Evidence map›Paper›PMID 30300504›Full record

ArticleThe FEBS journal2018

Biochemical characterization of the minimal domains of an iterative eukaryotic polyketide synthase.

Martin Sabatini, Santiago Comba, Silvia Altabe, Alejandro I Recio-Balsells, Guillermo R Labadie, Eriko Takano, Hugo Gramajo, Ana Arabolaza

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. An endosymbiotic origin of the crimson pigment from the lac insect.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Genome Mining ofMicroorganisms · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Genomic Analysis of theMycobiology · 2023
    Article
  13. The mud-dwelling clamProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. The biosynthetic diversity of the animal world.The Journal of biological chemistry · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Martin SabatiniFacultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Universidad Nacional de Rosario, Argentina.
Santiago CombaFacultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Universidad Nacional de Rosario, Argentina.
Silvia AltabeFacultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Universidad Nacional de Rosario, Argentina.
Alejandro I Recio-BalsellsFacultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Química de Rosario (IQUIR-CONICET), Universidad Nacional de Rosario, Argentina.
Guillermo R LabadieFacultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Química de Rosario (IQUIR-CONICET), Universidad Nacional de Rosario, Argentina.
Eriko TakanoManchester Centre of Fine and Specialty Chemicals (SYNBIOCHEM), Manchester Institute of Biotechnology (MIB), University of Manchester, UK.
Hugo GramajoFacultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Universidad Nacional de Rosario, Argentina.
Ana ArabolazaFacultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Universidad Nacional de Rosario, Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M017702/1
6 · The paper itself

Abstract

Iterative type I polyketide synthases (PKS) are megaenzymes essential to the biosynthesis of an enormously diverse array of bioactive natural products. Each PKS contains minimally three functional domains, β-ketosynthase (KS), acyltransferase (AT), and acyl carrier protein (ACP), and a subset of reducing domains such as ketoreductase (KR), dehydratase (DH), and enoylreductase (ER). The substrate selection, condensation reactions, and β-keto processing of the polyketide growing chain are highly controlled in a programmed manner. However, the structural features and mechanistic rules that orchestrate the iterative cycles, processing domains functionality, and chain termination in this kind of megaenzymes are often poorly understood. Here, we present a biochemical and functional characterization of the KS and the AT domains of a PKS from the mallard duck Anas platyrhynchos (ApPKS). ApPKS belongs to an animal PKS family phylogenetically more related to bacterial PKS than to metazoan fatty acid synthases. Through the dissection of the ApPKS enzyme into mono- to didomain fragments and its reconstitution in vitro, we determined its substrate specificity toward different starters and extender units. ApPKS AT domain can effectively transfer acetyl-CoA and malonyl-CoA to the ApPKS ACP stand-alone domain. Furthermore, the KS and KR domains, in the presence of Escherichia coli ACP, acetyl-CoA, and malonyl-CoA, showed the ability to catalyze the chain elongation and the β-keto reduction steps necessary to yield a 3-hydroxybutyryl-ACP derivate. These results provide new insights into the catalytic efficiency and specificity of this uncharacterized family of PKSs.

Indexed as

Acetyl Coenzyme AAcylationAnimalsCatalytic DomainDucksKineticsMalonyl Coenzyme APhylogenyPolyketide SynthasesProtein DomainsSubstrate SpecificityAcetyl Coenzyme AMalonyl Coenzyme APolyketide Synthasesdomain deconstructioniterative PKSPKS biochemistrysubstrate specificity

Identifiers

PMID30300504
PMCPMC6334511
OpenAlexW2896724190

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.