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Publication in ACS Chemical Biology:The Relationship between Substrate Structure and Selectivity of Ketoreduction in Multimodular Polyketide Synthases: A Comparative Study of A‑Type Ketoreductases from Late Modules Using Complex Precursor Analogues
08.01.2025
A part of Lisa's PhD thesis was just published in ACS Chemical Biology
We present studies on the three KR domains FosKR7, PlmKR6, and EryKR6 from the biosynthetic pathways of
fostriecin, phoslactomycin, and erythromycin by in vitro assays using close surrogates of the octaketidic FosKR7 biosynthetic precursor, complex derivatives and a diketide in the form of their biomimetic N-acetylcysteamine thioesters.
These results reinforce the importance of the substrate-dependent stereoselectivity of KR domains in PKSs and suggest more detailed experimental and structural studies with isolated KRs and full PKS modules that could ultimately lead to improved results in PKS engineering.
Congratulations to Lisa and all other contributors!