ArticleAngewandte Chemie (Weinheim an der Bergstrasse, Germany)2016
Insights into 6-Methylsalicylic Acid Bio-assembly by Using Chemical Probes.
Article in Angewandte Chemie (Weinheim an der Bergstrasse, Germany), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme.Angewandte Chemie (International ed. in English) · 2021Article
- Nonlinear Biosynthetic Assembly of Alpiniamide by a HybridACS chemical biology · 2020Article
- A Light-Activated Acyl Carrier Protein "Trap" for Intermediate Capture in Type II Iterative Polyketide Biocatalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- A Photoactivatable Small-Molecule Probe for the In Vivo Capture of Polyketide Intermediates.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Insights into 6-Methylsalicylic Acid Bio-assembly by Using Chemical Probes.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Chemical probes capable of reacting with KS (ketosynthase)-bound biosynthetic intermediates were utilized for the investigation of the model type I iterative polyketide synthase 6-methylsalicylic acid synthase (6-MSAS) in vivo and in vitro. From the fermentation of fungal and bacterial 6-MSAS hosts in the presence of chain termination probes, a full range of biosynthetic intermediates was isolated and characterized for the first time. Meanwhile, in vitro studies of recombinant 6-MSA synthases with both nonhydrolyzable and hydrolyzable substrate mimics have provided additional insights into substrate recognition, providing the basis for further exploration of the enzyme catalytic activities.
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Registered trials
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