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Complete stereoinversion of L-tryptophan by a fungal single module nonribosomal peptide synthetase
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Hai, Yang, Jenner, Matthew and Tang, Yi (2019) Complete stereoinversion of L-tryptophan by a fungal single module nonribosomal peptide synthetase. Journal of the American Chemical Society, 141 (41). pp. 16222-16226. doi:10.1021/jacs.9b08898 ISSN 0002-7863.
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WRAP-complete-stereoinversion-L-tryptophan-fungal-single-module-nonribosomal-peptide-syntetase-Jenner-2019.pdf - Accepted Version - Requires a PDF viewer. Download (1097Kb) | Preview |
Official URL: http://dx.doi.org/10.1021/jacs.9b08898
Abstract
Single-module nonribosomal peptide synthetases (NRPSs) and NRPS-like enzymes activate and transform carboxylic acids in both primary and secondary metabolism and are of great interest due to their biocatalytic potentials. The single-module NRPS IvoA is essential for fungal pigment biosynthesis. Here, we show that IvoA catalyzes ATP-dependent unidirectional stereoinversion of l-tryptophan to d-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain, the terminal condensation (C) domain stereoselectively hydrolyzes d-tryptophanyl-S-phosphopantetheine thioester and thus represents a noncanonical C domain function. Using IvoA, we demonstrate a biocatalytic stereoinversion/deracemization route to access a variety of substituted d-tryptophan analogs in high enantiomeric excess.
| Item Type: | Journal Article | |||||||||||||||
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| Subjects: | Q Science > QP Physiology T Technology > TP Chemical technology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | |||||||||||||||
| Library of Congress Subject Headings (LCSH): | Enzymes, Peptides, Tryptophan, Fungi -- Biotechnology | |||||||||||||||
| Journal or Publication Title: | Journal of the American Chemical Society | |||||||||||||||
| Publisher: | American Chemical Society | |||||||||||||||
| ISSN: | 0002-7863 | |||||||||||||||
| Official Date: | 16 October 2019 | |||||||||||||||
| Dates: |
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| Volume: | 141 | |||||||||||||||
| Number: | 41 | |||||||||||||||
| Page Range: | pp. 16222-16226 | |||||||||||||||
| DOI: | 10.1021/jacs.9b08898 | |||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||
| Publication Status: | Published | |||||||||||||||
| Reuse Statement (publisher, data, author rights): | This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/jacs.9b08898 | |||||||||||||||
| Access rights to Published version: | Restricted or Subscription Access | |||||||||||||||
| Date of first compliant deposit: | 11 November 2019 | |||||||||||||||
| Date of first compliant Open Access: | 1 October 2020 | |||||||||||||||
| RIOXX Funder/Project Grant: |
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