ArticleACS catalysis2021
The Peptide Ligase Activity of Human Legumain Depends on Fold Stabilization and Balanced Substrate Affinities.
Article in ACS catalysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Constrained diffusion-enabled construction of a highly expressed and robust peptide asparaginyl ligase.Chemical science · 2026Article
- Positional scanning and computational modeling reveal determinants of legumain transpeptidase activity.Protein science : a publication of the Protein Society · 2026Article
- Data Processing and Analysis in Positional Proteomics.Proteomics · 2025Review
- Polyphenols fromPharmaceutics · 2025Article
- Roles of C/EBPβ/AEP in Neurodegenerative Diseases.Current topics in medicinal chemistry · 2025Review
- Phytocystatin 6 is a context-dependent, tight-binding inhibitor of Arabidopsis thaliana legumain isoform β.The Plant journal : for cell and molecular biology · 2023Article
- Unambiguous Identification of Glucose-Induced Glycation in mAbs and other Proteins by NMR Spectroscopy.Pharmaceutical research · 2023Article
- On the design of a constitutively active peptide asparaginyl ligase for facile protein conjugation.FEBS open bio · 2023Article
- Mutations in α-synuclein, TDP-43 and tau prolong protein half-life through diminished degradation by lysosomal proteases.Molecular neurodegeneration · 2023Article
- Structural basis for proenzyme maturation, substrate recognition, and ligation by a hyperactive peptide asparaginyl ligase.The Plant cell · 2022Article
- Legumain Activity Is Controlled by Extended Active Site Residues and Substrate Conformation.International journal of molecular sciences · 2022Article
- Structural and functional studies of legumain-mycocypin complexes revealed a competitive, exosite-regulated mode of interaction.The Journal of biological chemistry · 2022Article
- The Asparaginyl Endopeptidase Legumain: An Emerging Therapeutic Target and Potential Biomarker for Alzheimer's Disease.International journal of molecular sciences · 2022Review
- Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein modification by enzymatic breaking and forming of peptide bonds significantly expands the repertoire of genetically encoded protein sequences. The dual protease-ligase legumain exerts the two opposing activities within a single protein scaffold. Primarily localized to the endolysosomal system, legumain represents a key enzyme in the generation of antigenic peptides for subsequent presentation on the MHCII complex. Here we show that human legumain catalyzes the ligation and cyclization of linear peptides at near-neutral pH conditions, where legumain is intrinsically unstable. Conformational stabilization significantly enhanced legumain's ligase activity, which further benefited from engineering the prime substrate recognition sites for improved affinity. Additionally, we provide evidence that specific legumain activation states allow for differential regulation of its activities. Together these results set the basis for engineering legumain proteases and ligases with applications in biotechnology and drug development.
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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.