| The multienzyme architecture of eukaryotic fatty acid synthases. | |
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MedLine Citation:
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PMID: 18948193 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Eukaryotic fatty acid synthases (FASs) are huge multifunctional enzymes that carry out all enzymatic steps essential for fatty acid biosynthesis. Recent crystallographic studies provide new insights into the architecture of the two distinct eukaryotic FAS systems, the 2.6 MDa heterododecameric fungal and the 540 kDa dimeric animal FAS. In this review, we compare the fundamentally different organization of these two megasynthases and discuss the structural principles of enzyme integration and substrate shuttling in FAS multienzymes. |
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Authors:
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Marc Leibundgut; Timm Maier; Simon Jenni; Nenad Ban |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review Date: 2008-11-07 |
Journal Detail:
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Title: Current opinion in structural biology Volume: 18 ISSN: 1879-033X ISO Abbreviation: Curr. Opin. Struct. Biol. Publication Date: 2008 Dec |
Date Detail:
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Created Date: 2008-12-08 Completed Date: 2009-02-17 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 9107784 Medline TA: Curr Opin Struct Biol Country: England |
Other Details:
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Languages: eng Pagination: 714-25 Citation Subset: IM |
Affiliation:
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Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Eukaryotic Cells / enzymology* Evolution, Molecular Fatty Acid Desaturases / chemistry Fatty Acid Synthetase Complex / chemistry*, genetics Fungal Proteins / chemistry*, genetics Hydro-Lyases / chemistry Molecular Structure Pantetheine / analogs & derivatives, metabolism Protein Structure, Tertiary Substrate Specificity Transferases / chemistry |
| Chemical | |
Reg. No./Substance:
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0/Fungal Proteins; 2226-71-3/4'-phosphopantetheine; 496-65-1/Pantetheine; EC 1.14.19.-/Fatty Acid Desaturases; EC 2.-/Transferases; EC 4.2.1.-/Hydro-Lyases; EC 6.-/Fatty Acid Synthetase Complex |
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