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In vitro biosynthetic studies of bottromycin expand the enzymatic capabilities of the YcaO superfamily
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Schwalen, Christopher J., Hudson, Graham A., Kosol, Simone, Mahanta, Nilkamal, Challis, Gregory L. and Mitchell, Douglas A. (2017) In vitro biosynthetic studies of bottromycin expand the enzymatic capabilities of the YcaO superfamily. Journal of the American Chemical Society, 139 (50). pp. 18154-18157. doi:10.1021/jacs.7b09899
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WRAP-in-vitro-biosynthetic-studies-bottromycin-expand-enzymatic-capabilities-Challis-2017.pdf - Accepted Version - Requires a PDF viewer. Download (886Kb) | Preview |
Official URL: http://dx.doi.org/10.1021/jacs.7b09899
Abstract
The bottromycins belong to the ribosomally synthesized and posttranslationally modified peptide (RiPP) family of natural products. Bottromycins exhibit unique structural features, including a hallmark macrolactamidine ring and thiazole heterocycle for which divergent members of the YcaO superfamily have been biosynthetically implicated. Here we report the in vitro reconstitution of two YcaO proteins, BmbD and BmbE, responsible for the ATP-dependent cyclodehydration reactions that yield thiazoline- and macrolactamidine-functionalized products, respectively. We also establish the substrate tolerance for BmbD and BmbE and systematically dissect the role of the follower peptide, which we show serves a purpose similar to canonical leader peptides in directing the biosynthetic enzymes to the substrate. Lastly, we leverage the expanded capabilities of YcaO proteins to conduct an extensive bioinformatic survey to classify known YcaO chemistry. This analysis predicts new functions remain to be uncovered within the superfamily.
| Item Type: | Journal Article | |||||||||||||||
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| Subjects: | Q Science > QD Chemistry | |||||||||||||||
| Divisions: | Faculty of Science > Chemistry | |||||||||||||||
| Library of Congress Subject Headings (LCSH): | Peptides -- Synthesis, Biosynthesis, Chemistry, Organic | |||||||||||||||
| Journal or Publication Title: | Journal of the American Chemical Society | |||||||||||||||
| Publisher: | American Chemical Society | |||||||||||||||
| ISSN: | 0002-7863 | |||||||||||||||
| Official Date: | 4 December 2017 | |||||||||||||||
| Dates: |
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| Volume: | 139 | |||||||||||||||
| Number: | 50 | |||||||||||||||
| Page Range: | pp. 18154-18157 | |||||||||||||||
| DOI: | 10.1021/jacs.7b09899 | |||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||
| Publication Status: | Published | |||||||||||||||
| Access rights to Published version: | Restricted or Subscription Access | |||||||||||||||
| RIOXX Funder/Project Grant: |
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