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	<entry>
		<id>https://en.formulasearchengine.com/w/index.php?title=Benzoin_aldolase&amp;diff=19659</id>
		<title>Benzoin aldolase</title>
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		<updated>2013-11-04T07:17:32Z</updated>

		<summary type="html">&lt;p&gt;78.128.188.193: &lt;/p&gt;
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&lt;div&gt;{{enzyme&lt;br /&gt;
| Name = citrate (pro-3S)-lyase&lt;br /&gt;
| EC_number = 4.1.3.6&lt;br /&gt;
| CAS_number = 9012-83-3&lt;br /&gt;
| IUBMB_EC_number = 4/1/3/6&lt;br /&gt;
| GO_code = 0008815&lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption = &lt;br /&gt;
}}&lt;br /&gt;
In [[enzymology]], a &#039;&#039;&#039;citrate (pro-3S)-lyase&#039;&#039;&#039; ({{EC number|4.1.3.6}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
:citrate &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; acetate + oxaloacetate&lt;br /&gt;
&lt;br /&gt;
Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[citrate]], and two [[product (chemistry)|products]], [[acetate]] and [[oxaloacetate]].&lt;br /&gt;
&lt;br /&gt;
This enzyme belongs to the family of [[lyase]]s, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds.  The systematic name of this enzyme class is &#039;&#039;&#039;citrate oxaloacetate-lyase (forming acetate from the pro-S carboxymethyl group of citrate)&#039;&#039;&#039;. Other names in common use include &#039;&#039;&#039;citrase&#039;&#039;&#039;, &#039;&#039;&#039;citratase&#039;&#039;&#039;, &#039;&#039;&#039;citritase&#039;&#039;&#039;, &#039;&#039;&#039;citridesmolase&#039;&#039;&#039;, &#039;&#039;&#039;citrate aldolase&#039;&#039;&#039;, &#039;&#039;&#039;citric aldolase&#039;&#039;&#039;, &#039;&#039;&#039;citrate lyase&#039;&#039;&#039;, &#039;&#039;&#039;citrate oxaloacetate-lyase&#039;&#039;&#039;, and &#039;&#039;&#039;citrate oxaloacetate-lyase [(pro-3S)-CH2COO--&amp;gt;acetate]&#039;&#039;&#039;.  This enzyme participates in [[citrate cycle (tca cycle)]] and [[two-component system - general]].  &lt;br /&gt;
&lt;br /&gt;
==Structural studies==&lt;br /&gt;
&lt;br /&gt;
As of late 2007, 4 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1U5H}}, {{PDB link|1U5V}}, {{PDB link|1Z6K}}, and {{PDB link|2HJ0}}.&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{reflist|1}}&lt;br /&gt;
* {{cite journal | author = DAGLEY S, DAWES EA | date = 1955 | title = Citridesmolase: its properties and mode of action | journal = Biochim. Biophys. Acta.  | volume = 17 | pages = 177&amp;amp;ndash;84  | pmid = 13239657 | doi = 10.1016/0006-3002(55)90348-6 | issue = 2 }}&lt;br /&gt;
* {{cite journal | author = Dimroth P, Loyal R, Eggerer H | date = 1977 | title = Characterization of the isolated transferase subunit of citrate lyase as a CoA-Transferase. Evidence against a covalent enzyme-substrate intermediate | journal = Eur. J. Biochem.  | volume = 80 | pages = 479&amp;amp;ndash;88  | pmid = 336371 | doi = 10.1111/j.1432-1033.1977.tb11903.x | issue = 2 }}&lt;br /&gt;
&lt;br /&gt;
{{4.1-enzyme-stub}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 4.1.3]]&lt;br /&gt;
[[Category:Enzymes of known structure]]&lt;/div&gt;</summary>
		<author><name>78.128.188.193</name></author>
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