Evidence map›Paper›PMID 28947739›Full record

ArticleNature microbiology2017

A metabolic pathway for catabolizing levulinic acid in bacteria.

Jacqueline M Rand, Tippapha Pisithkul, Ryan L Clark, Joshua M Thiede, Christopher R Mehrer, Daniel E Agnew, Candace E Campbell, Andrew L Markley, Morgan N Price, Jayashree Ray and 6 more

Open access · greenAbstract read
In one paragraph

Article in Nature microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. ACAD10 and ACAD11 enable mammalian 4-hydroxy acid lipid catabolism.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. Engineered Membrane Vesicle Production viaACS synthetic biology · 2025
    Article
  7. EngineeringMetabolic engineering communications · 2025
    Article
  8. ACAD10 and ACAD11 allow entry of 4-hydroxy fatty acids into β-oxidation.Cellular and molecular life sciences : CMLS · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. A Genetically Encoded Biosensor for the Detection of Levulinic Acid.Journal of microbiology and biotechnology · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Metabolic Engineering ofJournal of microbiology and biotechnology · 2022
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 2 institutions in 1 country.

Jacqueline M RandDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Tippapha PisithkulGraduate Program in Cellular and Molecular Biology, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Ryan L ClarkDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Joshua M ThiedeDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Christopher R MehrerDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Daniel E AgnewDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Candace E CampbellDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Andrew L MarkleyDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Morgan N PriceEnvironmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Jayashree RayEnvironmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Kelly M WetmoreEnvironmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Yumi SuhEnvironmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Adam P ArkinEnvironmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Adam M DeutschbauerEnvironmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Daniel Amador-NoguezGraduate Program in Cellular and Molecular Biology, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Brian F PflegerDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, 53706, USA. pfleger@engr.wisc.edu.ORCID http://orcid.org/0000-0002-9232-9959
University of Wisconsin–Madison · USLawrence Berkeley National Laboratory · US

Funding

BIOTECHNOLOGY TRAINING PROGRAMT32GM008349 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI FOX, BRIAN G · 1989 to 2019
$22.5M
Institutional Training in the Genomic SciencesT32HG002760 · NHGRI · UNIVERSITY OF WISCONSIN-MADISON · PI Qiongshi Lu · 2003 to 2026
$17.7M
NHGRI NIH HHS T32 HG002760NIGMS NIH HHS T32 GM008349
6 · The paper itself

Abstract

Microorganisms can catabolize a wide range of organic compounds and therefore have the potential to perform many industrially relevant bioconversions. One barrier to realizing the potential of biorefining strategies lies in our incomplete knowledge of metabolic pathways, including those that can be used to assimilate naturally abundant or easily generated feedstocks. For instance, levulinic acid (LA) is a carbon source that is readily obtainable as a dehydration product of lignocellulosic biomass and can serve as the sole carbon source for some bacteria. Yet, the genetics and structure of LA catabolism have remained unknown. Here, we report the identification and characterization of a seven-gene operon that enables LA catabolism in Pseudomonas putida KT2440. When the pathway was reconstituted with purified proteins, we observed the formation of four acyl-CoA intermediates, including a unique 4-phosphovaleryl-CoA and the previously observed 3-hydroxyvaleryl-CoA product. Using adaptive evolution, we obtained a mutant of Escherichia coli LS5218 with functional deletions of fadE and atoC that was capable of robust growth on LA when it expressed the five enzymes from the P. putida operon. This discovery will enable more efficient use of biomass hydrolysates and metabolic engineering to develop bioconversions using LA as a feedstock.

Indexed as

BacteriaBacterial ProteinsBase SequenceBiomassCarbonCRISPR-Cas SystemsDNA Transposable ElementsEscherichia coliGene Expression Regulation, BacterialGene Knockdown TechniquesGenes, BacterialLevulinic AcidsMetabolic EngineeringMetabolic Networks and PathwaysOperonPropionatesBacterial ProteinsCarbonDNA Transposable ElementsLevulinic AcidsPropionates

Identifiers

PMID28947739
PMCPMC5705400
OpenAlexW2759832015

What OpenQuestion holds

Textmetadata
LicenceTDM
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.