| Primary Identifier | IPR004562 | Type | Family |
| Short Name | LipoylTrfase_LipoateP_Ligase |
| description | Lipoic acid is an essential cofactor of the alpha-ketoacid dehydrogenase complexes and the glycine cleavage system. It is covalently attached to a specific lysine residue of the subunit of the complexes.In mammals, covalent attachment of lipoic acid to the proteins occurs in two successive reactions. First, lipoic acid is activated to lipoyl-AMP by lipoate-activating enzyme, and then the lipoyl moiety is transferred to apoproteins by the action of lipoyltransferase [, ]. In contrast, in Escherichia coli, lipoate-protein ligase A catalyses both the activation and the transfer of lipoate []. This entry includes lipoyltransferases and lipoate-protein ligases. |
