ArticleJournal of the American Chemical Society2013
Investigation of fungal iterative polyketide synthase functions using partially assembled intermediates.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 29 citations in OpenAlex.
- Synthetic Biology in Natural Product Biosynthesis.Chemical reviews · 2025Review
- Saccharomyces cerevisiae as a tool for mining, studying and engineering fungal polyketide synthases.Fungal genetics and biology : FG & B · 2016Review
- Insights into 6-Methylsalicylic Acid Bio-assembly by Using Chemical Probes.Angewandte Chemie (International ed. in English) · 2016Article
- Insights into 6-Methylsalicylic Acid Bio-assembly by Using Chemical Probes.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2016Article
- Biochemical and Structural Basis for Controlling Chemical Modularity in Fungal Polyketide Biosynthesis.Journal of the American Chemical Society · 2015Article
- A single module type I polyketide synthase directs de novo macrolactone biogenesis during galbonolide biosynthesis in Streptomyces galbus.The Journal of biological chemistry · 2014Article
- Fungal polyketide engineering comes of age.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Iterative polyketide synthases (PKSs) are large, multifunctional enzymes that resemble eukaryotic fatty acid synthases but can make highly functionalized secondary metabolites using complex and unresolved programming rules. During biosynthesis of the kinase inhibitor hypothemycin by Hypomyces subiculosus , a highly reducing iterative PKS, Hpm8, cooperates with a nonreducing iterative PKS, Hpm3, to construct the advanced intermediate dehydrozearalenol (DHZ). The identity of putative intermediates in the formation of the highly reduced hexaketide portion of DHZ were confirmed by incorporation of (13)C-labeled N-acetylcysteamine (SNAC) thioesters using the purified enzymes. The results show that Hpm8 can accept SNAC thioesters of intermediates that are ready for transfer from its acyl carrier protein domain to its ketosynthase domain and assemble them into DHZ in cooperation with Hpm3. Addition of certain structurally modified analogues of intermediates to Hpm8 and Hpm3 can produce DHZ derivatives.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.