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  • Title: A new type of uncompetitive inhibition of tyrosinase induced by Cl- binding.
    Author: Park YD, Kim SY, Lyou YJ, Lee JY, Yang JM.
    Journal: Biochimie; 2005 Nov; 87(11):931-7. PubMed ID: 16005559.
    Abstract:
    A new type of Cl- induced inhibition of mushroom derived tyrosinase has been detected in this study, and it is defined as the reversible partial hyperbolic uncompetitive inhibition. The Cl- binding site was only induced at the state of the enzyme-substrate complex, and this was confirmed with the intrinsic fluorescence changes. As the oxygen bridge is broken by L-DOPA binding, Cl- simultaneously binds to the ES state to form the ESI complex. It is worth noticing that tyrosinase reacts sensitively to Cl- in the manner of a complex interaction, and this indicates that Cl- might be physiologically involved in the regulation of tyrosinase activity.
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