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New features of the steady-state rate related with the initial concentration of substrate in the diphenolase and monophenolase activities of tyrosinase

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Abstract

Tyrosinase has two types of enzymatic activities: the hydroxylation of monophenols to o-diphenols (monophenolase activity) and oxidation of o-diphenols to o-quinones (diphenolase activity). The action on o-diphenols involves two substrates: oxygen and o-diphenol, while the mechanism proposed is a Uni Uni Bi Bi ping-pong. In this contribution, we demonstrate experimentally that there is a kinetically preferred pathway, which translates into the appearance of curves of initial velocity vs. initial diphenol concentration shows inhibition by an excess of substrate, while sigmoid curves are obtained when the initial velocity vs. initial oxygen concentration are graphed. However, the action mechanism of the enzyme on monophenols, which is more complex because it involves three substrates (monophenol, oxygen and o-diphenol), does behave differently from the hyperbolic behaviour as regards the initial velocity vs. initial monophenol concentration, results that can be explained if the limiting step in the action of tyrosinase is the hydroxylation of monophenol to o-diphenol.

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Authors and Affiliations

  1. GENZ: Grupo de Investigación Enzimología, Departamento de Bioquímica y Biología Molecular-A, Facultad de Biología, Universidad de Murcia, 30100, Espinardo, Murcia, Spain

    Jose Luis Muñoz-Muñoz, Francisco Garcia-Molina, Jose Tudela, Francisco Garcia-Cánovas & Jose N. Rodríguez-López

  2. Departamento de Química-Física, Escuela de Ingenieros Industriales de Albacete, Universidad de Castilla la Mancha, Avda. España s/n. Campus Universitario, 02071, Albacete, Spain

    Ramón Varon

Authors
  1. Jose Luis Muñoz-Muñoz
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  2. Francisco Garcia-Molina
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  3. Ramón Varon
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  4. Jose Tudela
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  5. Francisco Garcia-Cánovas
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  6. Jose N. Rodríguez-López
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Correspondence to Francisco Garcia-Cánovas.

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Muñoz-Muñoz, J.L., Garcia-Molina, F., Varon, R. et al. New features of the steady-state rate related with the initial concentration of substrate in the diphenolase and monophenolase activities of tyrosinase. J Math Chem 48, 347–362 (2010). https://doi.org/10.1007/s10910-010-9675-5

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  • DOI: https://doi.org/10.1007/s10910-010-9675-5

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