l}}-Asparagine| ImageFile = L-Asparagin - L-Asparagine.svg| ImageSize = 200px| ImageAlt = Skeletal formula of L-asparagine| ImageCaption = Skeletal formula of L-asparagine| ImageFile1 = L-Asparagin phys.svg| ImageSize1 = 220| ImageAlt1 = Ball-and-stick model of the L-asparagine molecule as a zwitterion| ImageFileL2 = Asparagine-from-xtal-3D-bs-17.png| ImageSizeL2 = 100| ImageCaptionL2 = Ball-and-stick model| ImageFileR2 = Asparagine-from-xtal-3D-sf.png| ImageSizeR2 = 110| ImageCaptionR2 = Space-filling model| IUPACName = Asparagine| OtherNames = 2-Amino-3-carbamoylpropanoic acid|Section1={{Chembox Identifiers| IUPHAR_ligand = 4533

correct|chemspider}}| ChemSpiderID = 6031

correct|FDA}}| UNII = 5Z33R5TKO7

correct|EBI}}| ChEMBL = 58832

correct|kegg}}| KEGG = C00152| InChI = 1/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1| InChIKey = DCXYFEDJOCDNAF-REOHCLBHBD

correct|chemspider}}| StdInChI = 1S/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1

correct|chemspider}}| StdInChIKey = DCXYFEDJOCDNAF-REOHCLBHSA-N| CASNo = 70-47-3

correct|CAS}}| EC_number = 200-735-9| PubChem = 236

correct|EBI}}| ChEBI = 17196

correct|drugbank}}| DrugBank = DB03943| SMILES = O=C(N)C[C@H](N)C(=O)O| SMILES1 = O=C(N)C[C@H]([NH3+])C(=O)[O-]| SMILES1_Comment = Zwitterion}}|Section2={{Chembox Properties

H=8

acids, Base (chemistry)>bases, negligible in methanol, ethanol, ether, benzene | pKa = {{Unbulleted list

| 2.1 (carboxyl; 20 Â°C, H2O)
| 8.80 (amino; 20 Â°C, H2O)BOOK, Haynes WM, 2016, CRC Handbook of Chemistry and Physics, 97th, CRC Press, 978-1498754286, 5â€“89, CRC Handbook of Chemistry and Physics,

}}| LogP = âˆ’3.82| MagSus = -69.5Â·10âˆ’6 cm3/mol

}}|Section3={{Chembox Structure| CrystalStruct = orthorhombic
}}|Section4={{Chembox Thermochemistry| DeltaHf = âˆ’789.4 kJ/mol
}}|Section7={{Chembox Hazards| ExternalSDS = Sigma-Alrich

NFPA-F = 0 | NFPA-R = 0| FlashPtC = 219| AutoignitionPtC =

}}

}}Asparagine (symbol Asn or NWEB,weblink Nomenclature and Symbolism for Amino Acids and Peptides, IUPAC-IUB Joint Commission on Biochemical Nomenclature, 1983, 5 March 2018,weblink" title="web.archive.org/web/20081009023202weblink">weblink 9 October 2008, dead, ) is an Î±-amino acid that is used in the biosynthesis of proteins. It contains an Î±-amino group (which is in the protonated âˆ’NH{{su|b=3|p=+}} form under biological conditions), an Î±-carboxylic acid group (which is in the deprotonated âˆ’COOâˆ’ form under biological conditions), and a side chain carboxamide, classifying it as a polar (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it. It is encoded by the codons AAU and AAC.The one-letter symbol N for asparagine was assigned arbitrarily,JOURNAL, 10 July 1968, IUPAC-IUB Commission on Biochemical Nomenclature A One-Letter Notation for Amino Acid Sequences,weblink Journal of Biological Chemistry, en, 243, 13, 3557â€“3559, 10.1016/S0021-9258(19)34176-6, free, with the proposed mnemonic asparagiNe;JOURNAL, Adoga, Godwin I, Nicholson, Bh, January 1988, Letters to the editor,weblink Biochemical Education, en, 16, 1, 49, 10.1016/0307-4412(88)90026-X,

