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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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Publisher copy:
10.1021/acschembio.8b00050

Authors


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Role:
Author
ORCID:
0000-0002-7163-4057
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Name:
European Research Council
Grant:
339367 NCB-TNT
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Name:
Biotechnology and Biological Sciences Research Council
Publisher:
American Chemical Society
Journal:
ACS Chemical Biology More from this journal
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
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

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