| Functional dissection of surfactin synthetase initiation module reveals insights into the mechanism of lipoinitiation. | |
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MedLine Citation:
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PMID: 20797616 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Although the N-terminally attached fatty acids are key structural elements of nonribosomally assembled lipopeptide antibiotics, little is known about the mechanism of lipid transfer during the initial step of biosynthesis. In this study, we investigated the activity of the dissected initiation module (C-A(Glu)-PCP) of surfactin synthetase SrfAA in vitro to gain further insights into the lipoinitiation reaction. The dissected condensation (C) domain catalyzes the transfer of CoA-activated 3-hydroxy fatty acid with high substrate specificity at its donor site to the peptidyl carrier protein (PCP) bound amino acid glutamate (Glu(1)). Additionally, biochemical studies on four putative acyl CoA ligases in Bacillus subtilis revealed that two of them activate 3-hydroxy fatty acids for surfactin biosynthesis in vitro and that the disruption of corresponding genes has a significant influence on surfactin production. |
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Authors:
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Femke I Kraas; Verena Helmetag; Melanie Wittmann; Matthias Strieker; Mohamed A Marahiel |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Chemistry & biology Volume: 17 ISSN: 1879-1301 ISO Abbreviation: Chem. Biol. Publication Date: 2010 Aug |
Date Detail:
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Created Date: 2010-08-27 Completed Date: 2011-01-18 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9500160 Medline TA: Chem Biol Country: United States |
Other Details:
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Languages: eng Pagination: 872-80 Citation Subset: IM |
Copyright Information:
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Copyright (c) 2010 Elsevier Ltd. All rights reserved. |
Affiliation:
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Department of Chemistry, Biochemistry, Philipps-University Marburg, Hans-Meerwein-Strasse, D-35032 Marburg, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Anti-Bacterial Agents
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biosynthesis* Bacillus subtilis / enzymology Bacterial Proteins / chemistry, metabolism* Biocatalysis Coenzyme A Ligases / metabolism Lipopeptides / biosynthesis* Myristic Acids / metabolism Peptide Synthases / chemistry, metabolism* Protein Structure, Tertiary |
| Chemical | |
Reg. No./Substance:
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0/Anti-Bacterial Agents; 0/Bacterial Proteins; 0/Lipopeptides; 0/Myristic Acids; 1961-72-4/beta-hydroxymyristic acid; EC 6.2.1.-/Coenzyme A Ligases; EC 6.3.2.-/Peptide Synthases; EC 6.3.2.-/surfactin synthetase |
| Comments/Corrections | |
Comment In:
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Chem Biol. 2010 Aug 27;17(8):791-3
[PMID:
20797606
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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