Evidence map›Paper›PMID 25089587›Full record

ArticleACS chemical biology2014

A double-hotdog with a new trick: structure and mechanism of the trans-acyltransferase polyketide synthase enoyl-isomerase.

Darren C Gay, Philip J Spear, Adrian T Keatinge-Clay

Abstract read
In one paragraph

Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
5.4field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Journal of natural products · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. New Alpiniamides FromFrontiers in microbiology · 2018
    Article
  14. Article
  15. Article
  16. Review
  17. Polyketide stereocontrol: a study in chemical biology.Beilstein journal of organic chemistry · 2017
    Review
  18. Article
  19. Article
  20. Harnessing natural product assembly lines: structure, promiscuity, and engineering.Journal of industrial microbiology & biotechnology · 2016
    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

3 authors at 1 institution in 1 country.

Darren C GayDepartment of Molecular Biosciences, University of Texas at Austin , Austin, Texas 78712, United States.
Philip J Spear
Adrian T Keatinge-Clay
The University of Texas at Austin · US

Funding

Determining the Architectures and Activities of Polyketide Synthase ModulesR01GM106112 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI KEATINGE-CLAY, ADRIAN TRISTAN · 2013 to 2025
$3.9M
Howard Hughes Medical InstituteNIGMS NIH HHS GM106112NIGMS NIH HHS R01 GM106112
6 · The paper itself

Abstract

Many polyketide natural products exhibit invaluable medicinal properties, yet much remains to be understood regarding the machinery responsible for their biosynthesis. The recently discovered trans-acyltransferase polyketide synthases employ processing enzymes that catalyze modifications unique from those of the classical cis-acyltransferase polyketide synthases. The enoyl-isomerase domains of these megasynthases shift double bonds and are well-represented by an enzyme that helps forge the triene system within the antibiotic produced by the prototypical bacillaene synthase. This first crystal structure of an enoyl-isomerase, at 1.73 Å resolution, not only revealed relationships between this class of enzymes and dehydratases but also guided an investigation into the mechanism of double bond migration. The catalytic histidine, positioned differently from that of dehydratases, was demonstrated to independently shuttle a proton between the γ- and α-positions of the intermediate. This unprecedented mechanism highlights the catalytic diversity of divergent enzymes within trans-acyltransferase polyketide synthases.

Indexed as

AcyltransferasesBacillus subtilisCatalysisCrystallography, X-RayHydro-LyasesModels, MolecularPolyketide SynthasesProtein ConformationProtein Structure, TertiaryProtonsAcyltransferasesHydro-LyasesPolyketide SynthasesProtons

Identifiers

PMID25089587
PMCPMC4201341
OpenAlexW2334382287

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.