InterPro: IPR012132 Glucose-methanol-choline oxidoreductase

Proteins in this entry are members of the glucose-methanol-choline oxidoreductase family of flavoenzymes [1]. These enzymes catalyse diverse reaction and include glucose dehydrogenase (EC:1.1.99.10), alcohol oxidase (EC:1.1.3.13), glucose oxidase (EC:1.1.3.4), choline dehydrogenase (EC:1.1.99.1), and hydroxynitrile lyase (EC:4.1.2.10). Structural studies indicate that these proteins are composed of an N-terminal FAD-binding domain, and a C-terminal substrate-binding domain [2, 3, 4]. The FAD-binding domain forms the alpha-beta fold typical of dinucleotide binding proteins, while the substrate-binding domain consists of a beta sheet surrounded by alpha helices. The genral topology of these proteins is conserved, though inserted structural elements occur in both choline dehydrogenase and alcohol dehydrogenase [5].