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Mushroom tyrosinase: a model system to combine experimental investigation of enzyme-catalyzed reactions, data handling using R, and enzyme-inhibitor structural studies

Research output: Contribution to journalArticlepeer-review



Robert Nairn, Will Cresswell, Jacqueline Nairn

School/Research organisations


The activity of mushroom tyrosinase can be measured by monitoring the conversion of phenolic compounds into quinone derivatives using spectrophotometry. This article describes a series of experiments which characterize the functional properties of tyrosinase, the analysis of the resulting data using R to determine the kinetic parameters, and the exploration of the structural properties of tyrosinase-inhibitor complexes. Tyrosinase assay development and subsequent activity measurements, in the presence of varying pH, substrate concentration and inhibitors, offers the opportunity to learn the enzyme characterization skills relevant to a research laboratory setting. Combining the activity studies with an exploration of the nature of the tyrosinase-inhibitor interactions enables a structural understanding of the experimental observations.


Original languageEnglish
Pages (from-to)370-376
JournalBiochemistry and Molecular Biology Education
Issue number5
Publication statusPublished - Sep 2015

    Research areas

  • Enzymes and catalysis, Laboratory exercises, Protein structure function and action mechanism, Computers in research and teaching

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