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Literature summary extracted from

  • Paul, S.; Ishida, H.; Nguyen, L.T.; Liu, Z.; Vogel, H.J.
    Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics (2017), Protein Sci., 26, 946-959 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.20 Mg2+ required for activity Actinoplanes friuliensis

Natural Substrates/ Products (Substrates)

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
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 AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
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 ?
6.2.1.20 ATP + a long-chain fatty acid + LipD Actinoplanes friuliensis
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 AMP + diphosphate + a long-chain acyl-LipD
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 ?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.20 Actinoplanes friuliensis Q7X541
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-

Substrates and Products (Substrate)

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]
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 Actinoplanes friuliensis AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
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 ?
6.2.1.20 ATP + a long-chain fatty acid + LipD
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 Actinoplanes friuliensis AMP + diphosphate + a long-chain acyl-LipD
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 ?
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
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 ?
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 ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
6.2.1.20 Acyl-CoA ligase
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 Actinoplanes friuliensis
6.2.1.20 Acyl-CoA synthetase
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 Actinoplanes friuliensis
6.2.1.20 LipA
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 Actinoplanes friuliensis

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.20 ATP
-
 Actinoplanes friuliensis

General Information

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