Substrate specificities of two ketosynthases in eukaryotic microalgal and prokaryotic marine bacterial DHA synthases.

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_A and KS_B, which show low similarities to those o

SUBMITTER: Ogata K 

PROVIDER: S-EPMC11962503 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature