ArticlePloS one2014
Albinism-causing mutations in recombinant human tyrosinase alter intrinsic enzymatic activity.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- Ampyrone is a direct agonist of human tyrosinase and a potential therapeutic for hypopigmentation disorders.JCI insight · 2026Article
- A rescue assay for genetic diagnosis of oculocutaneous albinism using melanocytic MNT1 knock-out cells.Frontiers in genetics · 2026Article
- Genetic mutations disrupt the coordinated mode of tyrosinase's intra-melanosomal domain.Protein science : a publication of the Protein Society · 2025Article
- Human recombinant tyrosinase destabilization caused by the double mutation R217Q/R402Q.Protein science : a publication of the Protein Society · 2025Article
- Enzyme Inhibitory, Physicochemical, and Phytochemical Properties and Botanical Sources of Honey, Bee Pollen, Bee Bread, and Propolis Obtained from the Same Apiary.Antioxidants (Basel, Switzerland) · 2024Article
- Molecular Modeling of the Multiple-Substrate Activity of the Human Recombinant Intra-Melanosomal Domain of Tyrosinase and Its OCA1B-Related Mutant Variant P406L.International journal of molecular sciences · 2024Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Potent inhibition of human tyrosinase inhibitor by verproside from the whole plant ofJournal of enzyme inhibition and medicinal chemistry · 2023Article
- Evaluating the Cysteine-Rich and Catalytic Subdomains of Human Tyrosinase and OCA1-Related Mutants Using 1 μs Molecular Dynamics Simulation.International journal of molecular sciences · 2023Article
- In vitro characterization of the intramelanosomal domain of human recombinant TYRP1 and its oculocutaneous albinism type 3-related mutant variants.Protein science : a publication of the Protein Society · 2023Article
- In Vitro Reconstitution of the Melanin Pathway's Catalytic Activities Using Tyrosinase Nanoparticles.International journal of molecular sciences · 2022Article
- Protein Biochemistry and Molecular Modeling of the Intra-Melanosomal Domain of Human Recombinant Tyrp2 Protein and OCA8-Related Mutant Variants.International journal of molecular sciences · 2022Article
- The Phenotypic and Mutational Spectrum of the FHONDA Syndrome and Oculocutaneous Albinism: Similarities and Differences.Investigative ophthalmology & visual science · 2022Article
- Assessing Foveal Structure in Individuals withOphthalmology science · 2021Article
- Characterization of Temperature-Dependent Kinetics of Oculocutaneous Albinism-Causing Mutants of Tyrosinase.International journal of molecular sciences · 2021Article
- Tyrosinase Nanoparticles: Understanding the Melanogenesis Pathway by Isolating the Products of Tyrosinase Enzymatic Reaction.International journal of molecular sciences · 2021Article
- Homology modeling and global computational mutagenesis of human myosin VIIa.Journal of analytical & pharmaceutical research · 2021Article
- Human Tyrosinase: Temperature-Dependent Kinetics of Oxidase Activity.International journal of molecular sciences · 2020Article
- Protein Stability and Functional Characterization of Intra-Melanosomal Domain of Human Recombinant Tyrosinase-Related Protein 1.International journal of molecular sciences · 2020Article
- FunctionalJournal of analytical & pharmaceutical research · 2020Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundTyrosinase (TYR) catalyzes the rate-limiting, first step in melanin production and its gene (TYR) is mutated in many cases of oculocutaneous albinism (OCA1), an autosomal recessive cause of childhood blindness. Patients with reduced TYR activity are classified as OCA1B; some OCA1B mutations are temperature-sensitive. Therapeutic research for OCA1 has been hampered, in part, by the absence of purified, active, recombinant wild-type and mutant human enzymes. METHODOLOGY/PRINCIPAL
findingsThe intra-melanosomal domain of human tyrosinase (residues 19-469) and two OCA1B related temperature-sensitive mutants, R422Q and R422W were expressed in insect cells and produced in T. ni larvae. The short trans-membrane fragment was deleted to avoid potential protein insolubility, while preserving all other functional features of the enzymes. Purified tyrosinase was obtained with a yield of >1 mg per 10 g of larval biomass. The protein was a monomeric glycoenzyme with maximum enzyme activity at 37°C and neutral pH. The two purified mutants when compared to the wild-type protein were less active and temperature sensitive. These differences are associated with conformational perturbations in secondary structure. CONCLUSIONS/SIGNIFICANCE: The intramelanosomal domains of recombinant wild-type and mutant human tyrosinases are soluble monomeric glycoproteins with activities which mirror their in vivo function. This advance allows for the structure - function analyses of different mutant TYR proteins and correlation with their corresponding human phenotypes; it also provides an important tool to discover drugs that may improve tyrosinase activity and treat OCA1.
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