| 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. | Name | Lipoyltransferase/lipoate-protein ligase |
| Short Name | LipoylTrfase_LipoateP_Ligase | Type | Family |
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