| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2048023 | FEBS Letters | 2012 | 6 Pages |
The non-ribosomally synthesized lipodepsipeptide CDA belongs to the group of acidic lipopeptide antibiotics, whose members feature a fatty acid side chain that strongly affects their antimicrobial activity. This study elucidates the N-acylation of the N-terminal serine in the CDA peptide chain. This reaction is referred to as lipoinitiation and is shown to be catalyzed by the dissected starter C domain found at the N-terminus of Cda-PSI. The recombinantly produced C domain specifically interacts with 2,3-epoxyhexanoyl-S-ACP and catalyzes the transfer of the fatty acid moiety onto the amino group of PCP-bound serine with high selectivity for both carrier protein bound substrates at the donor and acceptor site.
► Starter C domain of non-ribosomal peptide synthetases. ► Lipoinitiation reaction of CDA. ► Substrate specificity of the starter C domain Cda-C1. ► In vitro studies of N-acylation of PCP-bound serine.
