4-deoxy-L-erythro-5-hexoseulose uronate reductase (DEHR)

4-deoxy-L-erythro-5-hexoseulose uronate (DEH) reductase is a key enzyme in the microbial degradation of alginate, a major polysaccharide found in brown seaweed. It catalyzes the NAD(P)H-dependent reduction of DEH, an intermediate product of alginate lyase activity, into 2-keto-3-deoxy-D-gluconate (KDG), which then enters the Entner-Doudoroff pathway for energy production. While primarily studied in marine bacteria and organisms like abalone, DEH reductase is of significant interest in industrial biotechnology for the production of biofuels from macroalgae. In a medical context, it is associated with the metabolism of alginate-producing pathogens such as Pseudomonas aeruginosa, which forms protective biofilms in the lungs of cystic fibrosis patients. Although not currently a target for approved drugs, its essential role in alginate utilization and the potential toxicity of its substrate (DEH) to bacteria make it a promising candidate for novel antimicrobial strategies or metabolic engineering in synthetic biology.

Other names

4-deoxy-L-erythro-5-hexoseulose uronate reductaseDEH reductaseA1-RFlRedHdRed4-deoxy-L-erythro-5-hexoseulose-uronate reductase

Reduction of 4-deoxy-L-erythro-5-hexoseulose uronate (DEH) to 2-keto-3-deoxy-D-gluconate (KDG) using NAD(P)H as a cofactor.