EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.20 | Mg2+ | required for activity | Actinoplanes friuliensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.20 | ATP + a long-chain fatty acid + an [acyl-carrier protein] | Actinoplanes friuliensis | - |
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein] | - |
? | |
6.2.1.20 | ATP + a long-chain fatty acid + LipD | Actinoplanes friuliensis | - |
AMP + diphosphate + a long-chain acyl-LipD | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.2.1.20 | Actinoplanes friuliensis | Q7X541 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.20 | ATP + a long-chain fatty acid + an [acyl-carrier protein] | - |
Actinoplanes friuliensis | AMP + diphosphate + a long-chain acyl-[acyl-carrier protein] | - |
? | |
6.2.1.20 | ATP + a long-chain fatty acid + LipD | - |
Actinoplanes friuliensis | AMP + diphosphate + a long-chain acyl-LipD | - |
? | |
6.2.1.20 | ATP + a long-chain fatty acid + LipD | LipD structure analysis and comparisons, overview | Actinoplanes friuliensis | AMP + diphosphate + a long-chain acyl-LipD | - |
? | |
6.2.1.20 | additional information | different surface charges of acyl-carrier protein derivatives LipD and FAS-ACP from Actinoplanes friuliensis allow the acyl-CoA ligase to interact preferentially with the LipD instead of binding to the FAS-ACP, overview | Actinoplanes friuliensis | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.2.1.20 | Acyl-CoA ligase | - |
Actinoplanes friuliensis |
6.2.1.20 | Acyl-CoA synthetase | - |
Actinoplanes friuliensis |
6.2.1.20 | LipA | - |
Actinoplanes friuliensis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.20 | ATP | - |
Actinoplanes friuliensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.2.1.20 | metabolism | friulimicin is a cyclic lipodecapeptide antibiotic that is produced by Actinoplanes friuliensis. Similar to the related lipopeptide drug daptomycin, the peptide skeleton of friulimicin is synthesized by a large multienzyme nonribosomal peptide synthetase (NRPS) system. The LipD protein plays a major role in the acylation reaction of friulimicin. The attachment of the fatty acid group promotes its antibiotic activity. Phylogenetic analysis reveals that LipD is most closely related to other freestanding acyl carrier proteins (ACPs), for which the genes are located near to NRPS gene clusters | Actinoplanes friuliensis |
6.2.1.20 | physiological function | LipA seems to be involved in the initiation of the acylation reaction during the synthesis of lipopeptide antibiotics through the nonribosomal peptide synthetase (NRPS) system. The activation of the fatty acid is carried out by a two-step catalysis reaction in the presence of ATP and Mg2+ | Actinoplanes friuliensis |