Evidence map›Paper›PMID 19362640›Full record

ArticleMethods in enzymology2009

Type I polyketide synthases that require discrete acyltransferases.

Yi-Qiang Cheng, Jane M Coughlin, Si-Kyu Lim, Ben Shen

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
10.7field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Review
  3. Bongkrekic Acid andFoods (Basel, Switzerland) · 2023
    Review
  4. Review
  5. Review
  6. Biosynthesis of Largimycins inACS chemical biology · 2022
    Article
  7. An Unconventional Melanin Biosynthesis Pathway in Ustilago maydis.Applied and environmental microbiology · 2021
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Structural and evolutionary relationships of "AT-less" type I polyketide synthase ketosynthases.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  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

4 authors at 1 institution in 1 country.

Yi-Qiang ChengDepartment of Chemistry and Biochemistry, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin, USA.
Jane M Coughlin
Si-Kyu Lim
Ben Shen
University of Wisconsin–Milwaukee · US

Funding

Zeeh Pharmaceutical Experimental StationU19CA113297 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI HOFFMANN, F. MICHAEL · 2005 to 2009
$5.4M
Enediyne Biosynthesis and EngineeringR01CA078747 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI SHEN, BEN · 1999 to 2015
$3.4M
AT-less Type I Polyketide SynthasesR01CA106150 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI SHEN, BEN · 2004 to 2015
$3.3M
NCI NIH HHS CA106150NCI NIH HHS CA113297NCI NIH HHS R01 CA078747NCI NIH HHS R01 CA106150NCI NIH HHS U19 CA113297
6 · The paper itself

Abstract

The diverse structures of polyketide natural products are reflected by the equally diverse polyketide biosynthetic enzymes, namely polyketide synthases (PKSs). Three major classes of PKSs are known-noniterative type I PKSs, iterative type II PKSs and acyl carrier protein-independent type III PKSs, each of which consists of additional variants. One such variant is the noniterative type I PKS in which each PKS module lacks the cognate acyltransferase (AT) domain. The essential AT activity is instead provided by a discrete AT in trans. Termed "AT-less" type I PKSs, the loading of the malonate extender units by the discrete AT enzyme LnmG to each of the AT-less PKS modules of LnmI and LnmJ was confirmed experimentally for biosynthesis of the anticancer antibiotic leinamycin (LNM). The LNM PKS has since served as a model for the continuous discovery of numerous additional AT-less type I PKSs incorporating variable extender units. However, biochemical characterization of AT-less type I PKSs remains very limited, and the mechanism by which AT-less type I PKSs accommodate multiple extender units is unknown. This chapter provides the protocols used to establish and characterize the LNM PKS. Application of these methods to other AT-less type I PKSs should aid the biochemical characterization and hence possible exploitation of these unique PKSs for polyketide natural product structural diversity by combinatorial biosynthetic methods.

Indexed as

Acyl Carrier ProteinAcyltransferasesModels, BiologicalPhylogenyPolyketide SynthasesProtein Structure, TertiarySubstrate SpecificityAcyl Carrier ProteinAcyltransferasesPolyketide Synthases

Identifiers

PMID19362640
PMCPMC4480786
OpenAlexW2404041364

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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.