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{{enzyme
| Name = Lipoyl(octanoyl) transferase
| EC_number = 2.3.1.181
| CAS_number = 
| IUBMB_EC_number = 2/3/1/181
| GO_code = 
| image = 
| width = 
| caption = 
}}

In [[enzymology]], a '''lipoyl(octanoyl) transferase''' ({{EC number|2.3.1.181}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:octanoyl-[acyl-carrier-protein] + protein <math>\rightleftharpoons</math> protein N<sup>6</sup>-(octanoyl)lysine + acyl carrier protein

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are octanoyl-[acyl-carrier-protein] and [[protein]], whereas its two [[product (chemistry)|products]] are [[protein N6-(octanoyl)lysine]] and [[acyl carrier protein]].

This enzyme belongs to the family of [[transferase]]s, specifically those [[acyltransferase]]s transferring groups other than aminoacyl groups.  The systematic name of this enzyme class is '''octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase'''. Other names in common use include '''LipB''', '''lipoyl (octanoyl)-[acyl-carrier-protein]-protein''', '''N-lipoyltransferase''', '''lipoyl (octanoyl)-acyl carrier protein:protein transferase''', '''lipoate/octanoate transferase''', '''lipoyltransferase''', '''octanoyl-[acyl carrier protein]-protein N-octanoyltransferase''', and '''lipoyl(octanoyl)transferase'''.  This enzyme participates in [[lipoic acid]] metabolism.  

==References==
{{reflist|1}}
* {{cite journal | author = Broadwater JA, Haas JA, Fox BG, Booker SJ | date = 2005 | title = Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase | journal = Protein. Expr. Purif.  | volume = 39 | pages = 269&ndash;82  | pmid = 15642479 | issue = 2 | doi = 10.1016/j.pep.2004.10.021 }}
* {{cite journal | author = Vanden Boom TJ, Reed KE, Cronan JE Jr | date = 1991 | title = Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system | journal = J. Bacteriol.  | volume = 173 | pages = 6411&ndash;20  | pmid = 1655709 | issue = 20 | pmc = 208974 }}
* {{cite journal | author = Jordan SW, Cronan JE Jr | date = 1997 | title = A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria | journal = J. Biol. Chem.  | volume = 272 | pages = 17903&ndash;6  | pmid = 9218413 | doi = 10.1074/jbc.272.29.17903 | issue = 29 }}
* {{cite journal | author = Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE | date = 2003 | title = Assembly of the covalent linkage between lipoic acid and its cognate enzymes | journal = Chem. Biol.  | volume = 10 | pages = 1293&ndash;302  | pmid = 14700636 | doi = 10.1016/j.chembiol.2003.11.016 | issue = 12 }}
* {{cite journal | author = Wada M, Yasuno R, Jordan SW, Cronan JE Jr, Wada H | date = 2001 | title = Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase | journal = Plant. Cell. Physiol.  | volume = 42 | pages = 650&ndash;6  | pmid = 11427685 | doi = 10.1093/pcp/pce081 | issue = 6 }}
* {{cite journal | author = Perham RN | date = 2000 | title = Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions | journal = Annu. Rev. Biochem.  | volume = 69 | pages = 961&ndash;1004  | pmid = 10966480 | doi = 10.1146/annurev.biochem.69.1.961 }}

{{transferase-stub}}

[[Category:EC 2.3.1]]
[[Category:Enzymes of unknown structure]]