| Primary Identifier | IPR040097 | Type | Family |
| Short Name | FAAL/FAAC |
| description | Fatty acyl-AMP ligase (FAAL) belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin [, ].FAAL sequences are also found at the N terminus of non-ribosomal peptide synthetases, large modular enzymes that catalyse synthesis of important peptide products []. |
