Por favor, use este identificador para citar o enlazar este ítem: 10.3390/ijms19020633

Título: On the metal cofactor in the Tyrosinase family
Fecha de publicación: 23-feb-2018
Editorial: MDPI
Cita bibliográfica: International Journal of Molecular Sciences, 2018, 19, 633
ISSN: 1661-6596
1422-0067
Materias relacionadas: CDU::5 - Ciencias puras y naturales::57 - Biología
Palabras clave: Tyrosinase-related proteins
tyrosinase
melanin biosynthesis
copper
zinc
metal enzymes
adquisition protein structure
Resumen: 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.
Autor/es principal/es: Solano, Francisco
Facultad/Departamentos/Servicios: Departamento de Bioquimica y Biologia Molecular B e Inmunología
LAIB-IMIB
Versión del editor: www.mdpi.com/journal/ijms
URI: http://hdl.handle.net/10201/105661
DOI: 10.3390/ijms19020633
Tipo de documento: info:eu-repo/semantics/article
Número páginas / Extensión: 17
Derechos: info:eu-repo/semantics/openAccess
Aparece en las colecciones:Artículos: Bioquímica y Biología Molecular "B" e Inmunología

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