Mushroom tyrosinase: A model system to combine experimental investigation of enzyme-catalyzed reactions, data handling using R, and enzyme-inhibitor structural studies.
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.
School of Chemistry, University of St Andrews, North Haugh, St Andrews, KY16 9ST, Scotland, United Kingdom.
Robert
R
Nairn
School of Biology, University of St Andrews, North Haugh, St Andrews, KY16 9ST, Scotland, United Kingdom.
Will
W
Cresswell
School of Biology, University of St Andrews, North Haugh, St Andrews, KY16 9ST, Scotland, United Kingdom.
Jacqueline
J
Nairn
D000364:Agaricus / Q000737:chemistry* / Q000201:enzymology; D001671:Biochemistry / Q000193:education*; D057075:Enzyme Assays / Q000379:methods; D006801:Humans; D007753:Laboratories; D008954:Models, Biological; D014442:Monophenol Monooxygenase / Q000737:chemistry*; D018794:Problem-Based Learning / Q000379:methods*; D012106:Research / Q000193:education; D013053:Spectrophotometry / Q000379:methods; D014495:Universities
D014442:Monophenol Monooxygenase
computers in research and teaching; enzymes and catalysis; laboratory exercises; protein structure function and action mechanism