Evidence map›Paper›PMID 24048943›Full record

ArticleJournal of industrial microbiology & biotechnology2013

Improvement of NADPH bioavailability in Escherichia coli by replacing NAD(+)-dependent glyceraldehyde-3-phosphate dehydrogenase GapA with NADP (+)-dependent GapB from Bacillus subtilis and addition of NAD kinase.

Yipeng Wang, Ka-Yiu San, George N Bennett

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2013. 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
1.3field-weighted citation impact, top 20% 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, 27 citations in OpenAlex.

  1. Review
  2. Engineering Escherichia coli to produce medium chain oleochemicals from C2 substrates.Journal of industrial microbiology & biotechnology · 2026
    Article
  3. Glyceraldehyde-3-phosphate dehydrogenase homologs as bifunctional gatekeepers of metabolic segregation inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Positioning Bacillus subtilis as terpenoid cell factory.Journal of applied microbiology · 2021
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Bioengineering (Basel, Switzerland) · 2015
    Review
  11. Review
  12. NADPH-generating systems in bacteria and archaea.Frontiers in microbiology · 2015
    Review
  13. 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

3 authors at 1 institution in 1 country.

Yipeng WangDepartment of Biochemistry and Cell Biology, MS-140, Rice University, 6100 Main Street, Houston, TX, 77005, USA.
Ka-Yiu San
George N Bennett
Rice University · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Enzymatic synthesis of some industrially important compounds depends heavily on cofactor NADPH as the reducing agent. This is especially true in the synthesis of chiral compounds that are often used as pharmaceutical intermediates to generate the correct stereochemistry in bioactive products. The high cost and technical difficulty of cofactor regeneration often pose a challenge for such biocatalytic reactions. In this study, to increase NADPH bioavailability, the native NAD(+)-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gapA gene in Escherichia coli was replaced with a NADP(+)-dependent gapB from Bacillus subtilis. To overcome the limitation of NADP(+) availability, E. coli NAD kinase, nadK was also coexpressed with gapB. The recombinant strains were then tested in three reporting systems: biosynthesis of lycopene, oxidation of cyclohexanone with cyclohexanone monooxygenase (CHMO), and an anaerobic system utilizing 2-haloacrylate reductase (CAA43). In all the reporting systems, replacing NAD(+)-dependent GapA activity with NADP(+)-dependent GapB activity increased the synthesis of NADPH-dependent compounds. The increase was more pronounced when NAD kinase was also overexpressed in the case of the one-step reaction catalyzed by CAA43 which approximately doubled the product yield. These results validate this novel approach to improve NADPH bioavailability in E. coli and suggest that the strategy can be applied in E. coli or other bacterium-based production of NADPH-dependent compounds.

Indexed as

Bacillus subtilisBiological AvailabilityCarotenoidsChromatography, High Pressure LiquidEscherichia coliGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)GlycolysisLycopeneMetabolomeMutationNADNADPOxidation-ReductionOxygenasesPhosphotransferases (Alcohol Group Acceptor)PlasmidsCarotenoidscyclohexanone oxygenaseGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)LycopeneNADNAD kinaseNADPOxygenasesPhosphotransferases (Alcohol Group Acceptor)Protein Subunits

Identifiers

PMID24048943
OpenAlexW2051709446

What OpenQuestion holds

Textmetadata
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.