Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Zeitschriftenartikel

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

MPG-Autoren
/persons/resource/persons243323

Singh,  K.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons214493

Graf,  B.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons225538

Linden,  A.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons215664

Sautner,  V.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15947

Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons246051

Tittmann,  K.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15857

Stark,  H.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons133053

Chari,  A.
Research Group of Structural Biochemistry and Mechanisms, MPI for Biophysical Chemistry, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

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.


Zitierlink: https://hdl.handle.net/21.11116/0000-0005-DF3E-C
Zusammenfassung
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.