Evidence map›Paper›PMID 31399628›Full record

ArticleScientific reports2019

Construction of a synthetic pathway for the production of 1,3-propanediol from glucose.

Cláudio J R Frazão, Débora Trichez, Hélène Serrano-Bataille, Adilia Dagkesamanskaia, Christopher M Topham, Thomas Walther, Jean Marie François

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 48 citations in OpenAlex.

  1. Metabolic engineering enablesSynthetic and systems biotechnology · 2026
    Article
  2. Article
  3. Selective Deoxygenation of Biomass Polyols into Diols.Molecules (Basel, Switzerland) · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Progress in 1,3-propanediol biosynthesis.Frontiers in bioengineering and biotechnology · 2024
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. 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

7 authors at 2 institutions in 2 countries.

Cláudio J R FrazãoToulouse Biotechnology Institute (TBI), Université de Toulouse, CNRS, INRA, INSA, 135 Avenue de Rangueil, F-31077, Toulouse, France.
Débora TrichezToulouse Biotechnology Institute (TBI), Université de Toulouse, CNRS, INRA, INSA, 135 Avenue de Rangueil, F-31077, Toulouse, France.
Hélène Serrano-BatailleToulouse Biotechnology Institute (TBI), Université de Toulouse, CNRS, INRA, INSA, 135 Avenue de Rangueil, F-31077, Toulouse, France.
Adilia DagkesamanskaiaToulouse Biotechnology Institute (TBI), Université de Toulouse, CNRS, INRA, INSA, 135 Avenue de Rangueil, F-31077, Toulouse, France.
Christopher M TophamMolecular Forces Consulting, 40 rue Boyssonne, F-31400, Toulouse, France.
Thomas WaltherToulouse Biotechnology Institute (TBI), Université de Toulouse, CNRS, INRA, INSA, 135 Avenue de Rangueil, F-31077, Toulouse, France.
Jean Marie FrançoisToulouse Biotechnology Institute (TBI), Université de Toulouse, CNRS, INRA, INSA, 135 Avenue de Rangueil, F-31077, Toulouse, France. fran_jm@insa-toulouse.fr.ORCID http://orcid.org/0000-0001-9884-5535
Centre National de la Recherche Scientifique · FRMNM Consulting (France) · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this work, we describe the construction of a synthetic metabolic pathway enabling direct biosynthesis of 1,3-propanediol (PDO) from glucose via the Krebs cycle intermediate malate. This non-natural pathway extends a previously published synthetic pathway for the synthesis of (L)-2,4-dihydroxybutyrate (L-DHB) from malate by three additional reaction steps catalyzed respectively, by a DHB dehydrogenase, a 2-keto-4-hydroxybutyrate (OHB) dehydrogenase and a PDO oxidoreductase. Screening and structure-guided protein engineering provided a (L)-DHB dehydrogenase from the membrane-associated (L)-lactate dehydrogenase of E. coli and OHB decarboxylase variants derived from the branched-chain keto-acid decarboxylase encoded by kdcA from Lactococcus lactis or pyruvate decarboxylase from Zymomonas mobilis. The simultaneous overexpression of the genes encoding these enzymes together with the endogenous ydhD-encoded aldehyde reductase enabled PDO biosynthesis from (L)-DHB. While the simultaneous expression of the six enzymatic activities in a single engineered E. coli strain resulted in a low production of 0.1 mM PDO from 110 mM glucose, a 40-fold increased PDO titer was obtained by co-cultivation of an E. coli strain expressing the malate-DHB pathway with another strain harboring the DHB-to-PDO pathway.

Indexed as

Metabolic EngineeringBiosynthetic PathwaysCitric Acid CycleEscherichia coliGlucoseIndustrial MicrobiologyLactococcus lactisPropylene GlycolsPyruvate DecarboxylaseZymomonas1,3-propanediolGlucosePropylene GlycolsPyruvate Decarboxylase

Identifiers

PMID31399628
PMCPMC6689062
OpenAlexW2968439292

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.