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<div class="card-header"> Aspartic </div>
<div class="card-body">
<h5 class="card-title"> <i class="fa fa-info-circle" aria-hidden="true" title="information about amino-acid"></i>
</h5>
<p class="card-text">
<a-scene>
<a-assets>
<a-asset-item id="Aspartate_aminotransferase" src="/models/5AX8.glb"></a-asset-item>
</a-assets>
<a-entity gltf-model="#Aspartate_aminotransferase" animation-mixer position="30 32 -150" rotation="100 0 20"></a-entity>
</a-scene>
<table>
<tr>
<th> Group, </th>
<th> Alien-Protein-code, </th>
<th> Agent, </th>
<th> Formula, </th>
</tr>
<tr>
<td> Benzyl-group which is subsuite of methyl-group of alanine. </td>
<td>
Aspartate transaminase (AST),
</td>
<td> Acidic, </td>
<td>
<a class="jmol" href="https://chemapps.stolaf.edu/jmol/jmol.php?model=O%3DC%28%5BO-%5D%29CC%28%5BNH3%2B%5D%29C%28%3DO%29%5BO-%5D"title="Chemical structure of Aspartate molecule. In Aspartate compound Hydrogen atoms are abudant.">
C<small class="subscript">4-</small>H<small class="subscript">7-</small>NO<small class="subscript">4</small>
</a>
</td>
</tr>
<tr>
<th> Weight, </th>
<th> Nature, </th>
<th> Role, </th>
<th> Sidechain, </th>
</tr>
<tr>
<td>
133.103 g·mol−1,
</td>
<td>
</td>
<td>
D-Aspartate is one of two D-amino acids commonly found in mammals.
In proteins aspartate sidechains are often hydrogen bonded to form asx turns or asx motifs, which frequently occur at the N-termini of alpha helices.
The L-isomer of Asp is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins.
In the human body, aspartate is most frequently synthesized through the transamination of oxaloacetate.
In plants and microorganisms, aspartate is the precursor to several amino acids, including four that are essential for humans: methionine, threonine, isoleucine, and lysine.
In the urea cycle, aspartate and ammonia donate amino groups leading to the formation of urea.
It is 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.
Aspartate donates one nitrogen atom in the biosynthesis of inosine, the precursor to the purine bases. In addition, aspartic acid acts as a hydrogen acceptor in a chain of ATP synthase.
Dietary L-aspartic acid has been shown to act as an inhibitor of Beta-glucuronidase, which serves to regulate enterohepatic circulation of bilirubin and bile acids.
<li> Neurotransmitter </li>
</td>
<td>
CH2COOH,
</td>
</tr>
</table>
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