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	<entry>
		<id>https://en.formulasearchengine.com/index.php?title=Halstead_complexity_measures&amp;diff=20081</id>
		<title>Halstead complexity measures</title>
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		<updated>2014-01-29T17:04:43Z</updated>

		<summary type="html">&lt;p&gt;103.18.72.150: /* Example */&lt;/p&gt;
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&lt;div&gt;{{enzyme&lt;br /&gt;
| Name = phospholipid-translocating ATPase&lt;br /&gt;
| EC_number = 3.6.3.1&lt;br /&gt;
| CAS_number = &lt;br /&gt;
| IUBMB_EC_number = 3/6/3/1&lt;br /&gt;
| GO_code = 0004012&lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption = &lt;br /&gt;
}}&lt;br /&gt;
In [[enzymology]], a &#039;&#039;&#039;phospholipid-translocating ATPase&#039;&#039;&#039; ({{EC number|3.6.3.1}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
:ATP + H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;O + phospholipidin &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; ADP + phosphate + phospholipidout&lt;br /&gt;
&lt;br /&gt;
The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]], [[water|H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;O]], and [[phospholipid]], whereas its 3 [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]], [[phosphate]], and [[phospholipid]].&lt;br /&gt;
&lt;br /&gt;
This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is &#039;&#039;&#039;ATP phosphohydrolase (phospholipid-flipping)&#039;&#039;&#039;. Other names in common use include &#039;&#039;&#039;Mg&amp;lt;sup&amp;gt;2+&amp;lt;/sup&amp;gt;-ATPase&#039;&#039;&#039;, &#039;&#039;&#039;flippase&#039;&#039;&#039;, and &#039;&#039;&#039;aminophospholipid-transporting ATPase&#039;&#039;&#039;.  &lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{reflist|1}}&lt;br /&gt;
* {{cite journal | author = Morris MB, Auland ME, Xu YH, Roufogalis BD | year = 1993 | title = Characterization of the Mg(2+)-ATPase activity of the human erythrocyte membrane | journal = Biochem. Mol. Biol. Int.  | volume = 31 | pages = 823&amp;amp;ndash;32  | pmid = 8136700 | issue = 5 }}&lt;br /&gt;
* {{cite journal | doi = 10.3109/09687689609160582 | author = Vermeulen WP, Briede JJ, Roelofsen B | year = 1996 | title = Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity | journal = Mol. Membr. Biol.  | volume = 13 | pages = 95&amp;amp;ndash;102  | pmid = 8839453 | issue = 2 }}&lt;br /&gt;
* {{cite journal | author = Suzuki H, Kamakura M, Morii M, Takeguchi N | year = 1997 | title = The phospholipid flippase activity of gastric vesicles | journal = J. Biol. Chem.  | volume = 272 | pages = 10429&amp;amp;ndash;34  | pmid = 9099684 | doi = 10.1074/jbc.272.16.10429 | issue = 16 }}&lt;br /&gt;
* {{cite journal | author = Auland ME, Roufogalis BD, Devaux PF, Zachowski A | year = 1994 | title = Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes | journal = Proc. Natl. Acad. Sci. U.S.A.  | volume = 91 | pages = 10938&amp;amp;ndash;42  | pmid = 7971987 | doi = 10.1073/pnas.91.23.10938 | issue = 23 | pmc = 45141 }}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 3.6.3]]&lt;br /&gt;
[[Category:Enzymes of unknown structure]]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
{{hydrolase-stub}}&lt;/div&gt;</summary>
		<author><name>103.18.72.150</name></author>
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