View source for Long-chain-fatty-acid—luciferin-component ligase

{{infobox enzyme
| Name       = Long-chain-fatty-acid—luciferin-component ligase
| EC_number  = 6.2.1.19
| CAS_number = 82657-98-5
| GO_code    = 0047474
| image      =
| width      = 
| caption    =  
}}
In [[enzymology]], a '''long-chain-fatty-acid—luciferin-component ligase''' ({{EnzExplorer|6.2.1.19}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:ATP + an acid + protein <math>\rightleftharpoons</math> AMP + diphosphate + an acyl-protein thioester

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]].

This enzyme belongs to the family of [[ligase]]s, specifically those forming carbon-sulfur bonds as acid-thiol ligases.  The [[List of enzymes|systematic name]] of this enzyme class is '''long-chain-fatty-acid:protein ligase (AMP-forming)'''. This enzyme is also called '''acyl-protein synthetase'''.

==References==
{{reflist|1}}
* {{cite journal | vauthors = 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 | doi = 10.1016/S0021-9258(18)34515-0 | doi-access = free }}
* {{cite journal |author1 = Wall L |author2 =Meighen EA | year = 1986 | title = Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum | journal = Biochemistry  | volume = 25 |issue =15 | pages = 4315&ndash;4321 | doi = 10.1021/bi00363a021 }}

{{Ligases CO CS and CN}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}

{{DEFAULTSORT:Long-chain-fatty-acid-luciferin-component ligase}}
[[Category:EC 6.2.1]]
[[Category:Enzymes of unknown structure]]


{{ligase-stub}}