Asparagine

Asparagine

  Asparagine is not an essential amino acid.......which means it can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet.....The nervous system needs Asparagine to maintain equilibrium....

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The licorice plant(contains asparagine) is part of the pea family and is found in Turkey and Greece, although it is propagated in many parts of the world.

      This herb(licorice) contains asparagine, biotin, choline, folic acid, glycyrrhizin, gum, inositol, lecithin, manganese, pantothenic acid, PABA, pentacyclic terpenes, phosphorus, vitamin B1, B2, B3, B6 and E.

Asparagine in Beef

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Asparagine was first isolated in 1806 from asparagus juice, in which it is abundant -- hence its name -- 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: in 1891, Marceli Nencki claimed that the substance responsible was methanethiol, and Robert White's 1975 research indicated that the substances were various thioesters.

Other likely possibilities include asparagine aminosuccinic monoamide.

Asparagine in Legumes

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 Structural function in proteins

     Since the asparagine side chain can make efficient hydrogen bond interactions with the peptide backbone, asparagines are often found near the beginning and end of alpha-helices, and in turn motifs in beta sheets.

Its role can be thought as "capping" the hydrogen bond interactions which would otherwise need to be satisfied by the polypeptide backbone.

Glutamines have an extra methylene group, have more conformational entropy and thus are less useful in this regard.

Asparagine in Eggs

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  Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains..

Asparagine in Seeds

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 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.

Asparagine in Dairy

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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 in Seafood

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Degradation

Aspartate is a glucogenic amino acid. L-asparginase 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.

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