Evidence map›Paper›PMID 23720536›Full record

ReviewJournal of the Royal Society, Interface2013

Engineering the acyltransferase substrate specificity of assembly line polyketide synthases.

Briana J Dunn, Chaitan Khosla

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of the Royal Society, Interface, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

53 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Review
  3. 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
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Complex structure of the acyltransferase VinK and the carrier protein VinL with a pantetheine cross-linking probe.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  12. Recent trends in biocatalysis.Chemical Society reviews · 2021
    Review
  13. Interfacial plasticity facilitates high reaction rate ofProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Emerging evolutionary paradigms in antibiotic discovery.Journal of industrial microbiology & biotechnology · 2019
    Review
  20. Article
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

2 authors at 1 institution in 1 country.

Briana J DunnDepartment of Chemical Engineering, Stanford University, Stanford, CA, USA.
Chaitan Khosla
Stanford University · US

Funding

Structure, Mechanism, and Engineering of Assembly Line Polyketide SynthasesR01GM087934 · NIGMS · STANFORD UNIVERSITY · PI KHOSLA, CHAITAN · 2009 to 2021
$4.9M
NIGMS NIH HHS R01 GM 087934NIGMS NIH HHS R01 GM087934
6 · The paper itself

Abstract

Polyketide natural products act as a broad range of therapeutics, including antibiotics, immunosuppressants and anti-cancer agents. This therapeutic diversity stems from the structural diversity of these small molecules, many of which are produced in an assembly line manner by modular polyketide synthases. The acyltransferase (AT) domains of these megasynthases are responsible for selection and incorporation of simple monomeric building blocks, and are thus responsible for a large amount of the resulting polyketide structural diversity. The substrate specificity of these domains is often targeted for engineering in the generation of novel, therapeutically active natural products. This review outlines recent developments that can be used in the successful engineering of these domains, including AT sequence and structural data, mechanistic insights and the production of a diverse pool of extender units. It also provides an overview of previous AT domain engineering attempts, and concludes with proposed engineering approaches that take advantage of current knowledge. These approaches may lead to successful production of biologically active 'unnatural' natural products.

Indexed as

AcyltransferasesPolyketide SynthasesProtein EngineeringSubstrate SpecificityAcyltransferasesPolyketide Synthasesacyltransferaseantibioticsenzyme engineeringpolyketide

Identifiers

PMID23720536
PMCPMC3971720
OpenAlexW2136959581

What OpenQuestion holds

Textmetadata
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.