ArticleScientific reports2017
Heterologous expression and characterization of functional mushroom tyrosinase (AbPPO4).
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 45 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed, 111 citations in OpenAlex.
- In silico and in vitro exploration of a tyrosinase for biocatalytic production of catechols.FEBS open bio · 2026Article
- Genomic and Metabolomic Comparisons Provide New Insights into Plant Cell Wall Degradation, Mating Diversity and Secondary Metabolites in Brown and White CommercialInternational journal of molecular sciences · 2026Article
- Chemical Synthesis of Functionalized Peptidomelanin for Groundwater Uranium Extraction.ACS omega · 2026Article
- Tyrosinase Recovered from White Button Mushroom Waste: Extraction, Characterization, and Application in Casein Cross-Linking.Journal of agricultural and food chemistry · 2026Article
- Article
- Towards synthetic catechol rich protein analogues through tyrosinase catalyzed activation of a tyrosine dipeptide in continuous mode.Catalysis science & technology · 2025Article
- Acid-Adapted Polyphenol Oxidases from Agricultural Wastes: Extraction, Characterization, and Application in Plant Protein Crosslinking.Foods (Basel, Switzerland) · 2025Article
- Biochemical Analysis of Recombinant Pea Seed Coat-Specific Polyphenol Oxidase (Journal of agricultural and food chemistry · 2025Article
- Identification of an Activity Selector for the Nitroso-Forming Activity in Bacterial Type-III Copper Enzymes.Angewandte Chemie (International ed. in English) · 2025Article
- Gene Expression and Enzyme Kinetics of Polyphenol Oxidases in Strawberry and Their Possible Involvement in Enzymatic Browning Reactions in Strawberry Nectar.Foods (Basel, Switzerland) · 2025Article
- Engineered microbial platform confers resistance against heavy metals via phosphomelanin biosynthesis.Nature communications · 2025Article
- Classification of polyphenol oxidases shows ancient gene duplication leading to two distinct enzyme types.iScience · 2025Article
- Characterization of two bacterial tyrosinases from the halophilic bacterium Hahella sp. CCB MM4 relevant for phenolic compounds oxidation in wetlands.FEBS open bio · 2024Article
- Melanin for Photoprotection and Hair Coloration in the Emerging Era of Nanocosmetics.International journal of molecular sciences · 2024Review
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Biochemical Investigations of Five Recombinantly Expressed Tyrosinases Reveal Two Novel Mechanisms Impacting Carbon Storage in Wetland Ecosystems.Environmental science & technology · 2023Article
- Application of Molecular Dynamics Simulations to Determine Interactions between Canary Seed (International journal of molecular sciences · 2023Article
- Tissue engineering modalities in skeletal muscles: focus on angiogenesis and immunomodulation properties.Stem cell research & therapy · 2023Review
- Contribution of the Tyrosinase (MoTyr) to Melanin Synthesis, Conidiogenesis, Appressorium Development, and Pathogenicity inJournal of fungi (Basel, Switzerland) · 2023Article
- Biochemical characterization of Dimocarpus longan polyphenol oxidase provides insights into its catalytic efficiency.Scientific reports · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyrosinases are an ubiquitous group of copper containing metalloenzymes that hydroxylate and oxidize phenolic molecules. In an application context the term 'tyrosinase' usually refers to 'mushroom tyrosinase' consisting of a mixture of isoenzymes and containing a number of enzymatic side-activities. We describe a protocol for the efficient heterologous production of tyrosinase 4 from Agaricus bisporus in Escherichia coli. Applying this procedure a pure preparation of a single isoform of latent tyrosinase can be achieved at a yield of 140 mg per liter of autoinducing culture medium. This recombinant protein possesses the same fold as the enzyme purified from the natural source as evidenced by single crystal X-ray diffraction. The latent enzyme can be activated by limited proteolysis with proteinase K which cleaves the polypeptide chain after K382, only one The latent enzyme can amino acid before the main in-vivo activation site. Latent tyrosinase can be used as obtained and enzymatic activity may be induced in the reaction mixture by the addition of an ionic detergent (e.g. 2 mM SDS). The proteolytically activated mushroom tyrosinase shows >50% of its maximal activity in the range of pH 5 to 10 and accepts a wide range of substrates including mono- and diphenols, flavonols and chalcones.
Indexed as
Identifiers
What OpenQuestion holds
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.