Journal article
Characterization of the fast and promiscuous macrocyclase from plant PCY1 enables the use of simple substrates
- Abstract:
-
Cyclic ribosomally derived peptides possess diverse bioactivities and are currently of major interest in drug development. However, it can be chemically challenging to synthesize these molecules, hindering the diversification and testing of cyclic peptide leads. Enzymes used in vitro offer a solution to this; however peptide macrocyclization remains the bottleneck. PCY1, involved in the biosynthesis of plant orbitides, belongs to the class of prolyl oligopeptidases and natively displays subst...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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Authors
Funding
Biotechnology and Biological Sciences Research Council
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Bibliographic Details
- Publisher:
- American Chemical Society Publisher's website
- Journal:
- ACS Chemical Biology Journal website
- Volume:
- 13
- Issue:
- 3
- Pages:
- 801–811
- Publication date:
- 2018-01-29
- Acceptance date:
- 2018-01-29
- DOI:
- EISSN:
-
1554-8937
- ISSN:
-
1554-8929
- Pmid:
-
29377663
Item Description
- Language:
- English
- Pubs id:
-
pubs:822599
- UUID:
-
uuid:8d9c9797-0888-42f8-a2e6-d80d69982f26
- Local pid:
- pubs:822599
- Source identifiers:
-
822599
- Deposit date:
- 2018-03-01
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2018
- Notes:
- Copyright © 2018 American Chemical Society. This is the accepted manuscript version of the article. The final version is available online from American Chemical Society at: https://doi.org/10.1021/acschembio.8b00050
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