@article{eb9080997cdf465cb4cf59ec76b7ee4e,
title = "Activation of a cryptic gene cluster in lysobacter enzymogenes reveals a module/domain portable mechanism of nonribosomal peptide synthetases in the biosynthesis of pyrrolopyrazines",
abstract = "Lysobacter are considered {"}peptide specialists{"}. However, many of the nonribosomal peptide synthetase genes are silent. Three new compounds were identified from L. enzymogenes upon activating the six-module-containing led cluster by the strong promoter PHSAF. Although ledD was the first gene under PHSAF control, the second gene ledE was expressed the highest. Targeted gene inactivation showed that the two-module LedE and the one-module LedF were selectively used in pyrrolopyrazine biosynthesis, revealing a module/domain portable mechanism.",
author = "Shanren Li and Xiuli Wu and Limei Zhang and Yuemao Shen and Liangcheng Du",
note = "Funding Information: This work was supported in part by the NSFC (31329005), NIH (R01AI097260), Nebraska Research Initiative, Faculty Seed Grant, and Taishan Scholars Program of Shandong Province. X.W. was partly supported by the China Scholarship Council. The authors are grateful to Dr. Guoliang Qian at Nanjing Agricultural University for the gift of HW strain and Drs. Martha Morton, Ronald Cerny, and Javier Seravalli at the University of NebraskaLincoln for technical assistance. Publisher Copyright: {\textcopyright} 2017 American Chemical Society.",
year = "2017",
month = oct,
day = "6",
doi = "10.1021/acs.orglett.7b01611",
language = "English (US)",
volume = "19",
pages = "5010--5013",
journal = "Organic Letters",
issn = "1523-7060",
publisher = "American Chemical Society",
number = "19",
}