Evidence map›Paper›PMID 31115703›Full record

ArticleJournal of industrial microbiology & biotechnology2019

Structural insights into dehydratase substrate selection for the borrelidin and fluvirucin polyketide synthases.

Jesus F Barajas, Ryan P McAndrew, Mitchell G Thompson, Tyler W H Backman, Bo Pang, Tristan de Rond, Jose H Pereira, Veronica T Benites, Héctor García Martín, Edward E K Baidoo and 3 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Structure of a modular polyketide synthase reducing region.Structure (London, England : 1993) · 2023
    Article
  3. Article
  4. 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

13 authors at 4 institutions in 3 countries.

Jesus F BarajasDepartment of Energy Agile BioFoundry, Emeryville, CA, 94608, USA.
Ryan P McAndrewJoint BioEnergy Institute, 5885 Hollis St. 4th Floor, Emeryville, CA, 94608, USA.
Mitchell G ThompsonBiological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Tyler W H BackmanBiological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Bo PangBiological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Tristan de RondBiological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Jose H PereiraJoint BioEnergy Institute, 5885 Hollis St. 4th Floor, Emeryville, CA, 94608, USA.
Veronica T BenitesDepartment of Energy Agile BioFoundry, Emeryville, CA, 94608, USA.
Héctor García MartínDepartment of Energy Agile BioFoundry, Emeryville, CA, 94608, USA.
Edward E K BaidooDepartment of Energy Agile BioFoundry, Emeryville, CA, 94608, USA.
Nathan J HillsonDepartment of Energy Agile BioFoundry, Emeryville, CA, 94608, USA.
Paul D AdamsBiological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Jay D KeaslingBiological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA. jdkeasling@lbl.gov.ORCID http://orcid.org/0000-0002-4910-2222
Joint BioEnergy Institute · USLawrence Berkeley National Laboratory · USUniversity of California, Berkeley · USShenzhen Institutes of Advanced Technology · CN

Funding

Bioenergy Technologies Office DE-AC02-05CH11231
6 · The paper itself

Abstract

Engineered polyketide synthases (PKSs) are promising synthetic biology platforms for the production of chemicals with diverse applications. The dehydratase (DH) domain within modular type I PKSs generates an α,β-unsaturated bond in nascent polyketide intermediates through a dehydration reaction. Several crystal structures of DH domains have been solved, providing important structural insights into substrate selection and dehydration. Here, we present two DH domain structures from two chemically diverse PKSs. The first DH domain, isolated from the third module in the borrelidin PKS, is specific towards a trans-cyclopentane-carboxylate-containing polyketide substrate. The second DH domain, isolated from the first module in the fluvirucin B

Indexed as

Binding SitesFatty AlcoholsModels, MolecularPolyketide SynthasesProtein Structure, TertiarySubstrate SpecificityborrelidinFatty AlcoholsPolyketide SynthasesBorrelidinDehydrataseFluvirucinPolyketide

Identifiers

PMID31115703
PMCPMC6697708
OpenAlexW2944857295

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.