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B6db references: 26854280

type Journal Article
authors Wang Y, Wang J, Yu S, Wang F, Ma H, Yue C, Liu M, Deng Z, Huang Y, Qu X.

title Identifying the Minimal Enzymes for Unusual Carbon-Sulfur Bond Formation in Thienodolin Biosynthesis.
journal Chembiochem.
Activity thnj
Family thnj
sel selected
ui 26854280
year (2016)
volume 17
number 9
pages 799-803
abstract Thienodolin (THN) features a tricyclic indole-S-hetero scaffold that encompasses two unique carbon-sulfur bonds. Although its biosynthetic gene cluster has been recently identified in Streptomyces albogriseolus, the essential enzymes for the formation of C-S bonds have been relatively unexplored. Here, we isolated and characterized a new biosynthetic gene cluster from Streptomyces sp. FXJ1.172. Heterologous expression, systematic gene inactivation, and in vitro biochemical characterization enable us to determine the minimum set of genes for THN synthesis, and an aminotransferase (ThnJ) for catalyzing the downstream conversion of tryptophan chlorination. In addition, we evaluated (and mainly excluded) a previously assumed pivotal intermediate by feeding experiments. With these results, we narrowed down four enzymes (ThnC-F) that are responsible for the two unprecedented C-S bond formations. Our study provides a solid basis for further unraveling of the unique C-S mechanisms.
last changed 2018/03/27 10:13

B6db references