کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2048023 | 1074053 | 2012 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Exploring the mechanism of lipid transfer during biosynthesis of the acidic lipopeptide antibiotic CDA Exploring the mechanism of lipid transfer during biosynthesis of the acidic lipopeptide antibiotic CDA](/preview/png/2048023.png)
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.
Journal: FEBS Letters - Volume 586, Issue 3, 3 February 2012, Pages 283–288