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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 ISSN 0002-7863.

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Official URL: http://dx.doi.org/10.1021/jacs.7b09899

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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
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Science, Engineering and Medicine > 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:
DateEvent
4 December 2017Published
9 November 2017Accepted
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
Date of first compliant deposit: 15 December 2017
Date of first compliant Open Access: 4 December 2018
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
GM097142National Institutes of Healthhttp://dx.doi.org/10.13039/100000002
Chemistry–Biology Interface Training ProgramNational Institute of General Medical Scienceshttp://dx.doi.org/10.13039/100000057
UNSPECIFIEDUniversity of Illinois (Urbana-Champaign campus). Department of Chemistry and Chemical Engineeringhttps://viaf.org/viaf/131965017
Wolfson Research Merit Award (WM130033)Royal Societyhttp://dx.doi.org/10.13039/501100000288

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