ArticleScientific reports2019
A suite of kinetically superior AEP ligases can cyclise an intrinsically disordered protein.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 60 citations in OpenAlex.
- Transcriptome-guided discovery and active-site gatekeeper engineering of a Viola arcuata asparaginyl ligase with superior catalytic performance.The Journal of biological chemistry · 2026Article
- Metabolite Mediated Protein Macrocyclization.Synlett : accounts and rapid communications in synthetic organic chemistry · 2025Article
- An efficient and easily obtainable butelase variant for chemoenzymatic ligation and modification of peptides and proteins.Microbial cell factories · 2024Article
- Towards controlling activity of a peptide asparaginyl ligase (PAL) by lumazine synthetase compartmentalization.Faraday discussions · 2024Article
- Design of a recombinant asparaginyl ligase for site-specific modification using efficient recognition and nucleophile motifs.Communications chemistry · 2024Article
- Intracellular Application of an Asparaginyl Endopeptidase for Producing Recombinant Head-to-Tail Cyclic Proteins.JACS Au · 2023Article
- Calcium-assisted sortase A cleavage of SUMOylated metallothionein constructs leads to high-yield production of human MT3.Microbial cell factories · 2023Article
- 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
- 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
- Peptide/protein-based macrocycles: from biological synthesis to biomedical applications.RSC chemical biology · 2022Review
- Scalable and Efficient In Planta Biosynthesis of Sunflower Trypsin Inhibitor-1 (SFTI) Peptide Therapeutics.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The legumain McPAL1 from Momordica cochinchinensis is a highly stable Asx-specific splicing enzyme.The Journal of biological chemistry · 2021Article
- Evaluation of Efficient Non-reducing Enzymatic and Chemical Ligation Strategies for Complex Disulfide-Rich Peptides.Bioconjugate chemistry · 2021Article
- Direct N- or C-Terminal Protein Labeling Via a Sortase-Mediated Swapping Approach.Bioconjugate chemistry · 2021Article
- Bioconjugation Strategies for Connecting Proteins to DNA-Linkers for Single-Molecule Force-Based Experiments.Nanomaterials (Basel, Switzerland) · 2021Review
- Protein Macrocyclization for Tertiary Structure Stabilization.Chembiochem : a European journal of chemical biology · 2021Review
- Structural and biochemical analyses of concanavalin A circular permutation by jack bean asparaginyl endopeptidase.The Plant cell · 2021Article
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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
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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.