ArticleJournal of enzyme inhibition and medicinal chemistry2020
Histidine residues at the copper-binding site in human tyrosinase are essential for its catalytic activities.
Article in Journal of enzyme inhibition and medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 61 citations in OpenAlex.
- Article
- Phytochemical Characterization ofFood science & nutrition · 2026Article
- Herbal medicine for melanin regulation: biological synthesis, effective formulas/compounds, and biopharmaceutical methods.Journal of natural medicines · 2026Review
- Article
- Article
- The small molecule ML233 is a direct inhibitor of tyrosinase function.bioRxiv : the preprint server for biology · 2025Article
- In-silico evaluation of potential plant-based tyrosinase inhibitors for cosmetic and pharmaceutical applications.Biotechnology letters · 2025Article
- Article
- Natural Mimetic 4,6-Dihydroxyaurone Derivatives as Tyrosinase Inhibitors: Design, Synthesis, and Biological Evaluation.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2025Article
- Novel Tripeptides as Tyrosinase Inhibitors: In Silico and In Vitro Approaches.International journal of molecular sciences · 2024Article
- Anti-Melanogenic Activity of Ethanolic Extract fromAntioxidants (Basel, Switzerland) · 2024Article
- Effect of histidine protonation state on ligand binding at the ATP-binding site of human protein kinase CK2.Scientific reports · 2024Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Simple and rapid detection of tyrosinase activity with the adjustable light scattering properties of CoOOH nanoflakes.Analytical and bioanalytical chemistry · 2023Article
- A highly explicit electrochemical biosensor for catechol detection in real samples based on copper-polypyrrole.RSC advances · 2023Article
- Pueraria protein extract inhibits melanogenesis and promotes melanoma cell apoptosis through the regulation of MITF and mitochondrial‑related pathways.Molecular medicine reports · 2023Article
- Contribution of the Tyrosinase (MoTyr) to Melanin Synthesis, Conidiogenesis, Appressorium Development, and Pathogenicity inJournal of fungi (Basel, Switzerland) · 2023Article
- Pinostrobin Suppresses the α-Melanocyte-Stimulating Hormone-Induced Melanogenic Signaling Pathway.International journal of molecular sciences · 2023Article
- Investigation of phenyllactic acid as a potent tyrosinase inhibitor produced by probiotics.Current research in food science · 2023Article
- Theoretical Studies of Cyanophycin Dipeptides as Inhibitors of Tyrosinases.International journal of molecular sciences · 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
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyrosinase is a copper-binding enzyme involved in melanin biosynthesis. However, the detailed structure of human tyrosinase has not yet been solved, along with the identification of the key sites responsible for its catalytic activity. We used site-directed mutagenesis to identify the residues critical for the copper binding of human tyrosinase. Seven histidine mutants in the two copper-binding sites were generated, and catalytic activities were characterised. The tyrosine hydroxylase activities of the CuA site mutants were approximately 50% lower than those of the wild-type tyrosinase, while the dopa oxidation activities of the mutants were not significantly different from that of wild-type tyrosinase. By contrast, mutations at CuB significantly decreased both tyrosine hydroxylation and dopa oxidation activities, confirming that the catalytic sites for these two activities are at least partially distinct. These findings provide a useful resource for further structural determination and development of tyrosinase inhibitors in the cosmetic and pharmaceutical industries.
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.