Evidence map›Paper›PMID 30834961›Full record

ArticleApplied microbiology and biotechnology2019

The role of the acyl-CoA thioesterase "YciA" in the production of (R)-3-hydroxybutyrate by recombinant Escherichia coli.

Mónica Guevara-Martínez, Mariel Perez-Zabaleta, Martin Gustavsson, Jorge Quillaguamán, Gen Larsson, Antonius J A van Maris

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 33 citations in OpenAlex.

  1. Enhanced growth of 1-butanol producingBiodesign research · 2026
    Article
  2. Engineering New-to-Nature Biological Pathways for β,γ-Alkanediol Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022
    Article
  11. Development ofFrontiers in bioengineering and biotechnology · 2021
    Article
  12. 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

6 authors at 2 institutions in 2 countries.

Mónica Guevara-MartínezDepartment of Industrial Biotechnology, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE 10691, Stockholm, Sweden.
Mariel Perez-ZabaletaDepartment of Industrial Biotechnology, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE 10691, Stockholm, Sweden.
Martin GustavssonDepartment of Industrial Biotechnology, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE 10691, Stockholm, Sweden.
Jorge QuillaguamánFaculty of Science and Technology, Center of Biotechnology, Universidad Mayor de San Simón, Cochabamba, Bolivia.
Gen LarssonDepartment of Industrial Biotechnology, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE 10691, Stockholm, Sweden.
Antonius J A van MarisDepartment of Industrial Biotechnology, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Center, SE 10691, Stockholm, Sweden. tonvm@kth.se.ORCID http://orcid.org/0000-0001-5319-7511
AlbaNova · SEUniversidad Mayor de San Simón · BO

Funding

Svenska Forskningsrådet Formas 2014-1620Svenska Forskningsrådet Formas (SE) 211-2013-70
6 · The paper itself

Abstract

Biotechnologically produced (R)-3-hydroxybutyrate is an interesting pre-cursor for antibiotics, vitamins, and other molecules benefitting from enantioselective production. An often-employed pathway for (R)-3-hydroxybutyrate production in recombinant E. coli consists of three-steps: (1) condensation of two acetyl-CoA molecules to acetoacetyl-CoA, (2) reduction of acetoacetyl-CoA to (R)-3-hydroxybutyrate-CoA, and (3) hydrolysis of (R)-3-hydroxybutyrate-CoA to (R)-3-hydroxybutyrate by thioesterase. Whereas for the first two steps, many proven heterologous candidate genes exist, the role of either endogenous or heterologous thioesterases is less defined. This study investigates the contribution of four native thioesterases (TesA, TesB, YciA, and FadM) to (R)-3-hydroxybutyrate production by engineered E. coli AF1000 containing a thiolase and reductase from Halomonas boliviensis. Deletion of yciA decreased the (R)-3-hydroxybutyrate yield by 43%, whereas deletion of tesB and fadM resulted in only minor decreases. Overexpression of yciA resulted in doubling of (R)-3-hydroxybutyrate titer, productivity, and yield in batch cultures. Together with overexpression of glucose-6-phosphate dehydrogenase, this resulted in a 2.7-fold increase in the final (R)-3-hydroxybutyrate concentration in batch cultivations and in a final (R)-3-hydroxybutyrate titer of 14.3 g L

Indexed as

3-Hydroxybutyric AcidAcyl Coenzyme ABacterial ProteinsBatch Cell Culture TechniquesEscherichia coliEscherichia coli ProteinsHalomonasMetabolic EngineeringPalmitoyl-CoA HydrolaseThiolester Hydrolases3-Hydroxybutyric AcidAcyl Coenzyme ABacterial ProteinsEscherichia coli ProteinsPalmitoyl-CoA HydrolaseThiolester HydrolasesyciA protein, E coliEscherichia coliHalomonas boliviensis(R)-3-hydroxybutyrateThioesteraseyciA

Identifiers

PMID30834961
PMCPMC6469607
OpenAlexW2918951300

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.