Next Article in Journal
Sinus Bradycardia in Carriers of the SCN5A-1795insD Mutation: Unraveling the Mechanism through Computer Simulations
Next Article in Special Issue
Structure-Activity Relationships of Thiazolyl Resorcinols, Potent and Selective Inhibitors of Human Tyrosinase
Previous Article in Journal
Alternative mRNA Splicing in the Pathogenesis of Obesity
Previous Article in Special Issue
Nanomechanical Phenotype of Melanoma Cells Depends Solely on the Amount of Endogenous Pigment in the Cells
Article Menu
Issue 2 (February) cover image

Export Article

Open AccessReview
Int. J. Mol. Sci. 2018, 19(2), 633;

On the Metal Cofactor in the Tyrosinase Family

Department Biochemistry and Molecular Biology B and Immunology, School of Medicine and LAIB-IMIB, University of Murcia, 30100 Murcia, Spain
Received: 26 January 2018 / Revised: 13 February 2018 / Accepted: 13 February 2018 / Published: 23 February 2018
(This article belongs to the Special Issue Melanins and Melanogenesis: From Nature to Applications)
PDF [852 KB, uploaded 23 February 2018]


The production of pigment in mammalian melanocytes requires the contribution of at least three melanogenic enzymes, tyrosinase and two other accessory enzymes called the tyrosinase-related proteins (Trp1 and Trp2), which regulate the type and amount of melanin. The last two proteins are paralogues to tyrosinase, and they appeared late in evolution by triplication of the tyrosinase gene. Tyrosinase is a copper-enzyme, and Trp2 is a zinc-enzyme. Trp1 has been more elusive, and the direct identification of its metal cofactor has never been achieved. However, due to its enzymatic activity and similarities with tyrosinase, it has been assumed as a copper-enzyme. Recently, recombinant human tyrosinase and Trp1 have been expressed in enough amounts to achieve for the first time their crystallization. Unexpectedly, it has been found that Trp1 contains a couple of Zn(II) at the active site. This review discusses data about the metal cofactor of tyrosinase and Trps. It points out differences in the studied models, and it proposes some possible points accounting for the apparent discrepancies currently appearing. Moreover, some proposals about the possible flexibility of the tyrosinase family to uptake copper or zinc are discussed. View Full-Text
Keywords: tyrosinase-related proteins; tyrosinase; melanin biosynthesis; copper; zinc; metal enzymes; acquisition protein structure tyrosinase-related proteins; tyrosinase; melanin biosynthesis; copper; zinc; metal enzymes; acquisition protein structure

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Solano, F. On the Metal Cofactor in the Tyrosinase Family. Int. J. Mol. Sci. 2018, 19, 633.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top