期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 85, 期 1, 页码 97-102出版社
OXFORD UNIV PRESS
DOI: 10.1093/bbb/zbaa011
关键词
heterologous production; biosynthesis; peptide; protease inhibitor; marinostatin
类别
资金
- Japan Society for the Promotion of Science [20K05848]
- Koyanagi Foundation [19060023]
- Grants-in-Aid for Scientific Research [20K05848] Funding Source: KAKEN
In this study, a new analogous peptide named marinostatin E was successfully produced using Escherichia coli, exhibiting inhibitory activities against chymotrypsin and subtilisin. The structure of marinostatin E was determined through chemical treatments and tandem mass spectrometry experiments.
Bicyclic peptides, marinostatins, are protease inhibitors derived from the marine bacterium Algicola sagamiensis. The biosynthetic gene cluster of marinostatin was previously identified, although no heterologous production was reported. In this report, the biosynthetic gene cluster of marinostatin (mstA and mstB) was cloned into the expression vector pET-41a(+). As a result of the coexpression experiment, a new analogous peptide named marinostatin E was successfully produced using Escherichia coli BL21(DE3). The structure of marinostatin E was determined by a combination of chemical treatments and tandem mass spectrometry experiments. Marinostatin E exhibited inhibitory activities against chymotrypsin and subtilisin with an IC50 of 4.0 and 39.6 mu m, respectively.
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