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&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;{{enzyme&lt;br /&gt;
| Name = aspartate racemase&lt;br /&gt;
| EC_number = 5.1.1.13&lt;br /&gt;
| CAS_number = 37237-56-2&lt;br /&gt;
| IUBMB_EC_number = 5/1/1/13&lt;br /&gt;
| GO_code = 0047689&lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption = &lt;br /&gt;
}}&lt;br /&gt;
In [[enzymology]], an &amp;#039;&amp;#039;&amp;#039;aspartate racemase&amp;#039;&amp;#039;&amp;#039; ({{EC number|5.1.1.13}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
:L-aspartate &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; D-aspartate&lt;br /&gt;
&lt;br /&gt;
Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[aspartic acid|L-aspartate]], and one [[product (chemistry)|product]], [[aspartic acid|D-aspartate]].&lt;br /&gt;
&lt;br /&gt;
This enzyme belongs to the family of [[isomerase]]s, specifically those [[racemase]]s and [[epimerase]]s acting on [[amino acid]]s and derivatives.  The systematic name of this enzyme class is &amp;#039;&amp;#039;&amp;#039;aspartate racemase&amp;#039;&amp;#039;&amp;#039;. Other names in common use include &amp;#039;&amp;#039;&amp;#039;D-aspartate racemase&amp;#039;&amp;#039;&amp;#039;, and &amp;#039;&amp;#039;&amp;#039;McyF&amp;#039;&amp;#039;&amp;#039;.  This enzyme participates in [[alanine]] and [[aspartate]] metabolism.  &lt;br /&gt;
&lt;br /&gt;
==Structural studies==&lt;br /&gt;
&lt;br /&gt;
As of late 2007, 3 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1IU9}}, {{PDB link|1JFL}}, and {{PDB link|2DX7}}.&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{reflist|1}}&lt;br /&gt;
* {{cite journal | author = Lamont HC, Staudenbauer WL, Strominger JL | date = 1972 | title = Partial purification and characterization of an aspartate racemase from Streptococcus faecalis | journal = J. Biol. Chem.  | volume = 247 | pages = 5103&amp;amp;ndash;6  | pmid = 4626916 | issue = 16 }}&lt;br /&gt;
* {{cite journal | author = Yamauchi T, Choi SY, Okada H, Yohda M, Kumagai H, Esaki N, Soda K | date = 1992 | title = Properties of aspartate racemase, a pyridoxal 5&amp;#039;-phosphate-independent amino acid racemase | journal = J. Biol. Chem.  | volume = 267 | pages = 18361&amp;amp;ndash;4  | pmid = 1526977 | issue = 26 }}&lt;br /&gt;
* {{cite journal | author = Liu L, Iwata K, Kita A, Kawarabayasi Y, Yohda M, Miki K | date = 2002 | title = Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization | journal = J. Mol. Biol.  | volume = 319 | pages = 479&amp;amp;ndash;89  | pmid = 12051922 | doi = 10.1016/S0022-2836(02)00296-6 | issue = 2 }}&lt;br /&gt;
* {{cite journal | author = H, Borner T, Schwecke T | date = 2003 | title = The mcyF gene of the microcystin biosynthetic gene cluster from Microcystis aeruginosa encodes an aspartate racemase | journal = Biochem. J.  | volume = 373 | pages = 909&amp;amp;ndash;16  | pmid = 12713441 | doi = 10.1042/BJ20030396 | issue = Pt 3 | pmc = 1223527 }}&lt;br /&gt;
* {{cite journal | author = Yamashita T, Ashiuchi M, Ohnishi K, Kato S, Nagata S, Misono H | date = 2004 | title = Molecular identification of monomeric aspartate racemase from Bifidobacterium bifidum | journal = Eur. J. Biochem.  | volume = 271 | pages = 4798&amp;amp;ndash;803  | pmid = 15606767 | doi = 10.1111/j.1432-1033.2004.04445.x | issue = 23–24 }}&lt;br /&gt;
&lt;br /&gt;
{{isomerase-stub}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 5.1.1]]&lt;br /&gt;
[[Category:Enzymes of known structure]]&lt;/div&gt;</summary>
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