Abstract
Many alcohol dehydrogenases in nature are members of either the MDR (medium- chain dehydrogenases/reductases) or SDR (short-chain dehydrogenases/reductases) protein families In fact, both families were recognized in the early 80ies when an ADH was found be related to another enzyme and thus gave the first enzyme pair known in each family. For SDR the first pair was Drosophila ADH and ribitol dehydrogenase, which showede conservation of the Tyr-X-X-X-Lys active site (Jörnvall et al., 1981). For MDR the initial pair was mammalian ADH class I and sorbitol dehydrogenase, which showed the conservation of the Zinc at the active site and its Cys~46/His~67 ligands (Jeffery et al., 1984; Jörnvall et al., 1981). Since then, known members in both families have grown enormously. From the start, interpretations for MDR were much ahead of those for SDR because of a known three-dimensional structure of MDR already at that time (Eklund et al, 1976).
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Jörnvall, H. (1999). Multiplicity and Complexity of SDR and MDR Enzymes. In: Weiner, H., Maser, E., Crabb, D.W., Lindahl, R. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 7. Advances in Experimental Medicine and Biology, vol 463. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4735-8_44
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