Document Detail

Exploring the mechanism of lipid transfer during biosynthesis of the acidic lipopeptide antibiotic CDA.
MedLine Citation:
PMID:  22245678     Owner:  NLM     Status:  Publisher    
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.
Femke I Kraas; Tobias W Giessen; Mohamed A Marahiel
Related Documents :
18646828 - Design of a coumarin-based triketone as a fluorescent protecting group for primary amines.
18846198 - Segment coupling to a highly hindered n-terminal, alamethicin-related alpha-aminoisobut...
11672198 - Rigid dipeptide mimics: synthesis of enantiopure 5- and 7-benzyl and 5,7-dibenzyl indol...
21571528 - Ability to use the diazo dye, c.i. acid black 1 as a nitrogen source by the marine cyan...
11678438 - Quality attributes of three new improved lines of nigerian lima beans (phaseolus lunatu...
16782068 - Palmitic acid-induced activation of human t-lymphocytes and aortic endothelial cells wi...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-1-10
Journal Detail:
Title:  FEBS letters     Volume:  -     ISSN:  1873-3468     ISO Abbreviation:  -     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2012-1-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier B.V.
Department of Chemistry/Biochemistry, Philipps-University Marburg, Hans-Meerwein-Strasse, D-35032 Marburg, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Identification and characterization of an LCAT-like Arabidopsis thaliana gene encoding a novel phosp...
Next Document:  Anti-diabetic and anti-obesity agent sodium tungstate enhances GCN pathway activation through Glc7p ...