/25-36-26
RIDADR  UN 2811 6.1 / PGIII
WGK Germany  3
HazardClass  IRRITANT
HS Code  29241900

L-Asparagine price More Price(15)

Manufacturer Product number Product description CAS number Packaging Price Updated Buy
Sigma-Aldrich 51363 L-Asparagine certified reference material, TraceCERT 70-47-3 100mg $104 2021-03-22 Buy
Sigma-Aldrich 1043502 Asparagine anhydrous United States Pharmacopeia (USP) Reference Standard 70-47-3 200mg $399 2020-08-18 Buy
Alfa Aesar B21473 L-(+)-Asparagine, 99% 70-47-3 500g $177 2021-03-22 Buy
Alfa Aesar B21473 L-(+)-Asparagine, 99% 70-47-3 100g $61.8 2021-03-22 Buy
Sigma-Aldrich A0884 L-Asparagine ≥98% (HPLC) 70-47-3 100g $96.9 2021-03-22 Buy

L-Asparagine Chemical Properties,Uses,Production

Overview and history

Asparagine [symbol Asn or N][1] is a key α-amino acid that is used in the biosynthesis of proteins. It contains a α-amino group and a α-carboxylic acid group as well as a side chain carboxamide. It is classified as a polar [at physiological pH], aliphatic amino acid. It is non-essential in humans, and can undergo de novo synthesis inside the human body. From the aspect of genetic code during protein synthesis, it is encoded by the codons AAU and AAC[2].
The discovery of L-Asn dates back over 200 years with its identification from natural sources by Delaville[3] and first isolation by French chemists Vauquelin and Robiquet[4] from spears of Asparagus sativus. Not only was Asn the first amino acid identified, it was one of the first examples of the preparation of a Damino acid by Piutti[5]. Piutti was also credited with the determination of the chemical structure of Asn, and the first observation of enantioselectivity of a biological receptor, for his discovery of a difference in taste between Dand L-Asn. It was rapidly discovered that Asn is present in all higher plants, and Schulze and Winterstein[6] were the first to show that, although present in small quantities in green plants, it accumulates under carbohydrate deficiency or starvation in general. Asn was also reported to be formed as a temporary N reserve during aberrations in normal protein metabolism, when excess ammonium is formed[7]. Furthermore, the role of Asn as a translocated nitrogenous substance in a form suitable for subsequent re-synthesis from one organ of a plant to another was demonstrated by Chibnall[8]. Murneek[9] summarized the findings of several researchers at the time and reported that under carbohydrate depleted conditions excess protein unused by the plant is hydrolyzed by means of proteolytic enzymes and hence amino acids are formed including Asn.

Figure 1 The chemical structure of the L-asparagine ;

Synthesis and Metabolism

A major route for Asn biosynthesis is via the ATP-dependent transfer of the amide group of glutamine to the β-carboxyl group of aspartate by the action of asparagine synthetase[AS]. So far, two types of ASs, AsnA and AsnB, have been identified. While prokaryotes utilize AsnA type ASs that require ammonia as an amide donor as well as AsnB type ASs that can catalyze the reaction using either ammonium or glutamine as an amide donor, most eukaryotes only use AsnB type ASs[10, 11]. AS is notably difficult to assay from plant tissues[12]. AsnB-type ASs are members of the N-terminal nucleophile hydrolase[Ntn] group of glutamine amidotransferases[13, 14]. They are characterized by an N-terminal cysteine nucleophilic residue producing a cysteinyl-glutamine tetrahedral intermediate from which ammonium is abstracted. Glutamate is released by hydrolysis of the resulting γ-glutamyl thioester intermediate. The ammonia is tunneled to a C-terminal transferase domain. This domain activates aspartate through ATP hydrolysis as a β-aspartyl AMP intermediate. Nucleophilic attack by the ammonia results in cleavage and release of Asn. There are two groups of AS enzymes in higher plants designated as class I and II. Results of kinetic analyses of recombinant maize AS enzymes indicated that class I enzymes may have specialized functions as they can have higher affinity for glutamine and their expression is restricted to specific tissues[15]. The detailed schematic pathways of asparagine metabolic pathways are shown in Figure 2[16].

Figure 2 Asparagine metabolic pathways Ammonium is assimilated into the glutamine-amide group for glutamine synthesis by the reaction of glutamine synthetase[GS]. Glutamate synthase[GOGAT] transfers the amide group of glutamine to the 2-position of 2-oxoglutarate, generating glutamate. Asparagine synthetase[AS] converts either the glutamine-amide group or ammonium into aspartate, yielding asparagine. Transamination of glutamate with oxaloacetate by aspartate aminotransferase[AspAT] generates aspartate, which serves as a substrate of asparagine synthesis. The asparagine amide group can be degraded by asparaginase[ASPG], yielding ammonium and aspartate. The asparagine amino group is hydrolyzed by asparagine aminotransferase[AsnAT], producing ammonium and 2-oxosucinamate. AsnAT catalyzes the transamination reaction of asparagine with glyoxylate, pyruvate, 4-hydroxypyruvate and 4-hydroxy 2-oxobutyrate as amino acceptors, producing glycine, alanine, serine and homoserine, respectively. 2-Oxosuccinamate is then converted to ammonium and oxaloacetate by ω-amidase.

