DTDP-4-dehydrorhamnose 3,5-epimerase

In enzymology, a dTDP-4-dehydrorhamnose 3,5-epimerase is an enzyme that catalyzes the chemical reaction


 * dTDP-4-dehydro-6-deoxy-D-glucose $$\rightleftharpoons$$ dTDP-4-dehydro-6-deoxy-L-mannose

Hence, this enzyme has one substrate, dTDP-4-dehydro-6-deoxy-D-glucose, and one product, dTDP-4-dehydro-6-deoxy-L-mannose.

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase. Other names in common use include dTDP-L-rhamnose synthetase, dTDP-L-rhamnose synthetase, thymidine diphospho-4-ketorhamnose 3,5-epimerase, TDP-4-ketorhamnose 3,5-epimerase, dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase, and TDP-4-keto-L-rhamnose-3,5-epimerase. This enzyme participates in 3 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, and polyketide sugar unit biosynthesis.

Structural studies
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , , and.