Evidence map›Paper›PMID 21541714›Full record

ArticleJournal of industrial microbiology & biotechnology2011

Development of L-tryptophan production strains by defined genetic modification in Escherichia coli.

Zhi-Jun Zhao, Chun Zou, Yi-Xing Zhu, Jun Dai, Sheng Chen, Dan Wu, Jing Wu, Jian Chen

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  3. Review
  4. Review
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  6. Article
  7. A comprehensive review and comparison of L-tryptophan biosynthesis inFrontiers in bioengineering and biotechnology · 2023
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. EngineeringSynthetic and systems biotechnology · 2020
    Article
  15. Article
  16. Review
  17. Metabolic engineering for improving L-tryptophan production in Escherichia coli.Journal of industrial microbiology & biotechnology · 2019
    Review
  18. Article
  19. Article
  20. 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

8 authors at 1 institution in 1 country.

Zhi-Jun ZhaoState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Chun Zou
Yi-Xing Zhu
Jun Dai
Sheng Chen
Dan Wu
Jing Wu
Jian Chen
Jiangnan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Construction and improvement of industrial strains play a central role in the commercial development of microbial fermentation processes. L-tryptophan producers have usually been developed by classical random mutagenesis due to its complicated metabolic network and regulatory mechanism. However, in the present study, an L-tryptophan overproducing Escherichia coli strain was developed by defined genetic modification methodology. Feedback inhibitions of 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase (AroF) and anthranilate synthase (TrpED) were eliminated by site-directed mutagenesis. Expression of deregulated AroF and TrpED was achieved by using a temperature-inducible expression plasmid pSV. Transcriptional regulation of trp repressor was removed by deleting trpR. Pathway for L-Trp degradation was removed by deleting tnaA. L-phenylalanine and L-tyrosine biosynthesis pathways that compete with L-tryptophan biosynthesis were blocked by deleting their critical genes (pheA and tyrA). The final engineered E. coli can produce 13.3 g/l of L-tryptophan. Fermentation characteristics of the engineered strains were also analyzed.

Indexed as

Anthranilate SynthaseBacterial ProteinsEscherichia coliEscherichia coli ProteinsFeedback, PhysiologicalGene Knockout TechniquesMultienzyme ComplexesMutagenesis, Site-DirectedPhenylalaninePlasmidsPrephenate DehydrataseRepressor ProteinsTryptophanTryptophanaseTyrosineAnthranilate SynthaseBacterial ProteinsEscherichia coli ProteinsMultienzyme ComplexesPhenylalanineP-protein, E coliPrephenate DehydrataseRepressor ProteinsTRPR protein, E coliTryptophanTryptophanaseTyrosine

Identifiers

PMID21541714
OpenAlexW2026569578

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.