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	<title>Benzylsuccinate synthase - Revision history</title>
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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 = D-dopachrome decarboxylase&lt;br /&gt;
| EC_number = 4.1.1.84&lt;br /&gt;
| CAS_number = 184111-06-6&lt;br /&gt;
| IUBMB_EC_number = 4/1/1/84&lt;br /&gt;
| GO_code = &lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption = &lt;br /&gt;
}}&lt;br /&gt;
In [[enzymology]], a &amp;#039;&amp;#039;&amp;#039;D-dopachrome decarboxylase&amp;#039;&amp;#039;&amp;#039; ({{EC number|4.1.1.84}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
:D-dopachrome &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; 5,6-dihydroxyindole + CO&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;&lt;br /&gt;
&lt;br /&gt;
Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[D-dopachrome]], and two [[product (chemistry)|products]], [[5,6-dihydroxyindole]] and [[carbon dioxide|CO&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;]].&lt;br /&gt;
&lt;br /&gt;
This enzyme belongs to the family of [[lyase]]s, specifically the carboxy-lyases, which cleave carbon-carbon bonds.  The systematic name of this enzyme class is &amp;#039;&amp;#039;&amp;#039;D-dopachrome carboxy-lyase (5,6-dihydroxyindole-forming)&amp;#039;&amp;#039;&amp;#039;. Other names in common use include &amp;#039;&amp;#039;&amp;#039;phenylpyruvate tautomerase II&amp;#039;&amp;#039;&amp;#039;, &amp;#039;&amp;#039;&amp;#039;D-tautomerase&amp;#039;&amp;#039;&amp;#039;, &amp;#039;&amp;#039;&amp;#039;D-dopachrome tautomerase&amp;#039;&amp;#039;&amp;#039;, and &amp;#039;&amp;#039;&amp;#039;D-dopachrome carboxy-lyase&amp;#039;&amp;#039;&amp;#039;.  &lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{reflist|1}}&lt;br /&gt;
* {{cite journal | author = Odh G, Hindemith A, Rosengren AM, Rosengren E, Rorsman H | date = 1993 | title = Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole | journal = Biochem. Biophys. Res. Commun.  | volume = 197 | pages = 619&amp;amp;ndash;24  | pmid = 8267597 | doi = 10.1006/bbrc.1993.2524 | issue = 2 }}&lt;br /&gt;
* {{cite journal | author = Yoshida H, Nishihira J, Suzuki M, Hikichi K | date = 1997 | title = NMR characterization of physicochemical properties of rat D-dopachrome tautomerase | journal = Biochem. Mol. Biol. Int.  | volume = 42 | pages = 891&amp;amp;ndash;9  | pmid = 9285056 | issue = 5 }}&lt;br /&gt;
* {{cite journal | author = J | date = 1999 | title = Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 A resolution | journal = Biochemistry.  | volume = 38 | pages = 3268&amp;amp;ndash;79  | pmid = 10079069 | doi = 10.1021/bi982184o | last2 = Taniguchi | first2 = M | last3 = Nakagawa | first3 = A | last4 = Tanaka | first4 = I | last5 = Suzuki | first5 = M | last6 = Nishihira | first6 = J | issue = 11 }}&lt;br /&gt;
* {{cite journal | author = A, Tanaka I, Sakai M | date = 1998 | title = Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation | journal = Biochem. Biophys. Res. Commun.  | volume = 243 | pages = 538&amp;amp;ndash;44  | pmid = 9480844 | doi = 10.1006/bbrc.1998.8123 | issue = 2 }}&lt;br /&gt;
&lt;br /&gt;
{{4.1-enzyme-stub}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 4.1.1]]&lt;br /&gt;
[[Category:Enzymes of unknown structure]]&lt;/div&gt;</summary>
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