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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 = CDP-glucose 4,6-dehydratase&lt;br /&gt;
| EC_number = 4.2.1.45&lt;br /&gt;
| CAS_number = 37259-55-5&lt;br /&gt;
| IUBMB_EC_number = 4/2/1/45&lt;br /&gt;
| GO_code = 0047733&lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption = &lt;br /&gt;
}}&lt;br /&gt;
In the field of [[enzymology]], a &amp;#039;&amp;#039;&amp;#039;CDP-glucose 4,6-dehydratase&amp;#039;&amp;#039;&amp;#039; is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
:[[Cytidine diphosphate glucose|CDP-glucose]] &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; CDP-4-dehydro-6-deoxy-D-glucose + H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;O&lt;br /&gt;
&lt;br /&gt;
Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[cytidine diphosphate glucose|CDP-glucose]], and two [[product (chemistry)|products]], CDP-4-dehydro-6-deoxy-D-glucose and [[water|H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;O]].&lt;br /&gt;
&lt;br /&gt;
This enzyme belongs to the family of [[lyase]]s, specifically the hydro-lyases, which cleave carbon-oxygen bonds.  This enzyme participates in starch and sucrose [[metabolism]].  It employs one [[cofactor (biochemistry)|cofactor]], [[Nicotinamide adenine dinucleotide|NAD+]].  &lt;br /&gt;
&lt;br /&gt;
== Nomenclature ==&lt;br /&gt;
The systematic name of this enzyme class is CDP-glucose 4,6-hydro-lyase (CDP-4-dehydro-6-deoxy-D-glucose-forming). Other names in common use include:&lt;br /&gt;
*  cytidine diphosphoglucose oxidoreductase, and &lt;br /&gt;
* CDP-glucose 4,6-hydro-lyase.  &lt;br /&gt;
&lt;br /&gt;
==Structural studies==&lt;br /&gt;
&lt;br /&gt;
As of late 2007, two [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1RKX}} and {{PDB link|1WVG}}.&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{reflist|1}}&lt;br /&gt;
* {{cite journal | author = Hey AE, Elbein AD | date = 1966 | title = Biosynthesis of tyvelose. The purification and properties of cytidine diphosphate D-glucose oxidoreductase | journal = J. Biol. Chem.  | volume = 241 | pages = 5473&amp;amp;ndash;8  | pmid = 4380946 | issue = 22 }}&lt;br /&gt;
* {{cite journal | author = Matsuhashi S, Matsuhashi M, Brown JG, Strominger JL | date = 1966 | title = Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. 3 Cytidine diphosphate D-glucose oxidoreductase | journal = J. Biol. Chem.  | volume = 241 | pages = 4283&amp;amp;ndash;7  | pmid = 4288651 | issue = 18 }}&lt;br /&gt;
* {{cite journal | author = Melo A, Elliott WH, Glaser L | date = 1968 | title = The mechanism of 6-deoxyhexose synthesis. I. Intramolecular hydrogen transfer catalyzed by deoxythymidine diphosphate D-glucose oxidoreductase | journal = J. Biol. Chem.  | volume = 243 | pages = 1467&amp;amp;ndash;74  | pmid = 4869560 | issue = 7 }}&lt;br /&gt;
&lt;br /&gt;
{{4.2-enzyme-stub}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 4.2.1]]&lt;br /&gt;
[[Category:NADH-dependent enzymes]]&lt;br /&gt;
[[Category:Enzymes of known structure]]&lt;/div&gt;</summary>
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