History

Asparagine was first isolated in 1806 in a crystalline form by French chemists Louis Nicolas Vauquelin and Pierre Jean Robiquet (then a young assistant). It was isolated from asparagus juice,JOURNAL, La dÃ©couverte d'un nouveau principe vÃ©gÃ©tal dans le suc des asperges, Vauquelin LN, Robiquet PJ, Annales de Chimie, 1806, 57, 88â€“93, fr, 2027/nyp.33433062722578, BOOK, Plimmer RH, Plimmer RH, Hopkins FG, The chemical composition of the proteins,weblink January 18, 2010, 2nd, Monographs on biochemistry, Part I. Analysis, 1908, 1912, Longmans, Green and Co., London, 112, in which it is abundant, hence the chosen name. It was the first amino acid to be isolated.BOOK, Advances in Protein Chemistry, Anfinsen CB, Edsall JT, Richards FM, 1972, 99, 103, Academic Press, New York, 978-0-12-034226-6,weblink Three years later, in 1809, Pierre Jean Robiquet identified a substance from liquorice root with properties which he qualified as very similar to those of asparagine,JOURNAL, Robiquet PJ, Analyse de la racine de rÃ©glisse, Annales de Chimie et de Physique, 1809, 72, 1, 143â€“159,weblink Analysis of licorice root, fr, and which Plisson identified in 1828 as asparagine itself.JOURNAL, Plisson A, De l'indentitÃ© de l'asparagine avec l'agÃ©doÃ¯te, Journal de Pharmacie et des Sciences Accessoires, 1828, 14, 4, 177â€“182,weblink On the identity of asparagine with agÃ©doÃ¯te, fr, BOOK,weblink Glycyrrhiza (U. S. P.)â€”Glycyrrhiza, King's American Dispensatory, 1898, Harvey Wickes, Felter, John Uri, Lloyd, vanc, Henriette's Herbal Homepage, The determination of asparagine's structure required decades of research. The empirical formula for asparagine was first determined in 1833 by the French chemists Antoine FranÃ§ois Boutron Charlard and ThÃ©ophile-Jules Pelouze; in the same year, the German chemist Justus Liebig provided a more accurate formula.JOURNAL, Boutron-Charlard, Pelouze, Ueber das Asparamid (Asparagin des Herrn Robiquet) und die AsparamidsÃ¤ure, Annalen der Chemie, 1833, 6, 75â€“88,weblink On asparamide (the asparagine of Mr. Robiquet) and aspartic acid, de, 10.1002/jlac.18330060111, The empirical formula of asparagine appears on p. 80.JOURNAL, Liebig, Justus, vanc, Ueber die Zusammensetzung des Asparamids und der AsparaginsÃ¤ure, Annalen der Chemie, 1833, 7, 14, 146â€“150,weblink On the composition of asparamide [asparagine] and aspartic acid, de, 1834AnP...107..220L, 10.1002/andp.18341071405, The empirical formula appears on p. 149 ; the formula is correct if the subscripts are divided by 2. In 1846 the Italian chemist Raffaele Piria treated asparagine with nitrous acid, which removed the molecule's amine (â€“NH2) groups and transformed asparagine into malic acid.See:

