<?xml version="1.0" encoding='utf-8'?>
<!DOCTYPE wml PUBLIC "-//WAPFORUM//DTD WML 1.1//EN" "http://www.wapforum.org/DTD/wml_1.1.xml">
<wml>
<card id="card1" title="Aspartate transaminase - Page 10 - Wikipedia">
<p>
<a accesskey="1" href="page.php?w=Aspartate_transaminase&amp;p=9">1.Previous</a><br />
<a accesskey="3" href="page.php?w=Aspartate_transaminase&amp;p=11">3.Next</a>
</p>
<p>binding.</p>

<p>The two independent active sites are positioned near the interface between the two domains. Within each active site, a couple arginine residues are responsible for the enzyme's specificity for <a href="page.php?w=dicarboxylic_acid">dicarboxylic acid</a> substrates:  Arg386 interacts with the substrate's proximal (?-)carboxylate group, while Arg292 complexes with the distal (side-chain) carboxylate.</p>

<p>In terms of secondary structure, AST contains both ? and ? elements.  Each domain has a central sheet of ?-strands with ?-helices</p><p>
<a accesskey="1" href="page.php?w=Aspartate_transaminase&amp;p=9">1.Previous</a><br />
<a accesskey="3" href="page.php?w=Aspartate_transaminase&amp;p=11">3.Next</a>
</p>

<do type="prev" label="Search">
        <go href="search.wml"/>
</do>

</card>
</wml>
