Evidence map›Paper›PMID 38663033›Full record

ReviewAnnual review of biochemistry2024

Structure and Mechanisms of Assembly-Line Polyketide Synthases.

Alexander M Soohoo, Dillon P Cogan, Krystal L Brodsky, Chaitan Khosla

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Engineering an Acyl-CoA Ligase With Enhanced Activity Toward Synthetic CoA Alternatives.Chembiochem : a European journal of chemical biology · 2026
    Article
  8. Article
  9. Article
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  11. Article
  12. Article
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  14. Peptide Backbone Editing via Post-Translational O to C Acyl Shift.Journal of the American Chemical Society · 2025
    Article
  15. The structure of full-length AFPK supports the ACP linker in a role that regulates iterative polyketide and fatty acid assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. 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

4 authors.

Alexander M SoohooSarafan ChEM-H, Stanford University, Stanford, California, USA.
Dillon P CoganCurrent affiliation: Department of Pharmacology and Pharmaceutical Sciences, University of Southern California, Los Angeles, California, USA.
Krystal L BrodskyDepartment of Chemistry, Stanford University, Stanford, California, USA.
Chaitan KhoslaSarafan ChEM-H, Stanford University, Stanford, California, USA.

Funding

Mechanisms and Evolution of Assembly-Line Polyketide SynthasesR35GM141799 · NIGMS · STANFORD UNIVERSITY · PI CHAITAN KHOSLA · 2021 to 2026
$2.5M
Mechanistic Studies of Polyketide Synthases Enabled by Unnatural Amino Acids and Antibody Fragment Structural ToolsF32GM136039 · NIGMS · STANFORD UNIVERSITY · PI COGAN, DILLON P · 2020 to 2022
$196k
NIGMS NIH HHS F32 GM136039NIGMS NIH HHS R35 GM141799
6 · The paper itself

Abstract

Three decades of studies on the multifunctional 6-deoxyerythronolide B synthase have laid a foundation for understanding the chemistry and evolution of polyketide antibiotic biosynthesis by a large family of versatile enzymatic assembly lines. Recent progress in applying chemical and structural biology tools to this prototypical assembly-line polyketide synthase (PKS) and related systems has highlighted several features of their catalytic cycles and associated protein dynamics. There is compelling evidence that multiple mechanisms have evolved in this enzyme family to channel growing polyketide chains along uniquely defined sequences of 10-100 active sites, each of which is used only once in the overall catalytic cycle of an assembly-line PKS. Looking forward, one anticipates major advances in our understanding of the mechanisms by which the free energy of a repetitive Claisen-like reaction is harnessed to guide the growing polyketide chain along the assembly line in a manner that is kinetically robust yet evolutionarily adaptable.

Indexed as

Catalytic DomainPolyketide SynthasesModels, MolecularPolyketidesProtein ConformationSubstrate SpecificityPolyketidesPolyketide Synthasescatalytic cyclemultifunctional enzymepolyketidepolyketide synthasevectorial biosynthesis

Identifiers

PMID38663033
PMCPMC11907408

What OpenQuestion holds

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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.