Abstract
NAD (P)-dependent dehydrogenases catalyze the stereospecific transfer of hydrogen between substrates and the C-4 position of pyridine nucleotides. With respect to the coenzyme about half of the investigated enzymes show pro-R, the other half pro-S stereospecificity1. Historical and functional models have been proposed to explain the stereochemical diversity2,3. We have pointed out that neither the historical nor the functional model is able to predict the coenzyme stereospecificity of the ubiquitiously distributed alcohol/polyol dehydrogenases and we have introduced a new hypothesis: Zn-containing “long” forms of alcohol/polyol dehydrogenases are pro-R, “short” forms without zinc are pro-S specific4. We report here that our hypothesis is also in agreement with new findings shown for a sugar dehydrogenase.
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© 1991 Plenum Press, New York
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Schneider-Bernlöhr, H., Adolph, H.W., Zeppezauer, M. (1991). The Predictive Value of Historical and Functional Models: Coenzyme Stereospecificity of Glucose Dehydrogenase. In: Pandit, U.K., Alderweireldt, F.C. (eds) Bioorganic Chemistry in Healthcare and Technology. NATO ASI Series, vol 207. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1354-0_30
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DOI: https://doi.org/10.1007/978-1-4684-1354-0_30
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