ArticleProceedings of the National Academy of Sciences of the United States of America2025
Substrate specificities of two ketosynthases in eukaryotic microalgal and prokaryotic marine bacterial DHA synthases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Thraustochytrid PUFA synthase ER domains form a stable heterodimer.Journal of structural biology: X · 2026Article
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10 authors.
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Abstract
Highly reducing iterative polyketide synthases (HR-iPKSs) are huge enzyme complexes with multiple catalytic domains that biosynthesize polyketides by intrinsically programmed iterative carbon chain extensions and reductions. Unlike most HR-iPKSs, which possess a single ketosynthase (KS) domain for all carbon chain elongations, polyunsaturated fatty acid (PUFA) synthases contain two KS domains. We previously examined the substrate specificities of two KS domains of prokaryotic marine PUFA synthases with several acyl-ACP intermediates and showed that the two KS domains are utilized differentially depending on the carbon chain length. In this study, we investigated two KS domains in a eukaryotic microalgal DHA synthase, KS
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