Evidence map›Paper›PMID 24402505›Full record

ArticleJournal of industrial microbiology & biotechnology2014

Enhancement of L-ornithine production by disruption of three genes encoding putative oxidoreductases in Corynebacterium glutamicum.

Gui-Hye Hwang, Jae-Yong Cho

Abstract read
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In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Production of l-glutamate family amino acids inSynthetic and systems biotechnology · 2021
    Review
  3. Diamine Biosynthesis: Research Progress and Application Prospects.Applied and environmental microbiology · 2020
    Review
  4. Article
  5. Recent Advances of L-ornithine Biosynthesis in Metabolically EngineeredFrontiers in bioengineering and biotechnology · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
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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

2 authors at 1 institution in 1 country.

Gui-Hye HwangDepartment of Pharmaceutical Engineering, College of Health Science, Sangji University, Sangjidae-gil 83, Wonju-si, Gangwon-do, 220-702, Korea.
Jae-Yong Cho
Sangji University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recently, Corynebacterium glutamicum has been shown to exhibit gluconate bypass activity, with two key enzymes, glucose dehydrogenase (GDH) and gluconate kinase, that provides an alternate route to 6-phosphogluconate formation. In this study, gene disruption analysis was used to examine possible metabolic functions of three proteins encoded by open reading frames having significant sequence similarity to GDH of Bacillus subtilis. Chromosomal in-frame deletion of three genes (NCgl0281, NCgl2582, and NCgl2053) encoding putative NADP⁺-dependent oxidoreductases led to the absence of GDH activity and correlated with increased specific glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities. This finding suggested that enhanced carbon flux from glucose was directed toward the oxidative pentose phosphate (PP) pathway, when the mutant was cultivated with 6 % glucose. Consequently, the mutant showed 72.4 % increased intracellular NADPH and 66.3 % increased extracellular L-ornithine production. The enhanced activities of the oxidative PP pathway in the mutant explain both the increased intracellular NADPH and the high extracellular concentration of L-ornithine. Thus, the observed metabolic changes in this work corroborate the importance of NADPH in L-ornithine production from C. glutamicum.

Indexed as

Bacillus subtilisCorynebacterium glutamicumGene DeletionGlucose 1-DehydrogenaseGlucosephosphate DehydrogenaseNADPOrnithinePentose Phosphate PathwayPhosphogluconate DehydrogenaseGlucose 1-DehydrogenaseGlucosephosphate DehydrogenaseNADPOrnithinePhosphogluconate Dehydrogenase

Identifiers

PMID24402505
OpenAlexW2081492794

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.