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		<id>https://en.formulasearchengine.com/w/index.php?title=Synchronization_(alternating_current)&amp;diff=17131</id>
		<title>Synchronization (alternating current)</title>
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		<summary type="html">&lt;p&gt;82.114.187.158: /* Process */&lt;/p&gt;
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&lt;div&gt;{{Infobox enzyme&lt;br /&gt;
| Name = Carbamoyl-phosphate synthetase (glutamine-hydrolysing)&lt;br /&gt;
| EC_number = 6.3.5.5&lt;br /&gt;
| CAS_number = 37233-48-0&lt;br /&gt;
| IUBMB_EC_number = 6/3/5/5&lt;br /&gt;
| GO_code = &lt;br /&gt;
| image = &lt;br /&gt;
| width = &lt;br /&gt;
| caption =&lt;br /&gt;
}}&lt;br /&gt;
{{protein&lt;br /&gt;
|Name=carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase&lt;br /&gt;
|caption=&lt;br /&gt;
|image=&lt;br /&gt;
|width=&lt;br /&gt;
|HGNCid=1424&lt;br /&gt;
|Symbol=CAD&lt;br /&gt;
|AltSymbols=&lt;br /&gt;
|EntrezGene=790&lt;br /&gt;
|OMIM=114010&lt;br /&gt;
|RefSeq=NM_004341&lt;br /&gt;
|UniProt=P27708&lt;br /&gt;
|PDB=&lt;br /&gt;
|ECnumber=&lt;br /&gt;
|Chromosome=2&lt;br /&gt;
|Arm=p&lt;br /&gt;
|Band=21&lt;br /&gt;
|LocusSupplementaryData=&lt;br /&gt;
}}&lt;br /&gt;
&#039;&#039;&#039;Carbamoyl phosphate synthetase II&#039;&#039;&#039; ({{EC number|6.3.5.5}}) is an enzyme that catalyzes the reactions that produce [[carbamoyl phosphate]] in the [[cytosol]] (as opposed to type I, which functions in the [[mitochondria]]). It&#039;s systemic name is &#039;&#039;hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating)&#039;&#039;.&amp;lt;ref&amp;gt;{{cite journal | title = Evidence for an activated form of carbon dioxide in the reaction catalysed by &amp;lt;em&amp;gt;Escherichia coli&amp;lt;/em&amp;gt; carbamyl phosphate synthetase |author = Anderson, P.M. and Meister, A. |journal = Biochemistry |year = 1965 |volume = 4 |pages = 2803–2809 |pmid = 5326356 |issue=12}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Purification and properties of a bacterial carbamyl phosphate synthetase |author = Kalman, S.M., Duffield, P.H. and Brzozowski, T. |journal = J. Biol. Chem. |year = 1966 |volume = 241 |pages = 1871–1877 |pmid = 5329589 |issue=8}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Glutamine-dependent carbamyl phosphate synthetase. Properties and distribution in normal and neoplastic rat tissues |author = Yip, M.C.M. and Knox, W.E. |journal = J. Biol. Chem. |year = 1970 |volume = 245 |pages = 2199–2204 |pmid = 5442268 |issue=9}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase |author = Stapleton, M.A., Javid-Majd, F., Harmon, M.F., Hanks, B.A., Grahmann, J.L., Mullins, L.S. and Raushel, F.M. |journal = Biochemistry |year = 1996 |volume = 35 |pages = 14352–14361 |pmid = 8916922 |doi=10.1021/bi961183y}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Carbamoyl phosphate synthetase: a tunnel runs through it |author = Holden, H.M., Thoden, J.B. and Raushel, F.M. |journal = Curr. Opin. Struct. Biol. |year = 1998 |volume = 8 |pages = 679–685 |pmid = 9914247 |issue=6}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Carbamoyl phosphate synthetase: a crooked path from substrates to products |author = Raushel, F.M., Thoden, J.B., Reinhart, G.D. and Holden, H.M. |journal = Curr. Opin. Chem. Biol. |year = 1998 |volume = 2 |pages = 624–632 |pmid = 9818189 |issue=5}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia |author = Raushel, F.M., Thoden, J.B. and Holden, H.M. |journal = Biochemistry |year = 1999 |volume = 38 |pages = 7891–7899 |pmid = 10387030 |doi=10.1021/bi990871p}}&amp;lt;/ref&amp;gt;&amp;lt;ref&amp;gt;{{cite journal | title = Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia |author = Thoden, J.B., Huang, X., Raushel, F.M. and Holden, H.M. |journal = J. Biol. Chem. |year = 2002 |volume = 277 |pages = 39722–39727 |pmid = 12130656 |doi=10.1074/jbc.M206915200 |issue=42}}&amp;lt;/ref&amp;gt;&lt;br /&gt;
&lt;br /&gt;
In [[pyrimidine]] biosynthesis, it catalyzes the following reaction:&lt;br /&gt;
: 2 ATP + L-[[glutamine]] + HCO&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;&amp;lt;sup&amp;gt;-&amp;lt;/sup&amp;gt; + 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 ADP + [[phosphate]] + L-[[glutamate]] + [[carbamoyl phosphate]] (overall reaction)&lt;br /&gt;
: (1a) L-glutamine + H&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;O &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; L-glutamate + NH&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;&lt;br /&gt;
: (1b) 2 ATP + HCO&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;&amp;lt;sup&amp;gt;-&amp;lt;/sup&amp;gt; + NH&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt; &amp;lt;math&amp;gt;\rightleftharpoons&amp;lt;/math&amp;gt; 2 ADP + phosphate + carbamoyl phosphate&lt;br /&gt;
&lt;br /&gt;
It is activated by [[Adenosine triphosphate|ATP]] and [[PRPP]] and it is inhibited by UMP ([[Uridine monophosphate]], the end product of the pyrimidine synthesis pathway).  &lt;br /&gt;
&lt;br /&gt;
Neither CPSI nor CPSII require [[biotin]] as a coenzyme, as seen with most carboxylation reactions.  &lt;br /&gt;
&lt;br /&gt;
It is one of the three enzyme functions coded by the [[CAD (gene)|CAD]] gene. It is classified under {{EC number|6.3.5.5}}.&lt;br /&gt;
&lt;br /&gt;
== Nomenclature ==&lt;br /&gt;
&lt;br /&gt;
Carbamoyl-phosphate synthase (glutamine-hydrolysing) is also known as:&lt;br /&gt;
* hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating)&lt;br /&gt;
* carbamyl phosphate synthetase (glutamine)&lt;br /&gt;
* glutamine-dependent carbamyl phosphate synthetase&lt;br /&gt;
* [[carbamoyl phosphate synthetase]]&lt;br /&gt;
* CPS&lt;br /&gt;
* carbon-dioxide:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating)&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
{{reflist}}&lt;br /&gt;
&lt;br /&gt;
==External links==&lt;br /&gt;
* {{MeshName|Carbamoyl-Phosphate+Synthase+(Glutamine-Hydrolyzing)}}&lt;br /&gt;
&lt;br /&gt;
{{enzyme-stub}}&lt;br /&gt;
{{Ligases}}&lt;br /&gt;
{{Nucleotide metabolism}}&lt;br /&gt;
{{Multienzyme complexes}}&lt;br /&gt;
&lt;br /&gt;
[[Category:EC 6.3.5]]&lt;/div&gt;</summary>
		<author><name>82.114.187.158</name></author>
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