InterPro domain: IPR045010

The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH [ 1 ]. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR) [ 2 ]. The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES [ 3 ].

This entry represents the MDR (medium-chain dehydrogenase/reductase) family.

1. Medium- and short-chain dehydrogenase/reductase gene and protein families : the MDR superfamily. Cell. Mol. Life Sci. 65, 3879-94
2. Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling. Eur. J. Biochem. 269, 4267-76
3. Medium- and short-chain dehydrogenase/reductase gene and protein families : Three-dimensional structures of MDR alcohol dehydrogenases. Cell. Mol. Life Sci. 65, 3907-17