Document Detail

The multienzyme architecture of eukaryotic fatty acid synthases.
MedLine Citation:
PMID:  18948193     Owner:  NLM     Status:  MEDLINE    
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.
Marc Leibundgut; Timm Maier; Simon Jenni; Nenad Ban
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2008-11-07
Journal Detail:
Title:  Current opinion in structural biology     Volume:  18     ISSN:  1879-033X     ISO Abbreviation:  Curr. Opin. Struct. Biol.     Publication Date:  2008 Dec 
Date Detail:
Created Date:  2008-12-08     Completed Date:  2009-02-17     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9107784     Medline TA:  Curr Opin Struct Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  714-25     Citation Subset:  IM    
Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
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MeSH Terms
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
Reg. No./Substance:
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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