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Structure and function of eukaryotic fatty acid synthases

Maier, T. and Leibundgut, M. and Boehringer, D. and Ban, N.. (2010) Structure and function of eukaryotic fatty acid synthases. Quarterly Reviews of Biophysics, 43 (3). pp. 373-422.

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Official URL: http://edoc.unibas.ch/45842/

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Abstract

In all organisms, fatty acid synthesis is achieved in variations of a common cyclic reaction pathway by stepwise, iterative elongation of precursors with two-carbon extender units. In bacteria, all individual reaction steps are carried out by monofunctional dissociated enzymes, whereas in eukaryotes the fatty acid synthases (FASs) have evolved into large multifunctional enzymes that integrate the whole process of fatty acid synthesis. During the last few years, important advances in understanding the structural and functional organization of eukaryotic FASs have been made through a combination of biochemical, electron microscopic and X-ray crystallographic approaches. They have revealed the strikingly different architectures of the two distinct types of eukaryotic FASs, the fungal and the animal enzyme system. Fungal FAS is a 2.6 MDa alphabeta heterododecamer with a barrel shape enclosing two large chambers, each containing three sets of active sites separated by a central wheel-like structure. It represents a highly specialized micro-compartment strictly optimized for the production of saturated fatty acids. In contrast, the animal FAS is a 540 kDa X-shaped homodimer with two lateral reaction clefts characterized by a modular domain architecture and large extent of conformational flexibility that appears to contribute to catalytic efficiency.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Cambridge University Press
ISSN:0033-5835
e-ISSN:1469-8994
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:29 Nov 2017 11:09
Deposited On:29 Nov 2017 11:09

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