ArticlePloS one2018
Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.
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Who cites it
16 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.
- Potential Bioactive Function of Microbial Metabolites as Inhibitors of Tyrosinase: A Systematic Review.International journal of molecular sciences · 2026Pooled it
- Discovery ofJournal of enzyme inhibition and medicinal chemistry · 2025Article
- Redox reactivities of membrane-bound amyloid-β-Cu complexes and their targeting by metallothionein-3.Free radical biology & medicine · 2025Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Miglitol, an Oral Antidiabetic Drug, Downregulates Melanogenesis in B16F10 Melanoma Cells through the PKA, MAPK, and GSK3β/β-Catenin Signaling Pathways.Molecules (Basel, Switzerland) · 2022Article
- Plants as Modulators of Melanogenesis: Role of Extracts, Pure Compounds and Patented Compositions in Therapy of Pigmentation Disorders.International journal of molecular sciences · 2022Review
- 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
- Biophysical Compatibility of a Heterotrimeric Tyrosinase-TYRP1-TYRP2 Metalloenzyme Complex.Frontiers in pharmacology · 2021Article
- Histidine residues at the copper-binding site in human tyrosinase are essential for its catalytic activities.Journal of enzyme inhibition and medicinal chemistry · 2020Article
- Membrane insertion exacerbates the α-Synuclein-Cu(II) dopamine oxidase activity: Metallothionein-3 targets and silences all α-synuclein-Cu(II) complexes.Free radical biology & medicine · 2020Article
- 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
- Novel tyrosinase inhibitory peptide with free radical scavenging ability.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- The TYRP1-mediated protection of human tyrosinase activity does not involve stable interactions of tyrosinase domains.Pigment cell & melanoma research · 2019Article
- Dynamic analysis of human tyrosinase intra-melanosomal domain and mutant variants to further understand oculocutaneous albinism type 1.Journal of analytical & pharmaceutical research · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Human tyrosinase (hTyr) is a Type 1 membrane bound glycoenzyme that catalyzes the initial and rate-limiting steps of melanin production in the melanosome. Mutations in the Tyr gene are linked to oculocutaneous albinism type 1 (OCA1), an autosomal recessive disorder. Currently, the application of enzyme replacement therapy for a treatment of OCA1 is hampered by the absence of pure hTyr. Here, full-length hTyr (residues 1-529) was overexpressed in Trichoplusia ni larvae infected with a baculovirus, solubilized with detergent and purified using chromatography. Michaelis-Menten kinetics, enzymatic specific activity, and analytical ultracentrifugation were used to compare the hTyr in detergent with the soluble recombinant intra-melanosomal domain, hTyrCtr (residues 19-469). Active hTyr is monomeric in detergent micelles suggesting no stable interactions between protein molecules. Both, hTyr and hTyrCtr, exhibited similar enzymatic activity and ligand affinity in L-DOPA and L-Tyrosine reactions. In addition, expression in larvae is a scalable process that will allow high yield protein production. Thus, larval production of enzymatically active human tyrosinase potentially could be a useful tool in developing a cure for OCA1.
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Registered trials
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