Publisher DOI: 10.1007/s00253-012-4062-8
Title: Exploring the allosteric mechanism of dihydrodipicolinate synthase by reverse engineering of the allosteric inhibitor binding sites and its application for lysine production
Language: English
Authors: Geng, Feng 
Chen, Zhen 
Zheng, Ping 
Sun, Jibin 
Zeng, An-Ping  
Keywords: Allosteric binding site;Corynebacterium glutamicum;Dihydrodipicolinate synthase (DHDPS);Escherichia coli;l-Lysine overproduction
Issue Date: 29-May-2012
Publisher: Springer
Source: Applied Microbiology and Biotechnology 5 (97): 1963-1971 (2013)
Journal or Series Name: Applied microbiology and biotechnology 
Abstract (english): Dihydrodipicolinate synthase (DHDPS, EC catalyzes the first committed reaction of l-lysine biosynthesis in bacteria and plants and is allosterically regulated by l-lysine. In previous studies, DHDPSs from different species were proved to have different sensitivity to l-lysine inhibition. In this study, we investigated the key determinants of feedback regulation between two industrially important DHDPSs, the l-lysine-sensitive DHDPS from Escherichia coli and l-lysine-insensitive DHDPS from Corynebacterium glutamicum, by sequence and structure comparisons and site-directed mutation. Feedback inhibition of E. coli DHDPS was successfully alleviated after substitution of the residues around the inhibitor's binding sites with those of C. glutamicum DHDPS. Interestingly, mutagenesis of the lysine binding sites of C. glutamicum DHDPS according to E. coli DHDPS did not recover the expected feedback inhibition but an activation of DHDPS by l-lysine, probably due to differences in the allosteic signal transduction in the DHDPS of these two organisms. Overexpression of l-lysine-insensitive E. coli DHDPS mutants in E. coli MG1655 resulted in an improvement of l-lysine production yield by 46 %. © 2012 Springer-Verlag.
ISSN: 1432-0614
Institute: Bioprozess- und Biosystemtechnik V-1 
Type: (wissenschaftlicher) Artikel
Funded by: Chinese Academy of Sciences (project KSCX2-EW-G-14-1)
Deutsche Forschungsgemeinschaft (DFG) (project ZE 542/6-1)
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