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• W1699671485 startingPage "571" @default.
• W1699671485 abstract "Proteases usually cleave peptides, but under some conditions, they can ligate them. Seeds of the common sunflower contain the 14-residue, backbone-macrocyclic peptide sunflower trypsin inhibitor 1 (SFTI-1) whose maturation from its precursor has a genetic requirement for asparaginyl endopeptidase (AEP). To provide more direct evidence, we developed an in situ assay and used (18)O-water to demonstrate that SFTI-1 is excised and simultaneously macrocyclized from its linear precursor. The reaction is inefficient in situ, but a newfound breakdown pathway can mask this inefficiency by reducing the internal disulfide bridge of any acyclic-SFTI to thiols before degrading it. To confirm AEP can directly perform the excision/ligation, we produced several recombinant plant AEPs in E. coli, and one from jack bean could catalyze both a typical cleavage reaction and cleavage-dependent, intramolecular transpeptidation to create SFTI-1. We propose that the evolution of ligating endoproteases enables plants like sunflower and jack bean to stabilize bioactive peptides." @default.
• W1699671485 created "2016-06-24" @default.
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• W1699671485 date "2015-05-01" @default.
• W1699671485 modified "2023-10-16" @default.
• W1699671485 title "Peptide Macrocyclization by a Bifunctional Endoprotease" @default.
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• W1699671485 doi "https://doi.org/10.1016/j.chembiol.2015.04.010" @default.
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