Identification of the peptide epimerase MslH responsible for d-amino acid introduction at the C-terminus of ribosomal peptides

Feng, Zhi; Ogasawara, Yasushi; Dairi, Tohru

doi:10.1039/d0sc06308h


Hokkaido University \| Library \| HUSCAP	Advanced Search		言語

	Home
	About HUSCAP
	Open Access Policy

	Browse by Author

Browse
	Communities & Collections

	Scholarly Journals
	Theses
	Doctoral Dissertations Listed by Graduate Schools
	Conference Procs.
	Events

	HUSCAP Senior (in Japanese)

	Societies

	Downloads (country)

For university staff
	How to post your papers to HUSCAP
	Publication of theses
	Helpline about theses publication

Open Archives Compliant

You can search our collection also at:
	Google
	Google Scholar
	CiNii
	IRDB
	OAIster
	NDLTD

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Engineering / Faculty of Engineering >
Peer-reviewed Journal Articles, etc >

Identification of the peptide epimerase MslH responsible for d-amino acid introduction at the C-terminus of ribosomal peptides

This item is licensed under:Creative Commons Attribution-NonCommercial 3.0 Unported

Files in This Item:

The file(s) associated with this item can be obtained from the following URL: https://doi.org/10.1039/d0sc06308h

Title:	Identification of the peptide epimerase MslH responsible for d-amino acid introduction at the C-terminus of ribosomal peptides
Authors:	Feng, Zhi Browse this author
	Ogasawara, Yasushi Browse this author →KAKEN DB
	Dairi, Tohru Browse this author →KAKEN DB
Issue Date:	21-Feb-2021
Publisher:	Royal Society of Chemistry
Journal Title:	Chemical science
Volume:	12
Issue:	7
Start Page:	2567
End Page:	2574
Publisher DOI:	10.1039/d0sc06308h
Abstract:	A lasso peptide MS-271 is a ribosomally synthesized and post-translationally modified peptide (RiPP) consisting of 21 amino acids with a d-tryptophan (Trp) at its C terminus. The presence of d-amino acids is rare in RiPPs and few mechanisms of d-amino acid introduction have been characterized. Here, we report the identification of MslH, previously annotated as a hypothetical protein, as a novel epimerase involved in the post-translational epimerization of the C-terminal Trp residue of the precursor peptide MslA. MslH is the first epimerase that catalyzes epimerization at the C-alpha center adjacent to a carboxylic acid in a cofactor-independent manner. We also demonstrate that MslH exhibits broad substrate specificity toward the N-terminal region of the core peptide, showing that MslH-type epimerases offer opportunities in peptide bioengineering.
Rights:	https://creativecommons.org/licenses/by-nc/3.0/
Type:	article
URI:	http://hdl.handle.net/2115/81030
Appears in Collections:	工学院・工学研究院 (Graduate School of Engineering / Faculty of Engineering) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

OAI-PMH ( junii2 , jpcoar_1.0 )

- Hokkaido University