ArticleJournal of the American Chemical Society2019
Complete Stereoinversion of l-Tryptophan by a Fungal Single-Module Nonribosomal Peptide Synthetase.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Discovery of Fusadapamides, Accessory Chromosome-Associated Metabolites Incorporating l-2,3-Diaminopropionic Acid inJournal of natural products · 2025Article
- Structure, Function and Engineering of the Nonribosomal Peptide Synthetase Condensation Domain.International journal of molecular sciences · 2024Review
- The sugar cube: Network control and emergence in stereoediting reactions.Science (New York, N.Y.) · 2024Article
- Metabolomics-Guided Discovery, Isolation, Structure Elucidation, and Bioactivity of Myropeptins C-E fromJournal of natural products · 2023Article
- Characterization and catalytic investigation of fungal single-module nonribosomal peptide synthetase in terpene-amino acid meroterpenoid biosynthesis.Journal of industrial microbiology & biotechnology · 2023Article
- Unexpected assembly machinery for 4(3H)-quinazolinone scaffold synthesis.Nature communications · 2022Article
- Understanding and Circumventing the Requirement for Native Thioester Substrates for α-Oxoamine Synthase Reactions.ACS chemical biology · 2022Article
- Bacterial-Like Nonribosomal Peptide Synthetases Produce Cyclopeptides in the Zygomycetous Fungus Mortierella alpina.Applied and environmental microbiology · 2021Article
- Fungal siderophore biosynthesis catalysed by an iterative nonribosomal peptide synthetase.Chemical science · 2020Article
- Mass Spectrometry Guided Discovery and Design of Novel Asperphenamate Analogs FromFrontiers in microbiology · 2020Article
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Authors and funding
3 authors.
Funding
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.
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