English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
 Local TagsRelease HistoryDetailsSummary
  Redesign of substrate selection in glycopeptide antibiotic biosynthesis enables effective formation of alternate peptide backbones

Kaniusaite, M., Kittilä, T., Goode, R. J. A., Schittenhelm, R. B., & Cryle, M. J. (2020). Redesign of substrate selection in glycopeptide antibiotic biosynthesis enables effective formation of alternate peptide backbones. ACS Chemical Biology, 15(9), 2444-2455. doi:10.1021/acschembio.0c00435.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/21.11116/0000-0006-DF8E-0 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-D37B-1
Genre: Journal Article

Files

show Files
hide Files
:
ACSChemBiol_15_2020_2444.pdf (Any fulltext), 7MB
 
File Permalink:
-
Name:
ACSChemBiol_15_2020_2444.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
ACSChemBiol_15_2020_2444_Suppl.pdf (Supplementary material), 6MB
 
File Permalink:
-
Name:
ACSChemBiol_15_2020_2444_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
https://pubs.acs.org/doi/pdf/10.1021/acschembio.0c00435 (Any fulltext)
Description:
-
OA-Status:
Locator:
https://pubs.acs.org/doi/10.1021/acschembio.0c00435 (Any fulltext)
Description:
-
OA-Status:
Locator:
https://pubs.acs.org/doi/10.1021/acschembio.0c00435#article_content-right (Any fulltext)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Kaniusaite, Milda, Author
Kittilä, Tiia1, Author           
Goode, Robert J. A., Author
Schittenhelm, Ralf B., Author
Cryle, Max J., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: Peptides and proteins, Monomers, Biosynthesis, Assays, Selectivity
 Abstract: Nonribosomal peptide synthesis is capable of utilizing a wide range of amino acid residues due to the selectivity of adenylation (A)-domains. Changing the selectivity of A-domains could lead to new bioactive nonribosomal peptides, although remodeling efforts of A-domains are often unsuccessful. Here, we explored and successfully reengineered the specificity of the module 3 A-domain from glycopeptide antibiotic biosynthesis to change the incorporation of 3,5-dihydroxyphenylglycine into 4-hydroxyphenylglycine. These engineered A-domains remain selective in a functioning peptide assembly line even under substrate competition conditions and indicate a possible application of these for the future redesign of GPA biosynthesis.

Details

show
hide
Language(s): eng - English
 Dates: 2020-05-292020-08-142020-08-142020-09-18
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acschembio.0c00435
URI: https://pubmed.ncbi.nlm.nih.gov/32794694/
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: ACS Chemical Biology
  Abbreviation : ACS Chem. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 15 (9) Sequence Number: - Start / End Page: 2444 - 2455 Identifier: ISSN: 1554-8929
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000035040