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...

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Bibliographic Details
Published in:Biochemistry and molecular biology education 2015-09, Vol.43 (5), p.370-376
Main Authors: Nairn, Robert, Cresswell, Will, Nairn, Jacqueline
Format: Article
Language:English
Subjects:
Agaricus - chemistry
Agaricus - enzymology
Biochemistry
Biochemistry - education
Chemical reactions
computers in research and teaching
Enzyme Assays - methods
Enzymes
enzymes and catalysis
Humans
Laboratories
laboratory exercises
Laboratory Experiments
Light
Measurement
Models, Biological
Monophenol Monooxygenase - chemistry
Mushrooms
Problem-Based Learning - methods
protein structure function and action mechanism
Research - education
Science Experiments
Science Instruction
Science Laboratories
Scientific Concepts
Spectrophotometry - methods
Spectroscopy
Universities
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Summary: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. © 2015 by The International Union of Biochemistry and Molecular Biology, 43(5):370–376, 2015.
ISSN:1470-8175
1539-3429
DOI:10.1002/bmb.20887