A suite of kinetically superior AEP ligases can cyclise an intrinsically disordered protein.

ABSTRACT: 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_b. These AEPs work preferentially as ligases at

SUBMITTER: Harris KS 

PROVIDER: S-EPMC6658665 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature