Zobrazeno 1 - 10
of 1 506
pro vyhledávání: '"ribosomal binding site"'
Autor:
Yue Wu, Guang-Qing Du, Dong-Han Ma, Jin-Long Li, Huan Fang, Hui-Na Dong, Zhao-Xia Jin, Da-Wei Zhang
Publikováno v:
Synthetic and Systems Biotechnology, Vol 10, Iss 1, Pp 307-313 (2025)
Biotin (vitamin B7) is a crucial cofactor for various metabolic processes and has significant applications in pharmaceuticals, cosmetics, and animal feed. Bacillus subtilis, a well-studied Gram-positive bacterium, presents a promising host for biotin
Externí odkaz:
https://doaj.org/article/75ca6c60ed334e1fbfe6761e5e40ab9e
Publikováno v:
Microbial Cell Factories, Vol 21, Iss 1, Pp 1-12 (2022)
Abstract Background Lycopene is increasing in demand due to its widespread use in the pharmaceutical and food industries. Metabolic engineering and synthetic biology technologies have been widely used to overexpress the heterologous mevalonate pathwa
Externí odkaz:
https://doaj.org/article/90390951db0c407b9010a4e67b3725c5
Akademický článek
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Publikováno v:
Microbial Cell Factories, Vol 19, Iss 1, Pp 1-12 (2020)
Abstract Background Hydrogenobyrinic acid is a key intermediate of the de-novo aerobic biosynthesis pathway of vitamin B12. The introduction of a heterologous de novo vitamin B12 biosynthesis pathway in Escherichia coli offers an alternative approach
Externí odkaz:
https://doaj.org/article/631d44b6816e479f97f6937432dac19b
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
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Autor:
Yongfu Yang, Wei Shen, Ju Huang, Runxia Li, Yubei Xiao, Hui Wei, Yat-Chen Chou, Min Zhang, Michael E. Himmel, Shouwen Chen, Li Yi, Lixin Ma, Shihui Yang
Publikováno v:
Biotechnology for Biofuels, Vol 12, Iss 1, Pp 1-13 (2019)
Abstract Background Zymomonas mobilis is a model bacterial ethanologen with many systems biology studies reported. Besides lignocellulosic ethanol production, Z. mobilis has been developed as a platform for biochemical production through metabolic en
Externí odkaz:
https://doaj.org/article/b0575d613ad546e0939cd98f62962297
Publikováno v:
AMB Express, Vol 8, Iss 1, Pp 1-17 (2018)
Abstract Glutamate decarboxylase (GAD) converts l-glutamate (Glu) into γ-aminobutyric acid (GABA). Corynebacterium glutamicum that expresses exogenous GAD gene, gadB2 or gadB1, can synthesize GABA from its own produced Glu. To enhance GABA productio
Externí odkaz:
https://doaj.org/article/2037b1afb12c4a9e8630e04d40a0a4b6
Publikováno v:
Journal of Agricultural and Food Chemistry. 69:12241-12249
Riboflavin is widely used as a food additive. Here, multiple strategies were used to increase riboflavin production in Escherichia coli LS31T. First, purR deletion and co-overexpression of fbp, purF, prs, gmk, and ndk genes resulted in an increase of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8757911fa532897195a44dcbcbdf2caa
https://doi.org/10.1021/acs.jafc.1c04471
https://doi.org/10.1021/acs.jafc.1c04471
Publikováno v:
ACS Synthetic Biology. 10:2753-2762
The plasmid-driven T7 system (PDT7) is a flexible approach to trigger protein overexpression; however, most of the reported PDT7 rely on many auxiliary elements or inducible systems to attenuate the toxicity from the orthogonality of the T7 system, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::129a597cddddd2b4d3068d07d2a25185
https://doi.org/10.1021/acssynbio.1c00361
https://doi.org/10.1021/acssynbio.1c00361
Autor:
Ji-Young Ahn, Sung Min Woo, Young-Chang Kim, Yang-Hoon Kim, Woo-Ri Shin, Hyun-Ju Um, Simranjeet Singh Sekhon
Publikováno v:
Toxicology and Environmental Health Sciences. 13:183-192
In the described experiments, we identify and clone a novel serine palmitoyltransferase (SPT) isolated from the gram-negative obligatory aerobic bacteria Sphingobium chungbukense strain KCTC2955. SPT catalyzes the first rate-limiting reaction in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f5e97463c3297ad78cedf781e5fc3734
https://doi.org/10.1007/s13530-021-00092-8
https://doi.org/10.1007/s13530-021-00092-8