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Atomic structure of the mammalian 'fatty acid factory' determined
Date:9/5/2008

ymes. Now this latest publication describes the atomic structure of the mammalian fatty acid synthase. These results reveal the details of all catalytic active sites responsible for iterative fatty acid synthesis and show how the flexibility of this large multi-enzyme is used for transferring substrates from one enzymatic active site to the next. The structure can be considered a milestone for future research in the field.

Fatty acid synthases as drug targets?

In addition to the fundamental scientific interest in the function of this multi-enzyme that plays a central role in primary metabolism, mammalian fatty acid synthase is also considered a promising drug target. Although most fat accumulated in animals and humans is delivered to cells by ingestion and not by de novo synthesis, compounds that inhibit the function of the mammalian fatty acid synthase induce weight reduction in animals, showing potential for the treatment of obesity and obesity-related diseases, such as diabetes and coronary disorders. Furthermore, due to the increased requirement for fatty acid synthesis in cancer cells, inhibitors of this enzyme have anti-tumor activity, making fatty acid synthase an attractive drug target for anti-cancer therapy.

Multi-enzymes: the ultimate organic chemists

Mammalian fatty acid synthase belongs to a large family of multi-enzymes, some of which are responsible for the synthesis of complex natural products with antibiotic, anti-cancer, anti-fungal and immunosuppressive properties that are of outstanding medical relevance. The structure of mammalian fatty acid synthase reveals how different catalytic domains are excised or inserted in various members of this family to yield multi-enzymes capable of synthesizing a large variety of chemical products. The structure will facilitate the design of molecular assembly lines for the production of improved compounds. In particular, the engineering of novel multi-enzymes for
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Contact: Professor Nenad Ban
nenad.ban@mol.biol.ethz.ch
41-446-332-785
ETH Zurich/Swiss Federal Institute of Technology
Source:Eurekalert

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