ArticleInternational journal of molecular sciences2020
Human Tyrosinase: Temperature-Dependent Kinetics of Oxidase Activity.
Article in International journal of molecular sciences, 2020. 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, 17 citations in OpenAlex.
- Wearable sensors for monitoring drug pharmacokinetics in patients with Parkinson's disease.Scientific reports · 2026Article
- Maximizing dopa-oxidase activity in Aspergillus oryzae mycelia: insights into production optimization and potential biomedical applications.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- Human recombinant tyrosinase destabilization caused by the double mutation R217Q/R402Q.Protein science : a publication of the Protein Society · 2025Article
- 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
- In Vitro Reconstitution of the Melanin Pathway's Catalytic Activities Using Tyrosinase Nanoparticles.International journal of molecular sciences · 2022Article
- Iron as the concert master in the pathogenic orchestra playing in sporadic Parkinson's disease.Journal of neural transmission (Vienna, Austria : 1996) · 2021Review
- Considerations about the Continuous Assay Methods, Spectrophotometric and Spectrofluorometric, of the Monophenolase Activity of Tyrosinase.Biomolecules · 2021Article
- Characterization of Temperature-Dependent Kinetics of Oculocutaneous Albinism-Causing Mutants of Tyrosinase.International journal of molecular sciences · 2021Article
- Article
- 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
- Evaluating the Performance of a Non-Bonded CuInternational journal of molecular sciences · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Human tyrosinase (Tyr) is involved in pigment biosynthesis, where mutations in its corresponding gene TYR have been linked to oculocutaneous albinism 1, an autosomal recessive disorder. Although the enzymatic capabilities of Tyr have been well-characterized, the thermodynamic driving forces underlying melanogenesis remain unknown. Here, we analyze protein binding using the diphenol oxidase behavior of Tyr and van 't Hoff temperature-dependent analysis. Recombinant Tyr was expressed and purified using a combination of affinity and size-exclusion chromatography. Michaelis-Menten constants were measured spectrophotometrically from diphenol oxidase reactions of Tyr, using L-3,4-dihydroxyphenylalanine (L-DOPA) as a substrate, at temperatures: 25, 31, 37, and 43 °C. Under the same conditions, the Tyr structure and the L-DOPA binding activity were simulated using 3 ns molecular dynamics and docking. The thermal Michaelis-Menten kinetics data were subjected to the van 't Hoff analysis and fitted with the computational model. The temperature-dependent analysis suggests that the association of L-DOPA with Tyr is a spontaneous enthalpy-driven reaction, which becomes unfavorable at the final step of dopachrome formation.
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