| Description | Proteins in this entry are members of the glucose-methanol-choline oxidoreductase family of flavoenzymes [ ]. These enzymes catalyse diverse reaction and include glucose dehydrogenase (), alcohol oxidase ( ), glucose oxidase ( ), choline dehydrogenase ( ), and cyclase atC from Aspergillus terreus which oxidizes terremutin to terreic acid, a quinone epoxide inhibitor of a tyrosine kinase [ ].Structural studies indicate that these proteins are composed of an N-terminal FAD-binding domain, and a C-terminal substrate-binding domain [ , , ]. The FAD-binding domain forms the α-β fold typical of dinucleotide binding proteins, while the substrate-binding domain consists of a β-sheet surrounded by α-helices. The general topology of these proteins is conserved, though inserted structural elements occur in both choline dehydrogenase and alcohol dehydrogenase []. | Name | Glucose-methanol-choline oxidoreductase |
| Short Name | GMC_OxRdtase | Type | Family |
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