Polyketide Synthase EcPKS1
Ontology highlight
ABSTRACT:
SUBMITTER: Heidi Linda Schubert
PROVIDER: EMPIAR-12315 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
The structure of full-length AFPK supports the ACP linker in a role that regulates iterative polyketide and fatty acid assembly.
Schubert Heidi L HL Li Feng F Hill Christopher P CP Schmidt Eric W EW
Proceedings of the National Academy of Sciences of the United States of America 20250206 6
The polyketide synthases (PKSs) in microbes and the cytoplasmic fatty acid synthases in humans (FASs) are related enzymes that have been well studied. As a result, there is a paradigm explaining in general terms how FASs repeatedly use a set of enzymatic domains to produce simple fats, while PKSs use the domains in a much more complex manner to produce pharmaceuticals and other elaborate molecules. However, most animals also have PKSs that do not conform to the rules described in microbes, inclu ...[more]
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