JOURNAL, Piria, Raffaele, 177614807, vanc, Studi sulla costituzione chimica dell' asparagina e dell' acido aspartico, Il Cimento, January 1846, 4, 55â€“73,weblink Studies of the chemical constitution of asparagine and aspartic acid, it, 10.1007/BF02532918,
French translation: JOURNAL, Piria, Raffaele, vanc, Recherches sur la constitution chimique de l'asparagine et de l'acide aspartique, Annales de Chimie et de Physique, 1848, 22, 160â€“179,weblink 3rd series, Investigations into the chemical constitution of asparagine and of aspartic acid, fr, From p. 175: " â€¦ on voit, en outre, que l'asparagine et l'acide aspartique lui-mÃªme se dÃ©composent avec une facilitÃ© remarquable, sous l'influence de l'acide hyponitrique, en fournissant du gaz azote et de l'acide malique." ( â€¦ one sees, in addition, that asparagine and aspartic acid itself are decomposed with a remarkable ease under the influence of nitrous acid, rendering nitrogen gas and malic acid.) This revealed the molecule's fundamental structure: a chain of four carbon atoms. Piria thought that asparagine was a diamide of malic acid;BOOK, Plimmer, Robert Henry Aders, vanc, The Chemical Constitution of the Proteins. Part I: Analysis, 1912, Longmans, Green and Co., London, England, 112, 2nd,weblink however, in 1862 the German chemist Hermann Kolbe showed that this surmise was wrong; instead, Kolbe concluded that asparagine was an amide of an amine of succinic acid.JOURNAL, Kolbe, Hermann, vanc, Ueber die chemische Constitution des Asparagins und der AsparaginsÃ¤ure, Annalen der Chemie, 1862, 121, 2, 232â€“236,weblink On the chemical constitution of asparagine and aspartic acid, de, 10.1002/jlac.18621210209, In 1886, the Italian chemist Arnaldo Piutti (1857â€“1928) discovered a mirror image or "enantiomer" of the natural form of asparagine, which shared many of asparagine's properties, but which also differed from it.JOURNAL, Piutti A, Ein neues Asparagin, Berichte der Deutschen Chemischen Gesellschaft, 1886, 19, 2, 1691â€“1695,weblink A new asparagine, de, 10.1002/cber.18860190211, Since the structure of asparagine was still not fully known â€“ the location of the amine group within the molecule was still not settledThe French chemist Edouard Grimaux thought that the amine group (â€“NH2) was located next to the amide group (â€“C(O)NH2), whereas the Italian chemist Icilio Guareschi thought that the amine group was located next to the carboxyl group (â€“COOH).
JOURNAL, Grimaux, Edouard, vanc, Recherches synthÃ©tiques sur le groupe urique, Bulletin de la SociÃ©tÃ© Chimique de Paris, 1875, 24, 337â€“355,weblink 2nd series, Synthetic investigations of the uric group, fr, On p. 352, Grimaux presented two putative structures for asparagine, and on p. 353, he favored structure (I.), which is incorrect. From p. 353: " â€¦ ce sont les formules marquÃ©es du chiffre I qui me semblent devoir Ãªtre adoptÃ©es pour l'asparagine, â€¦ " ( â€¦ it is the formulas marked by the figure I which, it seems to me, should be adopted for asparagine, â€¦ )
JOURNAL, Guareschi, Icilio, vanc, Studi sull' asparagine e sull' acido aspartico, Atti della Reale Academia del Lincei, 1876, 3 (pt. 2), 378â€“393,weblink 2nd series, Studies of asparagine and of aspartic acid, it, On p. 388, Guareschi proposed two structures (Î± and Î²) for asparagine; he favored Î±, the correct one. From p. 388: "La formola Î± mi sembra preferibile per seguente ragione: â€¦ " (The formula Î± seems preferable to me for the following reason: â€¦ )
English abstract in: JOURNAL, Guareschi J, Asparagine and aspartic acid, Journal of the Chemical Society, 1877, 31, 457â€“459,weblink See especially p. 458. â€“ Piutti synthesized asparagine and thus published its true structure in 1888.JOURNAL, Piutti A, Sintesi e costituzione delle asparagine, Gazzetta Chimica Italiana, 1888, 18, 457â€“472,weblink Synthesis and constitution of asparagine, it,

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 of alpha-helices as asx turns and asx motifs, and in similar turn motifs, or as amide rings, in beta sheets. Its role can be thought as "capping" the hydrogen bond interactions that would otherwise be satisfied by the polypeptide backbone.Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains. Typically, a carbohydrate tree can solely be added to an asparagine residue if the latter is flanked on the C side by X-serine or X-threonine, where X is any amino acid with the exception of proline.BOOK, Brooker, Robert, Widmaier, Eric, Graham, Linda, Stiling, Peter, Hasenkampf, Clare, Hunter, Fiona, Bidochka, Michael, Riggs, Daniel, vanc, Biology, 2010, McGraw-Hill Ryerson, United States of America, 978-0-07-074175-1, 105â€“106, Canadian, Chapter 5: Systems Biology of Cell Organization, Asparagine can be hydroxylated in the HIF1 hypoxia-inducible transcription factor. This modification inhibits HIF1-mediated gene activation.JOURNAL, Lando D, Peet DJ, Gorman JJ, Whelan DA, Whitelaw ML, Bruick RK, FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor, Genes & Development, 16, 12, 1466â€“71, June 2002, 12080085, 186346, 10.1101/gad.991402,

