ArticleNature communications2018
Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 127 citations in OpenAlex.
- Mining of natural diversity enables efficient and expressible peptide asparaginyl ligases.Nature communications · 2026Article
- Protein engineering strategies to optimise recombinant product synthesis and accumulation in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Identification and functional analysis of novel precursor genes in cyclic peptide biosynthesis in Pseudostellaria heterophylla.BMC plant biology · 2025Article
- Metabolite Mediated Protein Macrocyclization.Synlett : accounts and rapid communications in synthetic organic chemistry · 2025Article
- Review
- Yeast as a tool for exploring disulfide-rich peptides.FEMS yeast research · 2025Review
- Updates in Alzheimer's disease: from basic research to diagnosis and therapies.Translational neurodegeneration · 2024Review
- Enhancing the Intrinsic Antiplasmodial Activity and Improving the Stability and Selectivity of a Tunable Peptide Scaffold Derived from Human Platelet Factor 4.ACS infectious diseases · 2024Article
- Hijacking of N-fixing legume albumin-1 genes enables the cyclization and stabilization of defense peptides.Nature communications · 2024Article
- Plant peptides - redefining an area of ribosomally synthesized and post-translationally modified peptides.Natural product reports · 2024Review
- Design of a recombinant asparaginyl ligase for site-specific modification using efficient recognition and nucleophile motifs.Communications chemistry · 2024Article
- Selective Late-Stage Functionalization of Tryptophan-Containing Peptides To Facilitate Bioorthogonal Tetrazine Ligation.Organic letters · 2024Article
- C-terminal modification and functionalization of proteins via a self-cleavage tag triggered by a small molecule.Nature communications · 2023Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- On the design of a constitutively active peptide asparaginyl ligase for facile protein conjugation.FEBS open bio · 2023Article
- Plant-based production of an orally active cyclotide for the treatment of multiple sclerosis.Transgenic research · 2023Article
- Self-cyclisation as a general and efficient platform for peptide and protein macrocyclisation.Communications chemistry · 2023Article
- Vacuolar Processing Enzymes in Plant Programmed Cell Death and Autophagy.International journal of molecular sciences · 2023Review
- Structural basis for proenzyme maturation, substrate recognition, and ligation by a hyperactive peptide asparaginyl ligase.The Plant cell · 2022Article
- Rational domestication of a plant-based recombinant expression system expands its biosynthetic range.Journal of experimental botany · 2022Article
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Asparaginyl endopeptidases (AEPs) are proteases that have crucial roles in plant defense and seed storage protein maturation. Select plant AEPs, however, do not function as proteases but as transpeptidases (ligases) catalyzing the intra-molecular ligation of peptide termini, which leads to peptide cyclization. These ligase-type AEPs have potential biotechnological applications ranging from in vitro peptide engineering to plant molecular farming, but the structural features enabling these enzymes to catalyze peptide ligation/cyclization rather than proteolysis are currently unknown. Here, we compare the sequences, structures, and functions of diverse plant AEPs by combining molecular modeling, sequence space analysis, and functional testing in planta. We find that changes within the substrate-binding pocket and an adjacent loop, here named the "marker of ligase activity", together play a key role for AEP ligase efficiency. Identification of these structural determinants may facilitate the discovery of more ligase-type AEPs and the engineering of AEPs with tailored catalytic properties.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.