Biochemical and Biophysical Research Communications
Reversible oxygenation of tyrosinase
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Dioxygen-binding in metalloproteins and corresponding models
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2014, Bioorganic and Medicinal ChemistryType-3 copper proteins: Recent advances on polyphenol oxidases
2014, Advances in Protein Chemistry and Structural BiologyCitation Excerpt :Other mutants (as Phe197 to alanine, Met61 and Met184 to leucine) revealed that Phe197, Met61, and Met184, which are located at the entrance to the binding site, are also important for enhancing the diphenolase activity. First reports on tyrosinase reacting aerobically with molar equivalents of H2O2 were published by Jolley, Evans, and Mason (1972). For a review describing the electronic properties of the type-3 copper center, see Solomon et al. (1992).
Extracellular tyrosinase from the fungus Trichoderma reesei shows product inhibition and different inhibition mechanism from the intracellular tyrosinase from Agaricus bisporus
2012, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :Both met- and oxy-forms show a diphenolase activity, whereas only the oxy-form shows a monophenolase activity [11,19]. The deoxy-form is a reduced and an instable form and binds oxygen to give the oxy-form [20–22]. Tyrosinase can accept a wide range of p-substituted monophenolic and diphenolic substrates.
Comparison of substrate specificity of tyrosinases from Trichoderma reesei and Agaricus bisporus
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