Asparagine

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Asparagine may be abbreviated as "Asn". For other uses of this abbreviation, see ASN
(disambiguation).
Not to be confused with Aspartic acid.

l-Asparagine

Skeletal formula of L-asparagine

Ball-and-stick model Space-filling model

Names

IUPAC name

Asparagine

Other names

2-Amino-3-carbamoylpropanoic acid
 Identifiers

CAS Number  70-47-3 

3D model (JSmol)  Interactive image

 Zwitterion: Interactive image

ChEBI  CHEBI:17196 

ChEMBL  ChEMBL58832 

ChemSpider  6031 

DrugBank  DB03943 

ECHA InfoCard 100.019.565 

EC Number  200-735-9

IUPHAR/BPS  4533

KEGG  C00152 

PubChem CID  236

UNII  5Z33R5TKO7 

CompTox  DTXSID30859927 
Dashboard (EPA)

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InChI

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SMILES

Properties

Chemical formula C4H8N2O3

Molar mass 132.119 g·mol−1

Appearance white crystals

Density 1.543 g/cm3

Melting point 234 °C (453 °F; 507 K)

Boiling point 438 °C (820 °F; 711 K)

Solubility in water 2.94 g/100 mL

Solubility soluble in acids, bases, negligible

in methanol, ethanol, ether, benzene
 log P −3.82

Acidity (pKa)  2.1 (carboxyl; 20 °C, H2O)

 8.80 (amino; 20 °C, H2O)[1]

Magnetic -69.5·10−6 cm3/mol
susceptibility (χ)

Structure

Crystal structure orthorhombic

Thermochemistry

Std enthalpy of −789.4 kJ/mol

formation(ΔfH⦵298)

Hazards

NFPA 704(fire diamond)

1
0
0
Flash point 219 °C (426 °F; 492 K)

Safety data sheet(SDS) Sigma-Alrich

Supplementary data page

Asparagine (data page)

Except where otherwise noted, data are given for materials in

their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

Asparagine (symbol Asn or N[2]) is an α-amino acid that is used in the biosynthesis of

proteins. It contains an α-amino group (which is in the protonated −NH+
3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated

−COO−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.

Contents

 1History
 2Structural function in proteins
 3Sources
 o 3.1Dietary sources
o 3.2Biosynthesis and catabolism
o 3.3Acrylamide controversy
 4Function
 5References
 6External links

History[edit]
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,[3][4] in which it is abundant, hence the chosen name. It was the first
amino acid to be isolated.[5]
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,[6] and
which Plisson identified in 1828 as asparagine itself.[7][8]
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 François
Boutron Charlard and Théophile-Jules Pelouze; in the same year, the German chemist Justus
Liebig provided a more accurate formula.[9][10] In 1846 the Italian chemist Raffaele Piria treated
asparagine with nitrous acid, which removed the molecule's amine (–NH2) groups and
transformed asparagine into malic acid.[11] This revealed the molecule's fundamental structure:
a chain of four carbon atoms. Piria thought that asparagine was a diamide of malic acid;
[12]
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.
[13]
 In 1886, the Italian chemist Arnaldo Piutti (1857–1928) 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.[14] Since the structure of asparagine was still not
fully known – the location of the amine group within the molecule was still not settled[15] –
Piutti synthesized asparagine and thus published its true structure in 1888.[16]

Structural function in proteins[edit]

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-serineor X-
threonine, where X is any amino acid with the exception of proline.[17]
Asparagine can be hydroxylated in the HIF1 hypoxia inducible transcription factor. This
modification inhibits HIF1-mediated gene activation.[18]

Sources[edit]
Dietary sources[edit]
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
 Plant sources: asparagus, potatoes, legumes, nuts, seeds, soy, whole grains
Biosynthesis and catabolism[edit]
The precursor to asparagine is oxaloacetate, which a transaminase enzyme converts
to aspartate. 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.
Asparagine synthetase uses ATP to activate aspartate, forming β-aspartyl-
AMP.  Glutamine donates an ammonium group, which reacts with β-aspartyl-AMP to form
asparagine and free AMP.[19]

The biosynthesis of asparagine from oxaloacetate

In 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).[19]
Acrylamide controversy[edit]
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.[20]