ArticleAngewandte Chemie (International ed. in English)2022
Enzymatic C-to-C Protein Ligation.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Protein engineering strategies to optimise recombinant product synthesis and accumulation in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Asparaginyl Ligases with Engineered Substrate Specificity for Controlled, Sequential Transpeptidation Reactions.Journal of the American Chemical Society · 2025Article
- Highly Efficient Transpeptidase-Catalyzed Isopeptide Ligation.Journal of the American Chemical Society · 2025Article
- An efficient and easily obtainable butelase variant for chemoenzymatic ligation and modification of peptides and proteins.Microbial cell factories · 2024Article
- Tertiary amide bond formation by an engineered asparaginyl ligase.Chemical science · 2024Article
- Biocompatible strategies for peptide macrocyclisation.Chemical science · 2024Review
- Enzymatic Protein Immobilization for Nanobody Array.Molecules (Basel, Switzerland) · 2024Article
- OaAEP1 Ligase-Assisted Chemoenzymatic Synthesis of Full Cysteine-Rich Metal-Binding Cyanobacterial Metallothionein SmtA.Bioconjugate chemistry · 2023Article
- Strategies for Conditional Regulation of Proteins.JACS Au · 2023Review
- Enzymatic Protein Immobilization on Amino-Functionalized Nanoparticles.Molecules (Basel, Switzerland) · 2023Article
- Chemical and Enzymatic Methods for Post-Translational Protein-Protein Conjugation.Journal of the American Chemical Society · 2022Review
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- Enzymatic C-to-C Protein Ligation.Angewandte Chemie (International ed. in English) · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transpeptidase-catalyzed protein and peptide modifications have been widely utilized for generating conjugates of interest for biological investigation or therapeutic applications. However, all known transpeptidases are constrained to ligating in the N-to-C orientation, limiting the scope of attainable products. Here, we report that an engineered asparaginyl ligase accepts diverse incoming nucleophile substrate mimetics, particularly when a means of selectively quenching the reactivity of byproducts released from the recognition sequence is employed. In addition to directly catalyzing formation of l-/d- or α-/β-amino acid junctions, we find C-terminal Leu-ethylenediamine (Leu-Eda) motifs to be bona fide mimetics of native N-terminal Gly-Leu sequences. Appending a C-terminal Leu-Eda to synthetic peptides or, via an intein-splicing approach, to recombinant proteins enables direct transpeptidase-catalyzed C-to-C ligations. This work significantly expands the synthetic scope of enzyme-catalyzed protein transpeptidation reactions.
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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.