PROSITE documentation PDOC01017Octanoyl-[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.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Morris T.W. Reed K.E. Cronan J.E. Jr. |
Title | Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein. | |
Source | J. Bacteriol. 177:1-10(1995). | |
PubMed ID | 8002607 |
2 | Authors | Zhao X. Miller J.R. Cronan J.E. |
Title | The reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate. | |
Source | Biochemistry 44:16737-16746(2005). | |
PubMed ID | 16342964 | |
DOI | 10.1021/bi051865y |
3 | Authors | Christensen Q.H. Cronan J.E. |
Title | Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases. | |
Source | Biochemistry 49:10024-10036(2010). | |
PubMed ID | 20882995 | |
DOI | 10.1021/bi101215f |
4 | Authors | Chen X.J. |
Title | Cloning 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. | |
Source | Mol. Gen. Genet. 255:341-349(1997). | |
PubMed ID | 9268025 |
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