Sources

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, seafood{{cn|date=April 2024}}
Plant sources: seaweed (spirulina), potatoes, soy protein isolate, tofu{{cn|date=April 2024}}

Biosynthesis and catabolism

The precursor to asparagine is oxaloacetate, which a transaminase enzyme converts to aspartate. The enzyme transfers the amino group from glutamate to oxaloacetate producing Î±-ketoglutarate and aspartate. The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. Asparagine synthetase uses ATP to activate aspartate, forming Î²-aspartyl-AMP. Glutamine donates an ammonium group, which reacts with Î²-aspartyl-AMP to form asparagine and free AMP.frame|center|The biosynthesis of asparagine from oxaloacetateIn reaction that is the reverse of its biosynthesis, asparagine is hydrolyzed to aspartate by asparaginase. Aspartate then undergoes transamination to form glutamate and oxaloacetate from alpha-ketoglutarate. Oxaloacetate, which enters the citric acid cycle (Krebs cycle).BOOK, Berg, Jeremy, Tymoczko, John, Stryer, Lubert, Biochemistry, 2002, W. H. Freeman, New York, 0716746840, 968, 5th,weblink 27 May 2021,

Acrylamide controversy

Heating a mixture of asparagine and reducing sugars or other source of carbonyls produces acrylamide in food. These products occur in baked goods such as French fries, potato chips, and toasted bread. Acrylamide is converted in the liver to glycidamide, which is a possible carcinogen.JOURNAL, 10.1021/jf030204+, 2003, 51, 16, Friedman, Mendel, Chemistry, Biochemistry, and Safety of Acrylamide. A Review, Journal of Agricultural and Food Chemistry, 4504â€“4526, 14705871,

Function

Asparagine synthetase is required for normal development of the brain.JOURNAL, Ruzzo EK, Capo-Chichi JM, Ben-Zeev B, Chitayat D, Mao H, Pappas AL, Hitomi Y, Lu YF, Yao X, Hamdan FF, Pelak K, Reznik-Wolf H, Bar-Joseph I, Oz-Levi D, Lev D, Lerman-Sagie T, Leshinsky-Silver E, Anikster Y, Ben-Asher E, Olender T, Colleaux L, DÃ©carie JC, Blaser S, Banwell B, Joshi RB, He XP, Patry L, Silver RJ, Dobrzeniecka S, Islam MS, Hasnat A, Samuels ME, Aryal DK, Rodriguiz RM, Jiang YH, Wetsel WC, McNamara JO, Rouleau GA, Silver DL, Lancet D, Pras E, Mitchell GA, Michaud JL, Goldstein DB, 6, Deficiency of asparagine synthetase causes congenital microcephaly and a progressive form of encephalopathy, Neuron, 80, 2, 429â€“41, October 2013, 24139043, 3820368, 10.1016/j.neuron.2013.08.013, Asparagine is also involved in protein synthesis during replication of poxviruses.JOURNAL, Pant A, Cao S, Yang Z, Asparagine Is a Critical Limiting Metabolite for Vaccinia Virus Protein Synthesis during Glutamine Deprivation, Journal of Virology, 93, 13, e01834â€“18, /jvi/93/13/JVI.01834â€“18.atom, July 2019, 30996100, 6580962, 10.1128/JVI.01834-18, Shisler JL, The addition of N-acetylglucosamine to asparagine is performed by oligosaccharyltransferase enzymes in the endoplasmic reticulum.JOURNAL, Burda P, Aebi M, The dolichol pathway of N-linked glycosylation, Biochimica et Biophysica Acta (BBA) - General Subjects, 1426, 2, 239â€“57, January 1999, 9878760, 10.1016/S0304-4165(98)00127-5, This glycosylation is involved in protein structureJOURNAL, Imperiali B, O'Connor SE, Effect of N-linked glycosylation on glycopeptide and glycoprotein structure, Current Opinion in Chemical Biology, 3, 6, 643â€“9, December 1999, 10600722, 10.1016/S1367-5931(99)00021-6, and function.JOURNAL, Patterson MC, Metabolic mimics: the disorders of N-linked glycosylation, Seminars in Pediatric Neurology, 12, 3, 144â€“51, September 2005, 16584073, 10.1016/j.spen.2005.10.002,

References

External links

GMD MS Spectrum

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