ArticleFrontiers in chemistry2021
Site-Specific Protein Modifications by an Engineered Asparaginyl Endopeptidase from
Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Constrained diffusion-enabled construction of a highly expressed and robust peptide asparaginyl ligase.Chemical science · 2026Article
- Mining of natural diversity enables efficient and expressible peptide asparaginyl ligases.Nature communications · 2026Article
- Transcriptome-guided discovery and active-site gatekeeper engineering of a Viola arcuata asparaginyl ligase with superior catalytic performance.The Journal of biological chemistry · 2026Article
- Article
- Hololectin Interdomain Linker Determines Asparaginyl Endopeptidase-Mediated Maturation of Antifungal Hevein-Like Peptides in Oats.Frontiers in plant science · 2022Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Asparaginyl endopeptidases (AEPs) or legumains are Asn/Asp (Asx)-specific proteases that break peptide bonds, but also function as peptide asparaginyl ligases (PALs) that make peptide bonds. This ligase activity can be used for site-specific protein modifications in biochemical and biotechnological applications. Although AEPs are common, PALs are rare. We previously proposed ligase activity determinants (LADs) of these enzymes that could determine whether they catalyze formation or breakage of peptide bonds. LADs are key residues forming the S2 and S1' substrate-binding pockets flanking the S1 active site. Here, we build on the LAD hypothesis with the engineering of ligases from proteases by mutating the S2 and S1' pockets of VcAEP, an AEP from
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