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The effect of halide ions on frog epidermis tyrosinase has been characterized with the trypsin-activated enzyme. At pH 7, the order of inhibition is I- greater than Br- greater than Cl- greater than F-. Chloride, the most extensively studied halide, shows a competitive pattern with respect to the substrate, L-DOPA. Inhibition is strongly pH-dependent, with a pKa of 6.12 for the responsible protonatable group. Other kinetic constants are also calculated using a novel approach. The mechanism of interaction between chloride and the enzyme is discussed, and a model is proposed in which chloride interferes the tyrosinase activity by displacing a catalytically important ligand, probably a histidine residue of the side-chain, from the copper at the enzyme-active site.
R Peñafiel, and
J D Galindo, and
F Solano, and
E Pedreño, and
J L Iborra, and
J A Lozano
July 1988,
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F Solano, and
E Pedreño, and
J L Iborra, and
J A Lozano
March 1978,
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R Peñafiel, and
J D Galindo, and
F Solano, and
E Pedreño, and
J L Iborra, and
J A Lozano
June 1979,
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R Peñafiel, and
J D Galindo, and
F Solano, and
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J L Iborra, and
J A Lozano
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R Peñafiel, and
J D Galindo, and
F Solano, and
E Pedreño, and
J L Iborra, and
J A Lozano
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R Peñafiel, and
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J A Lozano
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R Peñafiel, and
J D Galindo, and
F Solano, and
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J A Lozano
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R Peñafiel, and
J D Galindo, and
F Solano, and
E Pedreño, and
J L Iborra, and
J A Lozano
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R Peñafiel, and
J D Galindo, and
F Solano, and
E Pedreño, and
J L Iborra, and
J A Lozano
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R Peñafiel, and
J D Galindo, and
F Solano, and
E Pedreño, and
J L Iborra, and
J A Lozano
January 1979,
General pharmacology,
