ArticleACS chemical biology2018
Ketoreductase Domain Dysfunction Expands Chemodiversity: Malyngamide Biosynthesis in the Cyanobacterium Okeania hirsuta.
Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
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- Discovery of Cyanobacterial Natural Products Containing Fatty Acid Residues*.Angewandte Chemie (International ed. in English) · 2021Article
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- A Multi-Omics Characterization of the Natural Product Potential of Tropical Filamentous Marine Cyanobacteria.Marine drugs · 2021Article
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- Loss of Single-Domain Function in a Modular Assembly Line Alters the Size and Shape of a Complex Polyketide.Angewandte Chemie (International ed. in English) · 2019Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Dozens of type A malyngamides, principally identified by a decorated six-membered cyclohexanone headgroup and methoxylated lyngbic acid tail, have been isolated over several decades. Their environmental sources include macro- and microbiotic organisms, including sea hares, red alga, and cyanobacterial assemblages, but the true producing organism has remained enigmatic. Many type A analogues display potent bioactivity in human-health related assays, spurring an interest in this molecular class and its biosynthetic pathway. Here, we present the discovery of the type A malyngamide biosynthetic pathway in the first sequenced genome of the cyanobacterial genus Okeania. Bioinformatic analysis of two cultured Okeania genome assemblies identified 62 and 68 kb polyketide synthase/nonribosomal peptide synthetase (PKS/NRPS) pathways with unusual loading and termination genes. NMR data of malyngamide C acetate derived from
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