期刊
FEMS MICROBIOLOGY LETTERS
卷 353, 期 1, 页码 11-18出版社
OXFORD UNIV PRESS
DOI: 10.1111/1574-6968.12397
关键词
DAHP synthases; AroF; l-phenylalanine; Corynebacterium glutamicum
类别
资金
- National Natural Science Foundation of China (973 Program) [2014CB745103, 2013CB733602]
- National High Technology Research and Development Program of China (863 Program) [2012AA021201]
- National Natural Science Foundation of China [31200020]
- National Science Foundation for Post-doctoral Scientists of China [2013M540414]
- Jiangsu Planned Projects for Postdoctoral Research Funds [1301010B]
- 111 Project
- Priority Academic Program Development of Jiangsu Higher Education Institutions
3-Deoxy-d-arabino-heptulosonate 7-phosphate synthase (DAHP synthase) encoded by aroF is the first enzyme of the shikimate pathway. In the present study, an AroF variant with a deficiency in residue Ile11 (named AroF*) was shown to be insensitive to l-tyrosine. According to three-dimensional structure analysis, nine AroF variants were constructed with truncation of different N-terminal fragments, and overexpression of the variants AroF((1-9)), AroF((1-10)), AroF((1-12)) and, in particular, AroF((1-11)) significantly increased the accumulation of l-phenylalanine (l-Phe). However, the AroG and AroH variants with similar truncations of the N-terminal fragments decreased the production of l-Phe. By co-overexpressing AroF((1-11)) and PheA(fbr), the production of l-Phe was increased from 2.36 +/- 0.07gL(-1) (co-overexpression of the wild-type AroF and PheA(fbr)) to 4.29 +/- 0.06gL(-1). The novel variant AroF((1-11)) showed great potential for the production of aromatic amino acids and their derivatives.
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