- Asparagine
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For other articles using the abbreviation or acronym asn, see ASN (disambiguation).
L-Asparagine 
AsparagineOther names2-Amino-3-carbamoylpropanoic acidIdentifiers CAS number 70-47-3 
PubChem 236 ChemSpider 6031 UNII 7NG0A2TUHQ EC-number 200-735-9 DrugBank DB03943 KEGG C00152 ChEBI CHEBI:17196 ChEMBL CHEMBL58832 Jmol-3D images Image 1
Image 2- O=C(N)C[C@H](N)C(=O)O
C([C@@H](C(=O)O)N)C(=O)N
- InChI=1S/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1
Key: DCXYFEDJOCDNAF-REOHCLBHSA-N
InChI=1/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1
Key: DCXYFEDJOCDNAF-REOHCLBHBD
Properties Molecular formula C4H8N2O3 Molar mass 132.12 g mol−1 Acidity (pKa) 2.02 (carboxyl), 8.8 (amino)[1] Supplementary data page Structure and
propertiesn, εr, etc. Thermodynamic
dataPhase behaviour
Solid, liquid, gasSpectral data UV, IR, NMR, MS 
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Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)Infobox references Asparagine (abbreviated as Asn or N; Asx or B represent either asparagine or aspartic acid) is one of the 20 most common natural amino acids on Earth. It has carboxamide as the side-chain's functional group. It is not an essential amino acid. Its codons are AAU and AAC.[2]
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 roasted coffee.
Contents
History
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,[3][4] in which it is abundant — hence, the name they chose for that new matter — becoming the first amino acid to be isolated. The characteristic smell observed in the urine of individuals after their consumption of asparagus is attributed to various metabolic byproducts of asparagine.[5]
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.[6]
Structural function in proteins
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 backbone. 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.
Sources
Dietary sources
Asparagine is not an essential amino acid, which means that it can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet. Asparagine is found in:
- Animal sources: dairy, whey, beef, poultry, eggs, fish, lactalbumin, seafood
- Plant sources: asparagus, potatoes, legumes, nuts, seeds, soy, whole grains
Biosynthesis
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.
The biosynthesis of asparagine from oxaloacetateDegradation
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.
Function
The nervous system requires asparagine. It also plays an important role in the synthesis of ammonia.
Betaine structure
(S)-Asparagine (left) and (R)-asparagine (right) in zwitterionic form at neutral pH
References
- ^ Dawson, R.M.C., et al., Data for Biochemical Research, Oxford, Clarendon Press, 1959.
- ^ "Nomenclature and symbolism for amino acids and peptides (IUPAC-IUB Recommendations 1983)", Pure Appl. Chem. 56 (5): 595–624, 1984, doi:10.1351/pac198456050595.
- ^ Vauquelin LN, Robiquet PJ (1806). "La découverte d'un nouveau principe végétal dans le suc des asperges". Annales de Chimie 57: 88–93.
- ^ R.H.A. Plimmer (1912) [1908]. R.H.A. Plimmer & F.G. Hopkins. ed. The chemical composition of the proteins. Monographs on biochemistry. Part I. Analysis (2nd ed.). London: Longmans, Green and Co.. p. 112. http://books.google.com/?id=7JM8AAAAIAAJ&pg=PA112. Retrieved January 18, 2010.
- ^ S.C. Mitchell (2001). "Food Idiosyncrasies: Beetroot and Asparagus". Drug Metabolism and Disposition 29 (4 Pt 2): 539–534. PMID 11259347. http://dmd.aspetjournals.org/content/29/4/539.full. Retrieved january 18, 2010.
- ^ http://www.henriettesherbal.com/eclectic/kings/glycyrrhiza.html
External links
The 20 common amino acids By properties AliphaticBranched-chain amino acids (Valine · Isoleucine · Leucine) · Methionine · Alanine · Proline · GlycineAromaticPolar, unchargedPositive charge (pKa)Negative charge (pKa)GeneralOther classifications biochemical families: prot · nucl · carb (glpr, alco, glys) · lipd (fata/i, phld, strd, gllp, eico) · amac/i · ncbs/i · ttpy/iCategories:- Proteinogenic amino acids
- Glucogenic amino acids
- O=C(N)C[C@H](N)C(=O)O
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