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- W1793869430 abstract "This chapter describes the proton magnetic resonance (1H NMR) technique to measure the hydride transfer stereospecificity of nicotinamide adenine dinucleotide linked enzymes. In this technique, exact oxidoreduction site is directly monitored, rather than the entire coenzyme molecule, and crude extracts containing a given enzyme can often be employed. Specifically deuterated pyridine nucleotides are reacted with the enzyme whose stereospecificity is to be determined in the presence of the appropriate substrate. The examination of the 1H NMR spectra of the product coenzyme readily reveals which hydride is transferred to the coenzyme. Three methods can be employed for these studies that depend on the availability of substrates and on the equilibrium of a particular enzymic reaction. Method 1 is the simplest method in which [4B-2H] reduced nicotinamide adenine dinucleotide (NADH) is oxidized with the enzyme under investigation. The 1H NMR spectrum of the product nicotinamide adenine dinucleotide (NAD) is then analyzed for the retention of deuterium at the pyridine 4 position. Method 2, utilizes the oxidized coenzyme. In method 3, [4-2H]NAD + is first reduced to NADH with the enzyme under study and then it is reoxidized with a well-known A-stereospecific enzyme, yeast alcohol dehydrogenase." @default.
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- W1793869430 date "1978-01-01" @default.
- W1793869430 modified "2023-09-26" @default.
- W1793869430 title "[14] The hydride transfer stereospecificity of nicotinamide adenine dinucleotide linked enzymes: A proton magnetic resonance technique" @default.
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- W1793869430 doi "https://doi.org/10.1016/s0076-6879(78)54017-2" @default.
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