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Glucose dehydrogenase C-terminus
alcohol dehydrogenase catalytic domain-containing protein
This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure [1-2]. [1]. 8804825. Structural classification of proteins: new superfamilies. Murzin AG;. Curr Opin Struct Biol 1996;6:386-394. [2]. 10556240. Conserved structural features and sequence patterns in the GroES fold family. Taneja B, Mande SC;. Protein Eng 1999;12:815-818. (from Pfam)
zinc-binding dehydrogenase
L-threonine 3-dehydrogenase
L-threonine 3-dehydrogenase (TDH) catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate; belongs to the medium chain dehydrogenase/reductase (MDR) family
This protein is a tetrameric, zinc-binding, NAD-dependent enzyme of threonine catabolism. Closely related proteins include sorbitol dehydrogenase, xylitol dehydrogenase, and benzyl alcohol dehydrogenase. Eukaryotic examples of this enzyme have been demonstrated experimentally but do not appear in database search results. E. coli His-90 modulates substrate specificity and is believed part of the active site.
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