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		<id>https://en.formulasearchengine.com/w/index.php?title=Glucose-1-phosphate_adenylyltransferase&amp;diff=21205</id>
		<title>Glucose-1-phosphate adenylyltransferase</title>
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		<updated>2010-10-29T10:43:26Z</updated>

		<summary type="html">&lt;p&gt;141.14.245.16: &lt;/p&gt;
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&lt;div&gt;{{enzyme&lt;br /&gt;
| Name = glycerate kinase&lt;br /&gt;
| EC_number = 2.7.1.31&lt;br /&gt;
| CAS_number = 9026-61-3&lt;br /&gt;
| IUBMB_EC_number = 2/7/1/31&lt;br /&gt;
| GO_code = 0008887&lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption = &lt;br /&gt;
}}&lt;br /&gt;
{{Pfam box |Symbol = Glyc_kinase |Name = Glycerate kinase |Pfam = PF02595 |InterPro = IPR004381 |PROSITE =  |PDB = {{PDB|1to6}} }}&lt;br /&gt;
&lt;br /&gt;
In [[enzymology]], a &#039;&#039;&#039;glycerate kinase&#039;&#039;&#039; ({{EC number|2.7.1.31}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
:ATP + (R)-glycerate &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; ADP + 3-phospho-(R)-glycerate&lt;br /&gt;
&lt;br /&gt;
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[(R)-glycerate]], whereas its two [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]] and [[3-phospho-(R)-glycerate]].&lt;br /&gt;
&lt;br /&gt;
This enzyme belongs to the family of [[transferase]]s, specifically those transferring phosphorus-containing groups ([[phosphotransferase]]s) with an alcohol group as acceptor.  The systematic name of this enzyme class is &#039;&#039;&#039;ATP:(R)-glycerate 3-phosphotransferase&#039;&#039;&#039;. Other names in common use include &#039;&#039;&#039;glycerate kinase (phosphorylating)&#039;&#039;&#039;, &#039;&#039;&#039;D-glycerate 3-kinase&#039;&#039;&#039;, &#039;&#039;&#039;D-glycerate kinase&#039;&#039;&#039;, &#039;&#039;&#039;glycerate-3-kinase&#039;&#039;&#039;, &#039;&#039;&#039;GK&#039;&#039;&#039;, &#039;&#039;&#039;D-glyceric acid kinase&#039;&#039;&#039;, and &#039;&#039;&#039;ATP:D-glycerate 2-phosphotransferase&#039;&#039;&#039;.  This enzyme participates in 3 [[metabolism|metabolic pathways]]: [[serine]]/[[glycine]]/[[threonine]] metabolism, [[glycerolipid]] metabolism, and [[glyoxylate]]-[[dicarboxylate]] 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|1TO6}}, {{PDB link|1X3L}}, and {{PDB link|2B8N}}.&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{reflist|1}}&lt;br /&gt;
* {{cite journal | author = Doughty CC, Hayashi JA, Guenther HL | date = 1966 | title = Purification and properties of D-glycerate 3-kinase from Escherichia coli | journal = J. Biol. Chem.  | volume = 241 | pages = 568&amp;amp;ndash;72  | pmid = 5325263 | issue = 3 }}&lt;br /&gt;
* {{cite journal | author = ICHIHARA A, GREENBERG DM | date = 1957 | title = Studies on the purification and properties of D-glyceric acid kinase of liver | journal = J. Biol. Chem.  | volume = 225 | pages = 949&amp;amp;ndash;58  | pmid = 13416296 | issue = 2 }}&lt;br /&gt;
&lt;br /&gt;
{{enzyme-stub}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 2.7.1]]&lt;br /&gt;
[[Category:Enzymes of known structure]]&lt;/div&gt;</summary>
		<author><name>141.14.245.16</name></author>
	</entry>
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