ArticleScientific reports2017
A tyrosinase, mTyr-CNK, that is functionally available as a monophenol monooxygenase.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- A binuclear copper enzyme platform for enantioconvergent radical (pseudo)halogenation.bioRxiv : the preprint server for biology · 2026Article
- Intertidal Warfare: Synergistic Allelopathy Mediates Spatial Competition between Two Marine Calcareous-Shelled Sessile Organisms.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Tyrosinase-Catalyzed Peptide Macrocyclization for mRNA Display.Journal of the American Chemical Society · 2023Article
- A Preclinical Model for Parkinson's Disease Based on Transcriptional Gene Activation via KEAP1/NRF2 to Develop New Antioxidant Therapies.Antioxidants (Basel, Switzerland) · 2023Review
- Polyphenol-Hydroxylating Tyrosinase Activity under Acidic pH Enables Efficient Synthesis of Plant Catechols and Gallols.Microorganisms · 2021Article
- Synthesis of Multi-Protein Complexes through Charge-Directed Sequential Activation of Tyrosine Residues.Journal of the American Chemical Society · 2021Article
- Recent advancements in enzyme-mediated crosslinkable hydrogels:APL bioengineering · 2021Review
- A Novel Tyrosinase fromApplied and environmental microbiology · 2021Article
- A Novel Method for Creating a Synthetic L-DOPA Proteome and In Vitro Evidence of Incorporation.Proteomes · 2021Article
- On the Metal Cofactor in the Tyrosinase Family.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyrosinase efficiently catalyzes the ortho-hydroxylation of monophenols and the oxidation of diphenols without any additional cofactors. Although it is of significant interest for the biosynthesis of catechol derivatives, the rapid catechol oxidase activity and inactivation of tyrosinase have hampered its practical utilization as a monophenol monooxygenase. Here, we prepared a functional tyrosinase that exhibited a distinguished monophenolase/diphenolase activity ratio (V
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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.