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	<id>https://en.formulasearchengine.com/api.php?action=feedcontributions&amp;feedformat=atom&amp;user=84.160.202.124</id>
	<title>formulasearchengine - User contributions [en]</title>
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	<updated>2026-05-22T08:27:19Z</updated>
	<subtitle>User contributions</subtitle>
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	<entry>
		<id>https://en.formulasearchengine.com/index.php?title=Unspecific_peroxygenase&amp;diff=28616</id>
		<title>Unspecific peroxygenase</title>
		<link rel="alternate" type="text/html" href="https://en.formulasearchengine.com/index.php?title=Unspecific_peroxygenase&amp;diff=28616"/>
		<updated>2013-12-13T09:47:10Z</updated>

		<summary type="html">&lt;p&gt;84.160.202.124: correct some fact: Unspecific peroxygenase is not a P450 enzyme!&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Infobox enzyme&lt;br /&gt;
| Name = Linoleate 10R-lipoxygenase&lt;br /&gt;
| EC_number = 1.13.11.62&lt;br /&gt;
| CAS_number = &lt;br /&gt;
| IUBMB_EC_number = 1/13/11/62&lt;br /&gt;
| GO_code = &lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption =&lt;br /&gt;
}}&lt;br /&gt;
&#039;&#039;&#039;Linoleate 10R-lipoxygenase&#039;&#039;&#039; ({{EC number|1.13.11.62}}, &#039;&#039;10R-DOX&#039;&#039;, &#039;&#039;(10R)-dioxygenase&#039;&#039;, &#039;&#039;10R-dioxygenase&#039;&#039;) is an [[enzyme]] with system name &#039;&#039;linoleate:oxygen (10R)-oxidoreductase&#039;&#039;.&amp;lt;ref&amp;gt;{{cite journal | title = Leucine/valine residues direct oxygenation of linoleic acid by (10&amp;lt;em&amp;gt;R&amp;lt;/em&amp;gt;)- and (8&amp;lt;em&amp;gt;R&amp;lt;/em&amp;gt;)-dioxygenases: expression and site-directed mutagenesis of (10&amp;lt;em&amp;gt;R&amp;lt;/em&amp;gt;)-dioxygenase with epoxyalcohol synthase activity |author = Garscha, U. and Oliw, E.H. |journal = J. Biol. Chem. |year = 2009 |volume = 284 |pages = 13755–13765 |pmid = 19289462 |doi=10.1074/jbc.M808665200 |issue=20 |pmc=2679477}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Reaction mechanism of 5,8-linoleate diol synthase, 10&amp;lt;em&amp;gt;R&amp;lt;/em&amp;gt;-dioxygenase, and 8,11-hydroperoxide isomerase of &amp;lt;em&amp;gt;Aspergillus clavatus&amp;lt;/em&amp;gt; |author = Jerneren, F., Garscha, U., Hoffmann, I., Hamberg, M. and Oliw, E.H. |journal = Biochim. Biophys. Acta |year = 2010 |volume = 1801 |pages = 503–507 |pmid = 20045744 |doi=10.1016/j.bbalip.2009.12.012 |issue=4}}&amp;lt;/ref&amp;gt; This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
: linoleate + O&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt; &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; (8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate&lt;br /&gt;
&lt;br /&gt;
Linoleate 10R-lipoxygenase is involved in biosynthesis of [[oxylipins]].&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
{{reflist}}&lt;br /&gt;
&lt;br /&gt;
== External links ==&lt;br /&gt;
* {{MeshName|Linoleate+10R-lipoxygenase}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 1.13.11]]&lt;/div&gt;</summary>
		<author><name>84.160.202.124</name></author>
	</entry>
	<entry>
		<id>https://en.formulasearchengine.com/index.php?title=Feruloyl_esterase&amp;diff=20189</id>
		<title>Feruloyl esterase</title>
		<link rel="alternate" type="text/html" href="https://en.formulasearchengine.com/index.php?title=Feruloyl_esterase&amp;diff=20189"/>
		<updated>2013-12-13T09:31:47Z</updated>

		<summary type="html">&lt;p&gt;84.160.202.124: just correct typo (missing word) and cut out some abbreviations (only FAE, not FAEI and FAEII...)&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{enzyme&lt;br /&gt;
| Name = glucosylglycerol 3-phosphatase&lt;br /&gt;
| EC_number = 3.1.3.69&lt;br /&gt;
| CAS_number = &lt;br /&gt;
| IUBMB_EC_number = 3/1/3/69&lt;br /&gt;
| GO_code = 0050530&lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption = &lt;br /&gt;
}}&lt;br /&gt;
In [[enzymology]], a &#039;&#039;&#039;glucosylglycerol 3-phosphatase&#039;&#039;&#039; ({{EC number|3.1.3.69}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
:2-(beta-D-glucosyl)-sn-glycerol-3-phosphate + H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;O &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; 2-(beta-D-glucosyl)-sn-glycerol + phosphate&lt;br /&gt;
&lt;br /&gt;
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[2-(beta-D-glucosyl)-sn-glycerol-3-phosphate]] and [[water|H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;O]], whereas its two [[product (chemistry)|products]] are [[2-(beta-D-glucosyl)-sn-glycerol]] and [[phosphate]].&lt;br /&gt;
&lt;br /&gt;
This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on phosphoric [[ester|monoester]] bonds.  The systematic name of this enzyme class is &#039;&#039;&#039;2-(beta-D-glucosyl)-sn-glycerol-3-phosphate phosphohydrolase&#039;&#039;&#039;. This enzyme is also called &#039;&#039;&#039;salt tolerance protein A, StpA&#039;&#039;&#039;.  &lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{reflist|1}}&lt;br /&gt;
* {{cite journal | author = Hagemann M and Erdmann N | date = 1994 | title = Activation and pathway of glucosylglycerol biosynthesis in the cyanobacterium Synechocystis sp. PCC 6803 | journal = Microbiology  | volume = 140 | pages = 1427&amp;amp;ndash;1431 | doi = 10.1099/00221287-140-6-1427 | issue = 6 }}&lt;br /&gt;
* {{cite journal | author = Hagemann M, Richter S, Zuther E, Schoor A | date = 1996 | title = Characterization of a glucosylglycerol-phosphate-accumulating, salt-sensitive mutant of the cyanobacterium Synechocystis sp. strain PCC 6803 | journal = Arch. Microbiol.  | volume = 166 | pages = 83&amp;amp;ndash;91  | pmid = 8772170 | doi = 10.1007/s002030050360 | issue = 2 }}&lt;br /&gt;
* {{cite journal | author = Hagemann M, Schoor A, Jeanjean R, Zuther E, Joset F | date = 1997 | title = The stpA gene form synechocystis sp. strain PCC 6803 encodes the glucosylglycerol-phosphate phosphatase involved in cyanobacterial osmotic response to salt shock | journal = J. Bacteriol.  | volume = 179 | pages = 1727&amp;amp;ndash;33  | pmid = 9045835 | issue = 5 | pmc = 178888 }}&lt;br /&gt;
&lt;br /&gt;
{{hydrolase-stub}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 3.1.3]]&lt;br /&gt;
[[Category:Enzymes of unknown structure]]&lt;/div&gt;</summary>
		<author><name>84.160.202.124</name></author>
	</entry>
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