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<p><b>New page</b></p><div>{{enzyme<br />
| Name = long-chain-fatty-acid-luciferin-component ligase<br />
| EC_number = 6.2.1.19<br />
| CAS_number = 82657-98-5<br />
| IUBMB_EC_number = 6/2/1/19<br />
| GO_code = 0047474<br />
| image = <br />
| width = <br />
| caption = <br />
}}<br />
In [[enzymology]], a '''long-chain-fatty-acid-luciferin-component ligase''' ({{EC number|6.2.1.19}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]<br />
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:ATP + an acid + protein <math>\rightleftharpoons</math> AMP + diphosphate + an acyl-protein thioester<br />
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The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]], [[acid]], and [[protein]], whereas its 3 [[product (chemistry)|products]] are [[adenosine monophosphate|AMP]], [[diphosphate]], and [[acyl-protein thioester]].<br />
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This enzyme belongs to the family of [[ligase]]s, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is '''long-chain-fatty-acid:protein ligase (AMP-forming)'''. This enzyme is also called '''acyl-protein synthetase'''.<br />
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==References==<br />
{{reflist|1}}<br />
* {{cite journal | author = Riendeau D, Rodriguez A, Meighen E | year = 1982 | title = Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex | journal = J. Biol. Chem. | volume = 257 | pages = 6908&ndash;15 | pmid = 7085612 | issue = 12 }}<br />
* {{cite journal | author = Wall L and Meighen EA | year = 1986 | title = Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum | journal = Biochemistry | volume = 25 | pages = 4315&ndash;4321 | doi = 10.1021/bi00363a021 }}<br />
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{{DEFAULTSORT:Long-chain-fatty-acid-luciferin-component ligase}}<br />
[[Category:EC 6.2.1]]<br />
[[Category:Enzymes of unknown structure]]<br />
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{{ligase-stub}}</div>en>Citation bot 1