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		<id>https://en.formulasearchengine.com/index.php?title=Ornithine(lysine)_transaminase&amp;diff=20816</id>
		<title>Ornithine(lysine) transaminase</title>
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		<updated>2013-01-28T18:51:39Z</updated>

		<summary type="html">&lt;p&gt;138.202.150.157: &lt;/p&gt;
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&lt;div&gt;{{enzyme&lt;br /&gt;
| Name = succinylornithine transaminase&lt;br /&gt;
| EC_number = 2.6.1.81&lt;br /&gt;
| CAS_number = &lt;br /&gt;
| IUBMB_EC_number = 2/6/1/81&lt;br /&gt;
| GO_code = 0043825&lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption = &lt;br /&gt;
}}&lt;br /&gt;
&lt;br /&gt;
In [[enzymology]], a &#039;&#039;&#039;succinylornithine transaminase&#039;&#039;&#039; ({{EC number|2.6.1.81}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]&lt;br /&gt;
&lt;br /&gt;
:N&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;-succinyl-L-ornithine + 2-oxoglutarate &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; N-succinyl-L-glutamate 5-semialdehyde + L-glutamate&lt;br /&gt;
&lt;br /&gt;
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[N2-succinyl-L-ornithine]] and [[2-oxoglutarate]], whereas its two [[product (chemistry)|products]] are [[N-succinyl-L-glutamate 5-semialdehyde]] and [[L-glutamate]].&lt;br /&gt;
&lt;br /&gt;
This enzyme belongs to the family of [[transferase]]s, specifically the [[transaminases]], which transfer nitrogenous groups.  The systematic name of this enzyme class is &#039;&#039;&#039;N2-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase&#039;&#039;&#039;. Other names in common use include &#039;&#039;&#039;succinylornithine aminotransferase&#039;&#039;&#039;, &#039;&#039;&#039;N2-succinylornithine 5-aminotransferase&#039;&#039;&#039;, &#039;&#039;&#039;AstC&#039;&#039;&#039;, &#039;&#039;&#039;SOAT&#039;&#039;&#039;, and &#039;&#039;&#039;2-N-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase&#039;&#039;&#039;.  This enzyme participates in [[arginine and proline metabolism]].  &lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{reflist|1}}&lt;br /&gt;
* {{cite journal | author = Vander Wauven C, Stalon V | date = 1985 | title = Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia | journal = J. Bacteriol.  | volume = 164 | pages = 882&amp;amp;ndash;6  | pmid = 2865249 | issue = 2 | pmc = 214334 }}&lt;br /&gt;
* {{cite journal | author = Schneider BL, Kiupakis AK, Reitzer LJ | date = 1998 | title = Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli | journal = J. Bacteriol.  | volume = 180 | pages = 4278&amp;amp;ndash;86  | pmid = 9696779 | issue = 16 | pmc = 107427 }}&lt;br /&gt;
* {{cite journal | author = Cunin R, Glansdorff N, Pierard A, Stalon V | date = 1986 | title = Biosynthesis and metabolism of arginine in bacteria | journal = Microbiol. Rev.  | volume = 50 | pages = 314&amp;amp;ndash;52  | pmid = 3534538 | issue = 3 | pmc = 373073 }}&lt;br /&gt;
* {{cite journal | author = Itoh Y | date = 1997 | title = Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa | journal = J. Bacteriol.  | volume = 179 | pages = 7280&amp;amp;ndash;90  | pmid = 9393691 | issue = 23 | pmc = 179677 }}&lt;br /&gt;
* {{cite journal | author = Stalon V, Vander Wauven C, Momin P, Legrain C | date = 1987 | title = Catabolism of arginine, citrulline and ornithine by Pseudomonas and related bacteria | journal = J. Gen. Microbiol.  | volume = 133 | pages = 2487&amp;amp;ndash;95  | pmid = 3129535 | issue = 9 }}&lt;br /&gt;
&lt;br /&gt;
{{transferase-stub}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 2.6.1]]&lt;br /&gt;
[[Category:Enzymes of unknown structure]]&lt;/div&gt;</summary>
		<author><name>138.202.150.157</name></author>
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