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PROSITE documentation PDOC01017
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase (lipB) signature


Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase [1,2,3] (gene lipB) is the bacterial enzyme that creates an amide linkage that joins the free carboxyl group of octanoyl acid to the epsilon-amino group of a specific lysine residue in lipoyl domains (see <PDOC50968>).

Such an enzyme has also be found in fungi [4], where it is located in the mitochondria. It also seems to exist in plants and is encoded in the chloroplast genome of the red alga Cyanidium caldarium.

As a signature for lipB, we selected the most conserved region, located in the central part of the enzyme. This region contains one of two conserved histidines.

Last update:

September 2011 / Text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

LIPB, PS01313; Lipoate-protein ligase B signature  (PATTERN)


1AuthorsMorris T.W. Reed K.E. Cronan J.E. Jr.
TitleLipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein.
SourceJ. Bacteriol. 177:1-10(1995).
PubMed ID8002607

2AuthorsZhao X. Miller J.R. Cronan J.E.
TitleThe reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate.
SourceBiochemistry 44:16737-16746(2005).
PubMed ID16342964

3AuthorsChristensen Q.H. Cronan J.E.
TitleLipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases.
SourceBiochemistry 49:10024-10036(2010).
PubMed ID20882995

4AuthorsChen X.J.
TitleCloning and characterization of the lipoyl-protein ligase gene LIPB from the yeast Kluyveromyces lactis: synergistic respiratory deficiency due to mutations in LIPB and mitochondrial F1-ATPase subunits.
SourceMol. Gen. Genet. 255:341-349(1997).
PubMed ID9268025

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