PROSITE documentation PDOC51733
Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) catalytic domain profile


Biotin and lipoic acid are the covalently bound cofactors of various multicomponent enzyme complexes that catalyze key metabolic reactions. In these enzymes complexes, biotin and lipoic acid are attached via amide linkage through their carboxyl group and the epsilon-amino group of a specific lysine residue of a protein module known respectively as the biotinyl and the lipoyl domain (see <PDOC50968>). Covalent attachment of biotin and lipoic acid to these enzyme complexes occurs post-translationally, and it is mediated by biotinylating and lipoylating protein enzymes, which specifically recognize the biotinyl and lipoyl domains, ensuring their correct post-translational modification. Lipoylating and biotinylating enzymes are evolutionarily related protein families containing a homologous catalytic module [1].

Amino acid sequence conservation between the catalytic modules of biotinyl protein ligases (BPLs) and lipoyl protein ligases (LPLs) is very low, and mainly affects residues that are important for the scaffold of the structure, such as those contributing to the hydrophobic core. Despite the poor overall sequence similarity, a single lysine residue is strictly conserved in all LPL and BPL sequences. This lysine residue is likely to bind specifically to the carbonyl oxygen of the carboxyl group of biotin or at the end of the hydrogen-carbon tail of the lipoyl moiety [1]. The BPL/LPL catalytic domain contains a seven-stranded mixed β-sheet on one side and four α-helices on the other side (see <PDB:1WQ7>) [2].

The profile we developed covers the entire BPL/LPL catalytic domain.

Last update:

September 2014 / First entry.


Technical section

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

BPL_LPL_CATALYTIC, PS51733; Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) catalytic domain profile  (MATRIX)


1AuthorsReche P.A.
TitleLipoylating and biotinylating enzymes contain a homologous catalytic module.
SourceProtein Sci. 9:1922-1929(2000).
PubMed ID11106165

2AuthorsBagautdinov B. Kuroishi C. Sugahara M. Kunishima N.
TitleCrystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: structural basis of biotin activation.
SourceJ. Mol. Biol. 353:322-333(2005).
PubMed ID16169557

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