期刊
METABOLIC ENGINEERING
卷 18, 期 -, 页码 53-59出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymben.2013.04.002
关键词
FPP synthase; Z,E-FPP; Z,E-Farnesol; Protein fusion; Sesquiterpene
资金
- National Research Foundation [NRF-2010-C1AAA001-0029084]
- Intelligent Synthetic Biology Center of Global Frontier Project
- MEST [2011-0031964]
- Next-Generation BioGreen 21 Program, (SSAC), RDA, Korea [PJ0081842012]
- MEST, Korea
- National Research Foundation of Korea [2011-0031964] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Production of Z-type farnesyl diphosphate (FPP) has not been repotted in Escherichia coli. Here we present the fusion enzyme (ILRv) of E. coli E,E-FPP synthase (IspA) and Mycobacterium tuberculosis Z,E-FPP synthase (Rv1086), which can produce primarily Z,E-FPP rather than E,E-FPP, the predominant stereoisomer found in most organisms. Z,E-farnesol (FOH) was produced from E. coli harboring the bottom portion of the MVA pathway and the fusion FPP synthase (ILRv) at a titer of 115.6 mg/L in 2 YT medium containing 1% (v/v) glycerol as a carbon source and 5 mM mevalonate. The Z,E-FOH production was improved by 15-fold, compared with 7.7 mg/L obtained from the co-overexpression of separate IspA and Rv1086. The Z,E-FPP was not metabolized in native metabolic pathways of E. coli. It would be of interest to produce Z,E-FPP derived sesquiterpenes from recombinant E. coli due to no loss of Z,E-FPP substrate in endogenous metabolism of the host strain. (C) 2013 Elsevier Inc. All rights reserved.
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