Asparagine synthetase
Asparagine synthetase[l-aspartate: ammonia ligase[AMP-forming], EC] catalyzes the reversible conversion of l-aspartate, NH4+, and ATP to l-asparagine, AMP, and PPi. The enzyme is distributed widely in nature, but its enzymological properties have not been studied in detail. Pioneering studies have been made on the enzymes from lactic acid bacteria. The enzyme from Lactobacillus arabinosus can be stored at 4 ℃ for 3 weeks but not at–20℃[17]. The optimum pH is 8.2, and the optimum temperature is about 40℃. The enzyme is specific for l-aspartate and does not act on l-glutamate. β-l-Aspartyl hydroxamate is synthesized when hydroxamate is added to the reaction mixture instead of NH4+. The enzyme requires Mg2+ and is activated by Mn2+. No activation of Mg2+ was observed for the E. coli[18] and Streptococcus bovis enzymes.
Asparaginase[l-asparagine amidohydrolase, EC] catalyzes the hydrolysis of the amido bond of l-asparagine and irreversibly produces l-aspartate and ammonia. The enzyme is widely distributed in microorganisms, animals, and plants. The bacterial enzymes from Acinetobacter calcoaceticus[19], Bacillus coagulans[20], E. coli[21], and Vibrio succinogenes[22] also show enzymatic activity on d-asparagine. The enzyme from E. coli has been used for the industrial production of l-asparagine. Saccharomyces cerevisiae produces the enzyme both intracellularly and extracellularly[23]. The synthesis of the enzyme is stimulated by nitrogen starvation, requires an available energy source, and is prevented by cycloheximide. The intracellular enzyme appears to be constitutive. The extracellular activity is relatively insensitive to p-hydroxymercuribenzoate inhibition, whereas the intracellular activity is highly inhibited by this compound.


  2. Shu, Jian-Jun[2017]. "A new integrated symmetrical table for genetic codes". BioSystems. 151: 21–26.
  3. Delaville M[1802] Sur les se`ves d’asperges et de choux. Ann Chim 41:298
  4. Vuquelin LN, Robiquet PJ[1806] La de´couverte d’un nouveau principe ve´ge´tal dans le suc des asperges. Ann Chim 57:88–93
  5. Piutti A[1886] Ein neues Asparagin. Ber Dtsch Chem Ges 19:1691–1695
  6. Schulze E, Winterstein E[1910] Handbuch der biochemischen Arbeitsmethoden, vol 2. Berlin Urban & Schwarzenberg, Berlin, p 510
  7. Prianischnikov D[1922] Das ammoniak als anfangsund endprodukt des stickstoffumsatzes in den pflanzen. Landwirtsch Vers-Stat 99:267–286
  8. Chibnall AC[1924] Investigations on the nitrogenous metabolism of the higher plants. VI. The role of asparagine in the metabolism of the mature plant. Biochem J 18:395–404
  9. Murneek AE[1935] Physiological roˆle of asparagine and related substances in nitrogen metabolism of plants. Plant Physiol 10:447–464
  10. Gaufichon L, Reisdorf-Cren M, Rothstein SJ, Chardon F, Suzuki A[2010] Biological functions of asparagine synthetase in plants. Plant Sci 179:141–153. doi:10.1016/j.plantsci.2010.04.010
  11. Duff SMG[2015] Asparagine synthetase. In: D’Mello JPF[ed] Amino acids in higher plants. CAB International, Wallingford, pp 100–128
  12. Romagni JG, Dayan FE[2000] Measuring asparagine synthetase activity in crude plant extracts. J Agric Food Chem 48:1692–1696
  13. Larsen TM, Boehlein SK, Schuster SM, Richards NGJ, Thoden JB, Holden HM, Rayment I[1999] Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product. Biochemistry 38:16146–16157. doi:10.1021/bi9915768
  14. Massie`re F, Badet-Denisot MA[1998] The mechanism of glutamine-dependent amidotransferases. Cell Mol Life Sci 54:205–222
  15. Duff SMG, Qi Q, Reich T, Wu X, Brown T, Crowley JH, Fabbri B[2011] A kinetic comparison of asparagine synthetase isozymes from higher plants. Plant Physiol Biochem 49:251–256. doi:10.1016/j.plaphy.2010.12.006
  16. Gaufichon, Laure, S. J. Rothstein, and A. Suzuki. "Asparagine Metabolic Pathways in Arabidopsis." Plant & Cell Physiology 57.4[2017]:675.
  17. Meister A[1974] Asparagine synthesis. In: Boyer PD[ed] The Enzymes, 3rd edn, vol 10. Academic, New York, pp 561–580
  18. Sugiyama A, Kato H, Nishioka T, Oda J[1992] Overexpression and purification of asparagines synthetase from Escherichia coli. Biosci Biotechnol Biochem 56:376–379
  19. Joner PE, Kristiansen T, Einasson M[1973] Purification and properties of l-asparaginase A fromAcinetobacter calcoaceticus. Biochim Biophys Acta 327:146–456
  20. Law AS, Wriston JC[1971] Purification and properties of Bacillus coagulans l-asparaginase. Arch Biochem Biophys 147:744–752
  21. Peterson RG, Richards FF, Handschumacher RE[1977] Structure of peptide from active site region of Escherichia  coli l-asparaginase. J Biol Chem 252:2072–2076
  22. Distasio JA, Niederman RA, Kafkewitz D, Goodman D[1976] Purification and characterization of l-asparaginase with antilymphoma activity from Vibrio succinogenes. J Biol Chem 251:6929–6933
  23. Dunlop PC, Meyer GM, Ban D, Roon RJ[1978] Characterization of two forms of asparaginasein Saccharomyces cerevisiae. J Biol Chem 253:1297–1304


