https://en.formulasearchengine.com/w/api.php?action=feedcontributions&feedformat=atom&user=128.32.125.27formulasearchengine - User contributions [en]2026-09-23T20:18:43ZUser contributionsMediaWiki 1.47.0-wmf.7https://en.formulasearchengine.com/w/index.php?title=Taxadiene_synthase&diff=19963Taxadiene synthase2012-02-09T22:30:21Z<p>128.32.125.27: </p>
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<div>{{enzyme<br />
| Name = adenosine-tetraphosphatase<br />
| EC_number = 3.6.1.14<br />
| CAS_number = 37289-26-2<br />
| IUBMB_EC_number = 3/6/1/14<br />
| GO_code = 0047624<br />
| image = <br />
| width = <br />
| caption = <br />
}}<br />
In [[enzymology]], an '''adenosine-tetraphosphatase''' ({{EC number|3.6.1.14}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]<br />
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:adenosine 5'-tetraphosphate + H<sub>2</sub>O <math>\rightleftharpoons</math> ATP + phosphate<br />
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Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine 5'-tetraphosphate]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[adenosine triphosphate|ATP]] and [[phosphate]].<br />
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This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is '''adenosine-tetraphosphate phosphohydrolase'''. This enzyme participates in [[purine metabolism]]. <br />
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==Structural studies==<br />
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As of late 2007, only one [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|2V7Q}}.<br />
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==References==<br />
{{reflist|1}}<br />
* {{cite journal | author = Small GD, Cooper C | date = 1966 | title = Purification and properties of nucleoside tetraphosphate hydrolase from rabbit muscle | journal = Biochemistry. | volume = 5 | pages = 14&ndash;26 | pmid = 4287215 | doi = 10.1021/bi00865a003 | issue = 1 }}<br />
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{{hydrolase-stub}}<br />
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[[Category:EC 3.6.1]]<br />
[[Category:Enzymes of known structure]]</div>128.32.125.27