Journal article icon

Journal article

Kinetic landscape of a peptide bond-forming prolyl oligopeptidase

Abstract:

Prolyl oligopeptidase B from Galerina marginata (GmPOPB) has recently been discovered as a peptidase capable of breaking and forming peptide bonds to yield a cyclic peptide. Despite the relevance of prolyl oligopeptidases in human biology and disease, a kinetic analysis pinpointing rate-limiting steps for a member of this enzyme family is not available. Macrocyclase enzymes are currently exploited to produce cyclic peptides with potential therapeutic applications. Cyclic peptides are promisin...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed

Actions


Access Document


Files:
Publisher copy:
10.1021/acs.biochem.7b00012

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Role:
Author
More from this funder
Funding agency for:
Naismith, J
More from this funder
Funding agency for:
Naismith, J
Publisher:
American Chemical Society Publisher's website
Journal:
Biochemistry Journal website
Volume:
56
Issue:
15
Pages:
2086-2095
Publication date:
2017-04-18
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
Source identifiers:
699003
Language:
English
Keywords:
Pubs id:
pubs:699003
UUID:
uuid:4836b32a-f8ce-40b5-ad1c-58a8e79f7956
Local pid:
pubs:699003
Deposit date:
2017-07-13

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP