ArticleACS chemical biology2018
Biosynthesis of t-Butyl in Apratoxin A: Functional Analysis and Architecture of a PKS Loading Module.
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 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Canalesolide A, a Structurally Unique Polyhydroxy Macrolide from the Marine Cyanobacterium Okeania sp. with Potent Antitrypanosomal Activity.Journal of the American Chemical Society · 2026Article
- Evolution, structure and function of the putative biosynthetic gene cluster of the fungal secondary metabolite myriocin, a potent inhibitory sphingolipid.Communications biology · 2026Article
- Redefining the role of the EryM acetyltransferase in natural product biosynthetic pathways.Structure (London, England : 1993) · 2025Article
- Methylation of ciliary dynein motors involves the essential cytosolic assembly factor DNAAF3/PF22.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Genome-based discovery and total synthesis of janustatins, potent cytotoxins from a plant-associated bacterium.Nature chemistry · 2022Article
- Structural Basis for Control of Methylation Extent in Polyketide Synthase Metal-DependentACS chemical biology · 2022Article
- Cyclic Peptides for the Treatment of Cancers: A Review.Molecules (Basel, Switzerland) · 2022Review
- Mapping the catalytic conformations of an assembly-line polyketide synthase module.Science (New York, N.Y.) · 2021Article
- The Chemistry, Biochemistry and Pharmacology of Marine Natural Products fromMarine drugs · 2020Review
- Antibody Probes of Module 1 of the 6-Deoxyerythronolide B Synthase Reveal an Extended Conformation During Ketoreduction.Journal of the American Chemical Society · 2020Article
- Marine Cyanobacteria: A Source of Lead Compounds and their Clinically-Relevant Molecular Targets.Molecules (Basel, Switzerland) · 2020Review
- Repurposing the GNAT Fold in the Initiation of Polyketide Biosynthesis.Structure (London, England : 1993) · 2020Article
- Nature's Combinatorial Biosynthesis Produces Vatiamides A-F.Angewandte Chemie (International ed. in English) · 2019Article
- Ketoreductase Domain Dysfunction Expands Chemodiversity: Malyngamide Biosynthesis in the Cyanobacterium Okeania hirsuta.ACS chemical biology · 2018Article
- Protein-protein interactions in "cis-AT" polyketide synthases.Natural product reports · 2018Review
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 at 2 institutions in 1 country.
Funding
Abstract
The unusual feature of a t-butyl group is found in several marine-derived natural products including apratoxin A, a Sec61 inhibitor produced by the cyanobacterium Moorea bouillonii PNG 5-198. Here, we determine that the apratoxin A t-butyl group is formed as a pivaloyl acyl carrier protein (ACP) by AprA, the polyketide synthase (PKS) loading module of the apratoxin A biosynthetic pathway. AprA contains an inactive "pseudo" GCN5-related N-acetyltransferase domain (ΨGNAT) flanked by two methyltransferase domains (MT1 and MT2) that differ distinctly in sequence. Structural, biochemical, and precursor incorporation studies reveal that MT2 catalyzes unusually coupled decarboxylation and methylation reactions to transform dimethylmalonyl-ACP, the product of MT1, to pivaloyl-ACP. Further, pivaloyl-ACP synthesis is primed by the fatty acid synthase malonyl acyltransferase (FabD), which compensates for the ΨGNAT and provides the initial acyl-transfer step to form AprA malonyl-ACP. Additionally, images of AprA from negative stain electron microscopy reveal multiple conformations that may facilitate the individual catalytic steps of the multienzyme module.
Indexed as
Identifiers
What OpenQuestion holds
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.