ArticleChembiochem : a European journal of chemical biology2012
Mushroom tyrosinase oxidizes tyrosine-rich sequences to allow selective protein functionalization.
Article in Chembiochem : a European journal of chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Development of a novel method for generating Q-bodies using tyrosinase-mediated HA-tag labeling.Analytical and bioanalytical chemistry · 2025Article
- Site-selective cleavage of peptides and proteins targeting aromatic amino acid residues.RSC advances · 2025Review
- Recent developments in the cleavage, functionalization, and conjugation of proteins and peptides at tyrosine residues.Chemical science · 2023Review
- A novel tyrosine hyperoxidation enables selective peptide cleavage.Chemical science · 2022Article
- Oxidation-Induced "One-Pot" Click Chemistry.Chemical reviews · 2021Article
- Tyrosine bioconjugation - an emergent alternative.Organic & biomolecular chemistry · 2020Review
- Polyphenol oxidases exhibit promiscuous proteolytic activity.Communications chemistry · 2020Article
- Redox Signaling by Reactive Electrophiles and Oxidants.Chemical reviews · 2018Review
- ortho-Quinones and Analogues Thereof: Highly Reactive Intermediates for Fast and Selective Biofunctionalization.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Review
- Inducible, Site-Specific Protein Labeling by Tyrosine Oxidation-Strain-Promoted (4 + 2) Cycloaddition.Bioconjugate chemistry · 2017Article
- Click chemistry in complex mixtures: bioorthogonal bioconjugation.Chemistry & biology · 2014Review
- Tyrosinase-catalyzed site-specific immobilization of engineered C-phycocyanin to surface.Scientific reports · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We show that mushroom tyrosinase catalyzes the formation of reactive o-quinones on unstructured, tyrosine-rich sequences such as hemagglutinin (HA) tags (YPYDVPDYA). In the absence of exogenous nucleophiles and at low protein concentrations, the o-quinone decomposes with fragmentation of the HA tag. At higher protein concentrations (>5 mg mL⁻¹), crosslinking is observed. Besthorn's reagent intercepts the o-quinone to give a characteristic pink complex that can be observed directly on a denaturing SDS-PAGE gel. Similar labeled species can be formed by using other nucleophiles such as Cy5-hydrazide. These reactions are selective for proteins bearing HA and other unstructured poly-tyrosine-containing tags and can be performed in lysates to create specifically tagged proteins.
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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.