Evidence map›Paper›PMID 29728854›Full record

ArticleJournal of industrial microbiology & biotechnology2018

Improved L-ornithine production in Corynebacterium crenatum by introducing an artificial linear transacetylation pathway.

Qunfeng Shu, Meijuan Xu, Jing Li, Taowei Yang, Xian Zhang, Zhenghong Xu, Zhiming Rao

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Metabolic Engineering ofFrontiers in bioengineering and biotechnology · 2022
    Article
  7. Production of l-glutamate family amino acids inSynthetic and systems biotechnology · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Recent Advances of L-ornithine Biosynthesis in Metabolically EngineeredFrontiers in bioengineering and biotechnology · 2019
    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 1 institution in 1 country.

Qunfeng ShuThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, Jiangsu, People's Republic of China.
Meijuan XuThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, Jiangsu, People's Republic of China. xumeijuan@jiangnan.edu.cn.
Jing LiThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, Jiangsu, People's Republic of China.
Taowei YangThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, Jiangsu, People's Republic of China.
Xian ZhangThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, Jiangsu, People's Republic of China.
Zhenghong XuThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, Jiangsu, People's Republic of China.
Zhiming RaoThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, Jiangsu, People's Republic of China. raozhm@jiangnan.edu.cn.
Jiangnan University · CN

Funding

The Jiangsu Province Science Fund for Distinguished Young Scholars BK20150002The National Natural Science Foundation of China 31570085The National Natural Science Foundation of China 31770058The Research Project of Chinese Ministry of Education 113033A
6 · The paper itself

Abstract

L-Ornithine is a non-protein amino acid with extensive applications in the food and pharmaceutical industries. In this study, we performed metabolic pathway engineering of an L-arginine hyper-producing strain of Corynebacterium crenatum for L-ornithine production. First, we amplified the L-ornithine biosynthetic pathway flux by blocking the competing branch of the pathway. To enhance L-ornithine synthesis, we performed site-directed mutagenesis of the ornithine-binding sites to solve the problem of L-ornithine feedback inhibition for ornithine acetyltransferase. Alternatively, the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-L-ornithine deacetylase, respectively, were introduced into Corynebacterium crenatum to mimic the linear pathway of L-ornithine biosynthesis. Fermentation of the resulting strain in a 5-L bioreactor allowed a dramatically increased production of L-ornithine, 40.4 g/L, with an overall productivity of 0.673 g/L/h over 60 h. This demonstrates that an increased level of transacetylation is beneficial for L-ornithine biosynthesis.

Indexed as

Metabolic EngineeringAcetylationArginineBacterial ProteinsBioreactorsBiosynthetic PathwaysCorynebacteriumEscherichia coliFermentationIndustrial MicrobiologyMutagenesis, Site-DirectedMutationOrnithineSerratia marcescensArginineBacterial ProteinsOrnithineCorynebacterium crenatumLinear transacetylation pathwayL-OrnithineOrnithine acetyltransferase

Identifiers

PMID29728854
OpenAlexW2800889272

What OpenQuestion holds

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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.