A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors.
Amino Acid Sequence
Biocatalysis
Cyclization
Cysteine Endopeptidases
/ metabolism
Hydrogen-Ion Concentration
Kinetics
Models, Molecular
Peptides, Cyclic
/ chemistry
Plant Proteins
/ metabolism
Protein Engineering
Recombinant Proteins
/ metabolism
Substrate Specificity
Trypsin Inhibitors
/ metabolism
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
27 03 2020
27 03 2020
Historique:
received:
30
09
2019
accepted:
06
03
2020
entrez:
30
3
2020
pubmed:
30
3
2020
medline:
16
7
2020
Statut:
epublish
Résumé
Asparaginyl endopeptidases (AEPs) catalyze the key backbone cyclization step during the biosynthesis of plant-derived cyclic peptides. Here, we report the identification of two AEPs from Momordica cochinchinensis and biochemically characterize MCoAEP2 that catalyzes the maturation of trypsin inhibitor cyclotides. Recombinantly produced MCoAEP2 catalyzes the backbone cyclization of a linear cyclotide precursor (MCoTI-II-NAL) with a k
Identifiants
pubmed: 32221295
doi: 10.1038/s41467-020-15418-2
pii: 10.1038/s41467-020-15418-2
pmc: PMC7101308
doi:
Substances chimiques
Peptides, Cyclic
0
Plant Proteins
0
Recombinant Proteins
0
Trypsin Inhibitors
0
Cysteine Endopeptidases
EC 3.4.22.-
asparaginylendopeptidase
EC 3.4.22.34
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1575Références
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