This article investigates the structural dynamics of fatty acid synthase (FASN) in humans, focusing on its multi-domain architecture crucial for fatty acid synthesis. By employing single particle cryogenic electron microscopy on endogenous FASN in HEK293 cells, the researchers captured conformational changes throughout the condensation cycle of fatty acid production. Findings indicate that the two monomers in the FASN dimer operate in an unsynchronized manner, shaping a new understanding of FASN's catalytic mechanisms. This study provides valuable insights into the biochemical pathways relevant to lipid metabolism.
In our study on human FASN, we reveal that its function does not require large rotational motion, highlighting the unsynchronized nature of catalytic reactions during fatty acid synthesis.
By characterizing the structural dynamics of FASN, we provide new insights into how this enzyme catalyzes reactions essential for de novo fatty acid synthesis.
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