Exploring the allosteric mechanism of dihydrodipicolinate synthase by reverse engineering of the allosteric inhibitor binding sites and its application for lysine production
文献类型：期刊论文
| 作者 | Geng, Feng1,2,3; Chen, Zhen2,3,4; Zheng, Ping2,3,5,6; Sun, Jibin2,3,5,6; Zeng, An-Ping2,3,4 |
| 刊名 | APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
 |
| 出版日期 | 2013-03-01 |
| 卷号 | 97期号:5页码:1963-1971 |
| 关键词 | Dihydrodipicolinate synthase (DHDPS) Allosteric binding site Escherichia coli Corynebacterium glutamicum L-Lysine overproduction |
| 英文摘要 | Dihydrodipicolinate synthase (DHDPS, EC 4.2.1.52) 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 %. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biotechnology & Applied Microbiology |
| 关键词[WOS] | CORYNEBACTERIUM-GLUTAMICUM ; ESCHERICHIA-COLI ; HOMOSERINE DEHYDROGENASE ; CRYSTAL-STRUCTURE ; REGULATORY PROPERTIES ; BACILLUS-ANTHRACIS ; ASPARTATE KINASE ; ASPARTOKINASE ; BIOSYNTHESIS ; DEREGULATION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000314836600015 |
| 公开日期 | 2012-08-28 |
| 源URL | [http://localhost/handle/0/255]  |
| 专题 | 天津工业生物技术研究所_微生物代谢工程 张学礼_期刊论文 |
| 作者单位 | 1.Tianjin Univ, Sch Chem Engn & Technol, Dept Biopharmaceut Engn, Tianjin 300072, Peoples R China 2.IBB TUHH, Joint Lab Syst Biotechnol, Tianjin 300308, Peoples R China 3.TIB CAS, Tianjin 300308, Peoples R China 4.Hamburg Univ Technol IBB TUHH, Inst Bioproc & Biosyst Engn, D-21073 Hamburg, Germany 5.Chinese Acad Sci, Key Lab Syst Microbial Biotechnol, Tianjin 300308, Peoples R China 6.Chinese Acad Sci TIB CAS, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China |
| 推荐引用方式 GB/T 7714 | Geng, Feng,Chen, Zhen,Zheng, Ping,et al. Exploring the allosteric mechanism of dihydrodipicolinate synthase by reverse engineering of the allosteric inhibitor binding sites and its application for lysine production[J]. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,2013,97(5):1963-1971. |
| APA | Geng, Feng,Chen, Zhen,Zheng, Ping,Sun, Jibin,&Zeng, An-Ping.(2013).Exploring the allosteric mechanism of dihydrodipicolinate synthase by reverse engineering of the allosteric inhibitor binding sites and its application for lysine production.APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,97(5),1963-1971. |
| MLA | Geng, Feng,et al."Exploring the allosteric mechanism of dihydrodipicolinate synthase by reverse engineering of the allosteric inhibitor binding sites and its application for lysine production".APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 97.5(2013):1963-1971. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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