An efficient and easily obtainable butelase variant for chemoenzymatic ligation and modification of peptides and proteins.

ABSTRACT: The expanding field of site-specific ligation of proteins and peptides has catalyzed the development of novel methods that enhance molecular modification. Among these methods, enzymatic strategies have emerged as dominant due to their specificity and efficiency in modifying proteins under mild conditions. Asparaginyl endopeptidase is a group of cyclotide-producing cysteine proteases from plants. These plant cysteine proteases, known for their specificity, effectively recognize the tripeptide motif (Asx-Xaa-Yaa) and cleave at the C-terminal side of Asx residues, forming acyl-enzyme intermediates that facilitate transpeptidation. Butelase 1 stands out as the most efficient AEP for protein engineering, yet challenges in its expression and purification limit its accessibility for widespread re

SUBMITTER: Singh AK 

PROVIDER: S-EPMC11607802 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature