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

Robert Nairn, Will Cresswell, Jacqueline Nairn

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

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
Volume43
Issue number5
DOIs
Publication statusPublished - Sept 2015

Keywords

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

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