ArticleJournal of industrial microbiology & biotechnology2017
Reengineering of the feedback-inhibition enzyme N-acetyl-L-glutamate kinase to enhance L-arginine production in Corynebacterium crenatum.
Article in Journal of industrial microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Combing Directed Enzyme Evolution with Metabolic Engineering to Develop Efficient Microbial Cell Factories.Chem & bio engineering · 2025Review
- Enhanced Urea Production in the Diazotroph Azotobacter vinelandii as a Means of Stable Nitrogen Biofertiliser Production.Microbial biotechnology · 2025Article
- Mining unique cysteine synthetases and computational study on thoroughly eliminating feedback inhibition through tunnel engineering.Protein science : a publication of the Protein Society · 2024Article
- Multiple Functions of Compatible Solute Ectoine and Strategies for Constructing Overproducers for Biobased Production.Molecular biotechnology · 2024Review
- Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.Microbial cell factories · 2023Review
- Development of a 2-pyrrolidone biosynthetic pathway in Corynebacterium glutamicum by engineering an acetyl-CoA balance route.Amino acids · 2022Article
- Production of l-glutamate family amino acids inSynthetic and systems biotechnology · 2021Review
- PII Signal Transduction Protein GlnK Alleviates Feedback Inhibition ofApplied and environmental microbiology · 2020Article
- Recent Advances of L-ornithine Biosynthesis in Metabolically EngineeredFrontiers in bioengineering and biotechnology · 2019Review
- Improved L-ornithine production in Corynebacterium crenatum by introducing an artificial linear transacetylation pathway.Journal of industrial microbiology & biotechnology · 2018Article
- Our microbes not only produce antibiotics, they also overproduce amino acids.The Journal of antibiotics · 2017Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-acetyl-L-glutamate kinase (NAGK) catalyzes the second step of L-arginine biosynthesis and is inhibited by L-arginine in Corynebacterium crenatum. To ascertain the basis for the arginine sensitivity of CcNAGK, residue E19 which located at the entrance of the Arginine-ring was subjected to site-saturated mutagenesis and we successfully illustrated the inhibition-resistant mechanism. Typically, the E19Y mutant displayed the greatest deregulation of L-arginine feedback inhibition. An equally important strategy is to improve the catalytic activity and thermostability of CcNAGK. For further strain improvement, we used site-directed mutagenesis to identify mutations that improve CcNAGK. Results identified variants I74V, F91H and K234T display higher specific activity and thermostability. The L-arginine yield and productivity of the recombinant strain C. crenatum SYPA-EH3 (which possesses a combination of all four mutant sites, E19Y/I74V/F91H/K234T) reached 61.2 and 0.638 g/L/h, respectively, after 96 h in 5 L bioreactor fermentation, an increase of approximately 41.8% compared with the initial strain.
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