Desaturation of the Sphingofungin Polyketide Tail Results in Increased Serine Palmitoyltransferase Inhibition-Reference-Cited by-同舟云学术

Desaturation of the Sphingofungin Polyketide Tail Results in Increased Serine Palmitoyltransferase Inhibition

Published:2022-10-26 Issue:5 Volume:10 Page:
ISSN:2165-0497
Container-title:Microbiology Spectrum
language:en
Short-container-title:Microbiol Spectr

Author:

Hoefgen Sandra¹,Bissell Alexander U.¹²,Huang Ying¹²,Gherlone Fabio¹²,Raguž Luka³⁴,Beemelmanns Christine³,Valiante Vito¹^ORCID

Affiliation:

1. Biobricks of Microbial Natural Product Syntheses, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute (HKI), Jena, Germany

2. Faculty of Biological Sciences, Friedrich Schiller University Jena, Jena, Germany

3. Chemical Biology of Microbe-Host Interactions, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute (HKI), Jena, Germany

4. Faculty of Chemistry and Earth Sciences, Friedrich Schiller University Jena, Jena, Germany

Abstract

Targeting the cellular sphingolipid metabolism is often discussed as a potential approach to treat associated human diseases such as cancer and Alzheimer's disease. Alternatively, it is also a possible target for the development of antifungal compounds, which are direly needed.

Funder

Deutsche Forschungsgemeinschaft

EC | EU Social | European Social Fund

EC | European Research Council

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Cell Biology,Microbiology (medical),Genetics,General Immunology and Microbiology,Ecology,Physiology

Link

https://journals.asm.org/doi/pdf/10.1128/spectrum.01331-22

Reference34 articles.

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2. Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities

3. Structural, mechanistic and regulatory studies of serine palmitoyltransferase

4. Use of isotopically labeled substrates reveals kinetic differences between human and bacterial serine palmitoyltransferase

5. Sphingolipids and their metabolism in physiology and disease

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