Understanding the three-dimensional nature of an enzyme active-site and the result of this spatial orientation on the chemical reactions catalyzed by an enzyme are core learning goals of many biochemical curricula. Yeast alcohol dehydrogenase catalyzes the reduction of acetaldehyde to ethanol coupled to the oxidation of NADH to NAD+ by transferring the pro-R hydride from the nicotinamide moiety of NADH to the re-face of acetaldehyde. A laboratory and course module in which students determine the stereoselectivity of yeast alcohol dehydrogenase by observing enzyme catalyzed redox reactions using 1H-NMR with either ethanol or D6-ethanol as a substrate will be presented. Integration of this lab activity into a larger biochemistry and chemistry curriculum will be discussed.

Extending 1H-NMR analysis into an upper-division biochemistry course to investigate enzyme stereoselectivity and active-site architecture

253rd National Meeting (2017)

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