Indolylamide Macrocyclization by a Streptococcus pneumoniae ThiF-like Enzyme Family Member

IF 5 1区化学 Q1 CHEMISTRY, ORGANIC

Organic Letters Pub Date : 2025-05-21 DOI:10.1021/acs.orglett.5c0156110.1021/acs.orglett.5c01561

Anshul Rajput, Keelie S. Butler, Daniel A. Springer and Jonathan R. Chekan*,

引用次数: 0

Abstract

ThiF-like enzymes are present in diverse RiPP biosynthetic pathways and are known to catalyze reactions such as thiolactone and phosphoramidate bond formation. To uncover new chemical space for ThiF-like enzymes, we utilized a global genome mining approach and identified a minimal ind RiPP cluster in the human pathogen Streptococcus pneumoniae. In vitro characterization of IndF demonstrated the first indolylamide (Trp-Ile) linkage in a RiPP pathway and a new reaction type catalyzed by a ThiF-like enzyme.

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肺炎链球菌thif样酶家族成员的吲哚酰胺大环化

thif样酶存在于多种RiPP生物合成途径中，已知可催化硫内酯和磷酰胺键形成等反应。为了揭示thif样酶的新化学空间，我们利用全球基因组挖掘方法，在人类病原体肺炎链球菌中鉴定了一个最小的ind RiPP簇。在体外鉴定中，发现了RiPP通路中的第一个吲哚酰胺（Trp-Ile）连锁，以及一种由thif样酶催化的新反应类型。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Organic Letters 化学-有机化学

CiteScore

9.30

自引率

11.50%

发文量

1607

审稿时长

1.5 months

期刊介绍： Organic Letters invites original reports of fundamental research in all branches of the theory and practice of organic, physical organic, organometallic,medicinal, and bioorganic chemistry. Organic Letters provides rapid disclosure of the key elements of significant studies that are of interest to a large portion of the organic community. In selecting manuscripts for publication, the Editors place emphasis on the originality, quality and wide interest of the work. Authors should provide enough background information to place the new disclosure in context and to justify the rapid publication format. Back-to-back Letters will be considered. Full details should be reserved for an Article, which should appear in due course.