ArticleOrganic letters2017
MarH, a Bifunctional Enzyme Involved in the Condensation and Hydroxylation Steps of the Marineosin Biosynthetic Pathway.
Article in Organic letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Optimization of Prodiginines as Single-Dose Curative Antimalarials.Journal of medicinal chemistry · 2025Article
- Optimization of B-Ring-Functionalized Antimalarial Tambjamines and Prodiginines.Journal of medicinal chemistry · 2024Article
- Discovery and Optimization of Tambjamines as a Novel Class of Antileishmanial Agents.Journal of medicinal chemistry · 2024Article
- Marine Pyrrole Alkaloids.Marine drugs · 2021Review
- Total Synthesis and Antimalarial Activity of 2-(Journal of medicinal chemistry · 2021Article
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3 authors.
Funding
Abstract
A novel bifunctional enzyme, MarH, has been identified, and its key functional role in the marineosin biosynthesis successfully probed. MarH catalyzes (1) a condensation step between 4-methoxy-2,2'-bipyrrole-5-carboxaldehyde (MBC) and 2-undecylpyrrole (UP) to form undecylprodiginine (UPG) and (2) hydroxylation of the alkyl chain of UPG to form the (S)-23-hydroxyundecylprodiginine (HUPG), which is essential for MarG catalyzed bicyclization toward the formation of an unusual spiro-tetrahydropyran-aminal ring of marineosins. The final enigmatic steps in the marineosin biosynthesis have now been deciphered.
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