The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcholol to an acid without the release of an aldehyde intermediate [PMID:2470755, PMID:9013585].

The enzymes have a wide range of functions. In plants UDP-glucose dehydrogenase, EC: 1.1.1.22, is an important enzyme in the synthesis of hemicellulose and pectin [PMID:12031484], which are the components of newly formed cell walls; while in zebrafish UDP-glucose dehydrogenase is required for cardiac valve formation [PMID:11533493]. In Xanthomonas campestris, a plant pathogen, UDP-glucose dehydrogenase is required for virulence [PMID:11554764].

GDP-mannose dehydrogenase, EC: 1.1.1.132, catalyzes the formation of GDP-mannuronic acid, which is the monomeric unit from which the exopolysaccharide alginate is formed. Alginate is secreted by a number of bacteria, which include, the pathogenic bacterium Pseudomonas aeruginosa and Azotobacter vinelandii. In Pseudomonas aeruginosa alginate is believed to play an important role in the bacteria's resistance to antibiotics and the host immune response [PMID:12135385], while in Azotobacter vinelandii it is essential for the encystment process [PMID:9864323].

This entry contains the dimerisation and substrate-binding domains of these enzymes [PMID:10841783, PMID:12705829].