Reengineering of the feedback-inhibition enzyme N-acetyl-l-glutamate kinase to enhance l-arginine production in Corynebacterium crenatum View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2017-02

AUTHORS

Jingjing Zhang, Meijuan Xu, Xiaoxun Ge, Xian Zhang, Taowei Yang, Zhenghong Xu, Zhiming Rao

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. More... »

PAGES

271-283

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10295-016-1885-9

DOI

http://dx.doi.org/10.1007/s10295-016-1885-9

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https://app.dimensions.ai/details/publication/pub.1053339372

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28005186


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