<?xml version="1.0"?>
<feed xmlns="http://www.w3.org/2005/Atom" xml:lang="en">
	<id>https://en.formulasearchengine.com/w/api.php?action=feedcontributions&amp;feedformat=atom&amp;user=89.148.14.0%2F24</id>
	<title>formulasearchengine - User contributions [en]</title>
	<link rel="self" type="application/atom+xml" href="https://en.formulasearchengine.com/w/api.php?action=feedcontributions&amp;feedformat=atom&amp;user=89.148.14.0%2F24"/>
	<link rel="alternate" type="text/html" href="https://en.formulasearchengine.com/wiki/Special:Contributions/89.148.14.0/24"/>
	<updated>2026-09-24T14:34:31Z</updated>
	<subtitle>User contributions</subtitle>
	<generator>MediaWiki 1.47.0-wmf.7</generator>
	<entry>
		<id>https://en.formulasearchengine.com/w/index.php?title=Overtime_rate&amp;diff=17093</id>
		<title>Overtime rate</title>
		<link rel="alternate" type="text/html" href="https://en.formulasearchengine.com/w/index.php?title=Overtime_rate&amp;diff=17093"/>
		<updated>2013-12-31T13:58:11Z</updated>

		<summary type="html">&lt;p&gt;89.148.14.14: /* Calculation Formula */&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{Pfam_box &lt;br /&gt;
| Symbol = Urocanase &lt;br /&gt;
| Name = Urocanase &lt;br /&gt;
| image = PDB_2fkn_EBI.png&lt;br /&gt;
| width = &lt;br /&gt;
| caption = Crystal structure of Urocanase from &#039;&#039;B. subtilis&#039;&#039;.&lt;br /&gt;
| Pfam= PF01175&lt;br /&gt;
| InterPro= IPR000193&lt;br /&gt;
| SMART= &lt;br /&gt;
| Prosite = PDOC00947&lt;br /&gt;
| SCOP =     &lt;br /&gt;
| TCDB = &lt;br /&gt;
| OPM family= &lt;br /&gt;
| OPM protein= &lt;br /&gt;
| PDB= &lt;br /&gt;
{{PDB3|1uwk}}B:2-556     {{PDB3|1w1u}}A:2-556     {{PDB3|1uwl}}B:2-556     &lt;br /&gt;
}} &lt;br /&gt;
&lt;br /&gt;
[[Image:Urocanic acid.svg|thumb|[[Urocanic acid]]]]&lt;br /&gt;
[[Image:Imidazol-4-one-5-propionic acid.png|thumb|[[Imidazol-4-one-5-propionic acid]]]]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;Urocanase&#039;&#039;&#039;&amp;lt;ref name=&amp;quot;PUB00000161&amp;quot;&amp;gt;{{cite journal |author=Retey J |title=The urocanase story: a novel role of NAD+ as electrophile |journal=Arch. Biochem. Biophys. |volume=314 |issue=1 |pages=1–16 |year=1994 |pmid=7944380 |doi=10.1006/abbi.1994.1405}}&amp;lt;/ref&amp;gt; (also known as &#039;&#039;&#039;imidazolonepropionate hydrolase&#039;&#039;&#039; or &#039;&#039;&#039;urocanate hydratase&#039;&#039;&#039;) is the enzyme that catalyzes the second step in the degradation of histidine, the hydration of urocanate into imidazolonepropionate. &lt;br /&gt;
&lt;br /&gt;
: [[urocanate]] + H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;O &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; [[imidazol-4-one-5-propionic acid|4,5-dihydro-4-oxo-5-imidazolepropanoate]] &lt;br /&gt;
&lt;br /&gt;
Inherited deficiency of urocanase leads to elevated levels of urocanic acid in the urine, a condition known as [[urocanic aciduria]].&lt;br /&gt;
&lt;br /&gt;
Urocanase is found in some bacteria (gene hutU), in the liver of many vertebrates and has also been found in the plant &#039;&#039;[[Trifolium repens]]&#039;&#039; (white clover). Urocanase is a protein of about 60 Kd, it binds tightly to NAD&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt; and uses it as an electrophil cofactor. A conserved cysteine has been found to be important for the catalytic mechanism and could be involved in the binding of the NAD&amp;lt;sup&amp;gt;+&amp;lt;/sup&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{reflist}}&lt;br /&gt;
&lt;br /&gt;
==External links==&lt;br /&gt;
* {{MeshName|Urocanate+Hydratase}}&lt;br /&gt;
* {{EC number|4.2.1.49}}&lt;br /&gt;
&lt;br /&gt;
{{Carbon-oxygen lyases}}&lt;br /&gt;
{{Amino acid metabolism enzymes}}&lt;br /&gt;
&lt;br /&gt;
[[Category:Protein families]]&lt;br /&gt;
[[Category:EC 4.2.1]]&lt;br /&gt;
&lt;br /&gt;
{{Enzyme-stub}}&lt;/div&gt;</summary>
		<author><name>89.148.14.14</name></author>
	</entry>
</feed>