InterPro domain: IPR012132

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 ( 1.1.5.9 ), alcohol oxidase ( 1.1.3.13 ), glucose oxidase ( 1.1.3.4 ), choline dehydrogenase ( 1.1.99.1 ), and cyclase atC from Aspergillus terreus which oxidizes terremutin to terreic acid, a quinone epoxide inhibitor of a tyrosine kinase [ 2 ].

Structural studies indicate that these proteins are composed of an N-terminal FAD-binding domain, and a C-terminal substrate-binding domain [ 3 , 4 , 5 ]. 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 general topology of these proteins is conserved, though inserted structural elements occur in both choline dehydrogenase and alcohol dehydrogenase [ 6 ].

1. GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities. J. Mol. Biol. 223, 811-4
2. Molecular genetic characterization of terreic acid pathway in Aspergillus terreus. Org. Lett. 16, 5250-3
3. 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes. Acta Crystallogr. D Biol. Crystallogr. 55, 969-77
4. The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase. Structure 9, 803-15
5. Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants. Biochemistry 38, 4277-86
6. Glucose oxidase from Penicillium amagasakiense. Primary structure and comparison with other glucose-methanol-choline (GMC) oxidoreductases. Eur. J. Biochem. 252, 90-9