Identification of the peptide epimerase MslH responsible for d-amino acid introduction at the C-terminus of ribosomal peptides
Author:
Affiliation:
1. Graduate School of Chemical Sciences and Engineering
2. Hokkaido University
3. Sapporo
4. Japan
5. Graduate School of Engineering
Abstract
The biosynthesis of d-tryptophan containing lasso peptide MS-271 involves the epimerization of a ribosomal peptide MslA catalyzed by a novel class of metal- and cofactor-independent peptide epimerase MslH.
Funder
Japan Society for the Promotion of Science
Hokkaido University
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2021/SC/D0SC06308H
Reference34 articles.
1. Lasso peptides: structure, function, biosynthesis, and engineering
2. Lasso Peptides: An Intriguing Class of Bacterial Natural Products
3. Genome mining for lasso peptides: past, present, and future
4. Cryptand-imidazolium supported total synthesis of the lasso peptide BI-32169 and its d-enantiomer
5. Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature
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1. Peptide Epimerase Responsible for d-Amino Acid Introduction in Poly-γ-glutamic Acid Biosynthesis;Biomacromolecules;2023-12-14
2. Structural and functional analysis of hyper-thermostable ancestral L-amino acid oxidase that can convert Trp derivatives to D-forms by chemoenzymatic reaction;Communications Chemistry;2023-09-22
3. Structure of lasso peptide epimerase MslH reveals metal-dependent acid/base catalytic mechanism;Nature Communications;2023-08-08
4. Peptide epimerase-dehydratase complex responsible for biosynthesis of the linaridin class ribosomal peptides;Bioscience, Biotechnology, and Biochemistry;2023-08-04
5. Leader peptide removal in lasso peptide biosynthesis based on penultimate isoleucine residue;Frontiers in Microbiology;2023-07-10
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