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  Discovery of a regulatory subunit of the yeast fatty acid synthase.

Singh, K., Graf, B., Linden, A., Sautner, V., Urlaub, H., Tittmann, K., et al. (2020). Discovery of a regulatory subunit of the yeast fatty acid synthase. Cell, 180(6), 1130-1143.e20. doi:10.1016/j.cell.2020.02.034.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-DF3E-C Version Permalink: http://hdl.handle.net/21.11116/0000-0006-A0D8-1
Genre: Journal Article

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 Creators:
Singh, K.1, Author              
Graf, B.1, Author              
Linden, A.2, Author              
Sautner, V.1, Author              
Urlaub, H.2, Author              
Tittmann, K.1, Author              
Stark, H.1, Author              
Chari, A.1, Author              
Affiliations:
1Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              
2Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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Free keywords: FAS; FAS engineering; Tma17p; biotechnology; cryo-EM; energy landscape; enzyme kinetics; fatty acid synthase; inhibitor design; x-ray crystallography; γ subunit
 Abstract: Fatty acid synthases (FASs) are central to metabolism but are also of biotechnological interest for the production of fine chemicals and biofuels from renewable resources. During fatty acid synthesis, the growing fatty acid chain is thought to be shuttled by the dynamic acyl carrier protein domain to several enzyme active sites. Here, we report the discovery of a γ subunit of the 2.6 megadalton α6-β6S. cerevisiae FAS, which is shown by high-resolution structures to stabilize a rotated FAS conformation and rearrange ACP domains from equatorial to axial positions. The γ subunit spans the length of the FAS inner cavity, impeding reductase activities of FAS, regulating NADPH turnover by kinetic hysteresis at the ketoreductase, and suppressing off-pathway reactions at the enoylreductase. The γ subunit delineates the functional compartment within FAS. As a scaffold, it may be exploited to incorporate natural and designed enzymatic activities that are not present in natural FAS.

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Language(s): eng - English
 Dates: 2020-04-022020-03-042020-03-19
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.cell.2020.02.034
 Degree: -

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Title: Cell
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 180 (6) Sequence Number: - Start / End Page: 1130 - 1143.e20 Identifier: -