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Aspartic acid (abbreviated as Asp or D; Asx or B represent either aspartic acid or asparagine) is an α-amino acid with the chemical formula HO2CCH(NH2)CH2CO2H
The L-isomer is one of the 20 proteinogenic amino acids, i.e., the building blocks of proteins. Its codons are GAU and GAC.
The carboxylate anion of aspartic acid is known as aspartate.
Aspartic acid is, together with glutamic acid, classified as an acidic amino acid.
Aspartic acid is pervasive in biosynthesis.
As with all amino acids, the location of acid protons depends on the pH of the solution and the crystallization conditions.
Role in biosynthesis of amino acids:
Aspartic acid is non-essential in mammals, being produced from oxaloacetate by transamination.
The conversion of aspartic acid to these other amino acids begins with reduction of aspartic acid to its "semialdehyde," HO2CCH(NH2)CH2CHO.
Asparagine is derived from aspartic acid via transamidation:
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HO2CCH(NH2)CH2CO2H + GC(O)NH2 HO2CCH(NH2)CH2CONH2 + GC(O)OH
(where GC(O)NH2 and GC(O)OH are glutamine and glutamic acid, respectively).
Other biochemical roles:
Aspartic acid is also a metabolite in the urea cycle and participates in gluconeogenesis.
It carries reducing equivalents in the malate-aspartate shuttle, which utilizes the ready interconversion of aspartate and oxaloacetate, which is the oxidized (dehydrogenated) derivative of malic acid.
Aspartic acid donates one nitrogen atom in the biosynthesis of inositol, the precursor to the purine bases.
Neurotransmitter:
Aspartate (the conjugate base of aspartic acid) stimulates NMDA receptors, though not as strongly as the amino acid neurotransmitter glutamate does. [3]
Chemical Synthesis:
Racemic aspartic acid can be synthesized from diethyl sodium phthalimidomalonate, (C6H4(CO)2NC(CO2Et)2). *
* Read an Article in Wikipedia June 5, 2011