ArticleChemical science2017
Broad substrate tolerance of tubulin tyrosine ligase enables one-step site-specific enzymatic protein labeling.
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 44 citations in OpenAlex.
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- Orthogonal Site-Specific Dual Bioconjugation of Aryl and Alkyl Thiols.Journal of the American Chemical Society · 2025Article
- Enhancing Sensitivity of Nuclear Magnetic Resonance in Biomolecules: Parahydrogen-Induced Hyperpolarization in Synthetic Disulfide-Rich Miniproteins.Journal of the American Chemical Society · 2024Article
- Cu-Catalyzed Azide-Alkyne-Thiol Reaction Forms Ubiquitous Background in Chemical Proteomic Studies.Journal of the American Chemical Society · 2024Article
- Review
- Chemical Proteomics Reveals Protein Tyrosination Extends Beyond the Alpha-Tubulins in Human Cells.Chembiochem : a European journal of chemical biology · 2022Article
- Site-Specific Antibody Fragment Conjugates for Reversible Staining in Fluorescence Microscopy.Chembiochem : a European journal of chemical biology · 2021Article
- Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020Review
- Frequent mutation of hypoxia-related genes in persistent pulmonary hypertension of the newborn.Respiratory research · 2020Article
- Single-Virus Tracking: From Imaging Methodologies to Virological Applications.Chemical reviews · 2020Review
- Recent progress in enzymatic protein labelling techniques and their applications.Chemical Society reviews · 2018Review
- Advancing the Frontiers of Chemical Protein Synthesis-The 7Cell chemical biology · 2018Article
- Nanobodies: Chemical Functionalization Strategies and Intracellular Applications.Angewandte Chemie (International ed. in English) · 2018Review
- Enzyme-Based Labeling Strategies for Antibody-Drug Conjugates and Antibody Mimetics.Antibodies (Basel, Switzerland) · 2018Review
- Nanobody Conjugates for Targeted Cancer Therapy and Imaging.Technology in cancer research & treatmentReview
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The broad substrate tolerance of tubulin tyrosine ligase is the basic rationale behind its wide applicability for chemoenzymatic protein functionalization. In this context, we report that the wild-type enzyme enables ligation of various unnatural amino acids that are substantially bigger than and structurally unrelated to the natural substrate, tyrosine, without the need for extensive protein engineering. This unusual substrate flexibility is due to the fact that the enzyme's catalytic pocket forms an extended cavity during ligation, as confirmed by docking experiments and all-atom molecular dynamics simulations. This feature enabled one-step C-terminal biotinylation and fluorescent coumarin labeling of various functional proteins as demonstrated with ubiquitin, an antigen binding nanobody, and the apoptosis marker Annexin V. Its broad substrate tolerance establishes tubulin tyrosine ligase as a powerful tool for
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Registered trials
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