Evidence map›Paper›PMID 10347010›Full record

ArticleApplied and environmental microbiology1999

Expression of the Escherichia coli pntA and pntB genes, encoding nicotinamide nucleotide transhydrogenase, in Saccharomyces cerevisiae and its effect on product formation during anaerobic glucose fermentation.

M Anderlund, T L Nissen, J Nielsen, J Villadsen, J Rydström, B Hahn-Hägerdal, M C Kielland-Brandt

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Impact of overexpressing NADH kinase on glucoamylase production in Aspergillus niger.Journal of industrial microbiology & biotechnology · 2022
    Article
  3. Article
  4. Intracellular Redox Perturbation inFrontiers in bioengineering and biotechnology · 2020
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Progress in metabolic engineering of Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2008
    Review
  14. Article
  15. Article
  16. Improved anaerobic use of arginine by Saccharomyces cerevisiae.Applied and environmental microbiology · 2003
    Article
  17. Article
  18. Article
  19. Metabolic engineering of Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2000
    Review
  20. 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

7 authors at 4 institutions in 2 countries.

M AnderlundDepartment of Yeast Genetics, Carlsberg Laboratory, DK-2500 Copenhagen Valby, Denmark.
T L Nissen
J Nielsen
J Villadsen
J Rydström
B Hahn-Hägerdal
M C Kielland-Brandt
Carlsberg Laboratory · DKTechnical University of Denmark · DKChalmers University of Technology · SELund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We studied the physiological effect of the interconversion between the NAD(H) and NADP(H) coenzyme systems in recombinant Saccharomyces cerevisiae expressing the membrane-bound transhydrogenase from Escherichia coli. Our objective was to determine if the membrane-bound transhydrogenase could work in reoxidation of NADH to NAD+ in S. cerevisiae and thereby reduce glycerol formation during anaerobic fermentation. Membranes isolated from the recombinant strains exhibited reduction of 3-acetylpyridine-NAD+ by NADPH and by NADH in the presence of NADP+, which demonstrated that an active enzyme was present. Unlike the situation in E. coli, however, most of the transhydrogenase activity was not present in the yeast plasma membrane; rather, the enzyme appeared to remain localized in the membrane of the endoplasmic reticulum. During anaerobic glucose fermentation we observed an increase in the formation of 2-oxoglutarate, glycerol, and acetic acid in a strain expressing a high level of transhydrogenase, which indicated that increased NADPH consumption and NADH production occurred. The intracellular concentrations of NADH, NAD+, NADPH, and NADP+ were measured in cells expressing transhydrogenase. The reduction of the NADPH pool indicated that the transhydrogenase transferred reducing equivalents from NADPH to NAD+.

Indexed as

AnaerobiosisBlotting, WesternCloning, MolecularEscherichia coliFermentationGlucoseNADNADP TranshydrogenasesRecombinant ProteinsSaccharomyces cerevisiaeTransformation, GeneticGlucoseNADNADP TranshydrogenasesRecombinant Proteins

Identifiers

PMID10347010
PMCPMC91345
OpenAlexW1480463281

What OpenQuestion holds

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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.