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31 P NMR of the pyruvate kinase reaction: An undergraduate experiment in enzyme kinetics
Author(s) -
Werner R. Marshall,
Johnson Austin
Publication year - 2017
Publication title -
biochemistry and molecular biology education
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 39
eISSN - 1539-3429
pISSN - 1470-8175
DOI - 10.1002/bmb.21079
Subject(s) - kinetics , pyruvate kinase , enzyme kinetics , enzyme , chemistry , nuclear magnetic resonance spectroscopy , biochemistry , proton nmr , stereochemistry , active site , glycolysis , physics , quantum mechanics
Understanding how to perform an enzyme assay is a critical learning skill in the undergraduate biochemistry curriculum. Students in biochemistry typically have been exposed to the use of NMR spectroscopy as a tool to determine chemical structure, but rarely are they exposed to the utility of NMR to evaluate enzyme kinetics. Furthermore, coverage of NMR experiments utilizing “alternative nuclei”, such as 15 N, 19 F, and 31 P may be neglected. Herein we report a simple 31 P NMR tube experiment that allows students to examine the enzyme kinetics and equilibrium constant of the reaction catalyzed by pyruvate kinase. © 2017 by The International Union of Biochemistry and Molecular Biology, 45(6):509–514, 2017.