DTDP-glucose 4,6-dehydratase

In enzymology, a dTDP-glucose 4,6-dehydratase is an enzyme that catalyzes the chemical reaction


 * dTDP-glucose $$\rightleftharpoons$$ dTDP-4-dehydro-6-deoxy-D-glucose + H2O

Hence, this enzyme has one substrate, dTDP-glucose, and two products, dTDP-4-dehydro-6-deoxy-D-glucose and H2O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is dTDP-glucose 4,6-hydro-lyase (dTDP-4-dehydro-6-deoxy-D-glucose-forming). Other names in common use include thymidine diphosphoglucose oxidoreductase, TDP-glucose oxidoreductase, and dTDP-glucose 4,6-hydro-lyase. This enzyme participates in 4 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, polyketide sugar unit biosynthesis, and biosynthesis of vancomycin group antibiotics. It employs one cofactor, NAD+.

Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , and.