Asparagine (abbreviated as Asn or N) is one of the 20 most common natural amino acids on Earth. It has carboxamide as the sidechain's functional group. It is not an essential amino acid. Its codons are AAU and AAC.
A reaction between asparagine and reducing sugars or reactive carbonyls produces acrylamide ( acrylic amide ) in food when heated to sufficient temperature. These products occur in baked goods such as French fries, potato chips, and toasted bread.

Chemical Properties

White crystalline powder or rhombic hemihedral crystals; sltly sweet taste. Sol in water; insol in alc, ether.


Dietary sources
Asparagine is not essential for humans, which means that it can be synthesized from central metabolic pathway intermediates and is not required in the diet. Asparagine is found in :
Animal sources : dairy, whey, beef, poultry, eggs, fish, lactalbumin , sea food
Plant sources : asparagus, potatoes, legumes, nuts, seeds, soy, whole grains.
The precursor to asparagine is oxaloacetate. Oxaloacetate is converted to aspartate using a transaminase enzyme. The enzyme transfers the amino group from glutamate to oxaloacetate producing α- ketoglutarate and aspartate. The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. In the asparagine synthetase reaction, ATP is used to activate aspartate, forming β-aspartyl-AMP. Glutamine donates an ammonium group, which reacts with β-aspartyl-AMP to form asparagine and free AMP.


Asparagine was first isolated in 1806, under a crystalline form, by French chemists Louis Nicolas Vauquelin and Pierre Jean Robiquet (then a young assistant) from asparagus juice, in which it is abundant — hence, the name they chose for that new matter — becoming the first amino acid to be isolated.
A few years later, in 1809, Pierre Jean Robiquet again identified, this time from liquorice root, a substance with properties he qualified as very similar to those of asparagine, that Plisson in 1828 identified as asparagine itself.


Biochemical research, preparation of culture media, medicine.


ChEBI: An optically active form of asparagine having L-configuration.

Biological Functions

Since the asparagine side-chain can form hydrogen bond interactions with the peptide backbone, asparagine residues are often found near the beginning and the end of alpha-helices, and in turn motifs in beta sheets. Its role can be thought as "capping" the hydrogen bond interactions that would otherwise be satisfied by the polypeptide back bone. Glutamines, with an extra methylene group, have more conformational entropy and thus are less useful in this regard.
Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains.

Biological Functions

The nervous system requires asparagine. It also plays an important role in the synthesis of ammonia.
The addition of N-acetyl glucosamine to asparagine is performed by oligosaccharyltransferase enzymes in the endoplasmic reticulum. This glycosylation is important both for protein structure and protein function.

Safety Profile

When heated to decomposition emits toxic fumes of Nox

Purification Methods

Likely impurities are aspartic acid and tyrosine. Crystallise it from H2O or aqueous EtOH. It slowly effloresces in dry air. [Greenstein & Winitz The Chemistry of the Amino Acids J. Wiley, Vol 3 p 1856 1961, Beilstein 4 IV 3005.]


Aspartate is a glucogenic amino acid. L-asparaginase hydrolyzes the amide group to form aspartate and ammonium. A transaminase converts the aspartate to oxaloacetate, which can then be metabolized in the citric acid cycle or gluconeogenesis.

L-Asparagine Preparation Products And Raw materials

Raw materials

Preparation Products

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View Lastest Price from L-Asparagine manufacturers

Image Release date Product Price Min. Order Purity Supply Ability Manufacturer
2021-11-15 L-Asparagine
US $15.00 / KG 1000KG 99.9% 100tons Hebei Yirun Sega Biological Technology Co. Ltd
2021-09-29 L-Asparagine
US $0.00 / Kg/Drum 1KG 98%min 500kgs WUHAN FORTUNA CHEMICAL CO., LTD
2021-08-12 L-asparagine
US $100.00 / Kg 1KG 99% 20tons Shanghai Dumi Biotechnology Co.,ltd

L-Asparagine Spectrum

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