A suite of kinetically superior AEP ligases can cyclise an intrinsically disordered protein.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
25 07 2019
25 07 2019
Historique:
received:
24
05
2019
accepted:
11
07
2019
entrez:
27
7
2019
pubmed:
28
7
2019
medline:
22
10
2020
Statut:
epublish
Résumé
Asparaginyl endopeptidases (AEPs) are a class of enzymes commonly associated with proteolysis in the maturation of seed storage proteins. However, a subset of AEPs work preferentially as peptide ligases, coupling release of a leaving group to formation of a new peptide bond. These "ligase-type" AEPs require only short recognition motifs to ligate a range of targets, making them useful tools in peptide and protein engineering for cyclisation of peptides or ligation of separate peptides into larger products. Here we report the recombinant expression, ligase activity and cyclisation kinetics of three new AEPs from the cyclotide producing plant Oldenlandia affinis with superior kinetics to the prototypical recombinant AEP ligase OaAEP1
Identifiants
pubmed: 31346249
doi: 10.1038/s41598-019-47273-7
pii: 10.1038/s41598-019-47273-7
pmc: PMC6658665
doi:
Substances chimiques
Antigens, Protozoan
0
Intrinsically Disordered Proteins
0
Plant Proteins
0
Protozoan Proteins
0
Recombinant Proteins
0
merozoite surface protein 2, Plasmodium
0
Cysteine Endopeptidases
EC 3.4.22.-
asparaginylendopeptidase
EC 3.4.22.34
Ligases
EC 6.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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