ArticleComputational and structural biotechnology journal2021
From thiol-subtilisin to omniligase: Design and structure of a broadly applicable peptide ligase.
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Aqueous-Phase Peptide Synthesis via Stepwise Amino Acid Elongation Catalyzed by Aqualigase.ACS organic & inorganic Au · 2026Article
- Do We Still Need Chemistry for Water-Soluble Prodrugs? What Biocatalysis Already Does, and What It Does Not.Pharmaceutics · 2026Review
- Targeted drug conjugates and molecular mechanisms in overcoming lung cancer drug resistance.Discover oncology · 2025Review
- Toward single-molecule protein sequencing using nanopores.Nature biotechnology · 2025Review
- Site-Specific Glyco-Tagging of Native Proteins for the Development of Biologicals.Journal of the American Chemical Society · 2024Article
- AbAMPdb: a database of Acinetobacter baumannii specific antimicrobial peptides.Database : the journal of biological databases and curation · 2024Article
- Towards controlling activity of a peptide asparaginyl ligase (PAL) by lumazine synthetase compartmentalization.Faraday discussions · 2024Article
- Drug conjugates for the treatment of lung cancer: from drug discovery to clinical practice.Experimental hematology & oncology · 2024Review
- Insights into the synthesis strategies of plant-derived cyclotides.Amino acids · 2023Review
- Nature-inspired protein ligation and its applications.Nature reviews. Chemistry · 2023Review
- Biologic Evaluation of a Heterodimeric HER2-Albumin Targeted Affibody Molecule Produced by Chemo-Enzymatic Peptide Synthesis.Pharmaceutics · 2022Article
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Authors and funding
9 authors.
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Abstract
Omniligase-1 is a broadly applicable enzyme for peptide bond formation between an activated acyl donor peptide and a non-protected acyl acceptor peptide. The enzyme is derived from an earlier subtilisin variant called peptiligase by several rounds of protein engineering aimed at increasing synthetic yields and substrate range. To examine the contribution of individual mutations on S/H ratio and substrate scope in peptide synthesis, we selected peptiligase variant M222P/L217H as a starting enzyme and introduced successive mutations. Mutation A225N in the S1' pocket and F189W of the S2' pocket increased the synthesis to hydrolysis (S/H) ratio and overall coupling efficiency, whereas the I107V mutation was added to S4 pocket to increase the reaction rate. The final omniligase variants appeared to have a very broad substrate range, coupling more than 250 peptides in a 400-member library of acyl acceptors, as indicated by a high-throughput FRET assay. Crystal structures and computational modelling could rationalize the exceptional properties of omniligase-1 in peptide synthesis.
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