Dihydroxyacetone Kinase 2 (DAK)

DAK is a member of the family of dihydroxyacetone kinases, which have a protein structure distinct from other kinases. The product of this gene phosphorylates dihydroxyacetone, and also catalyzes the formation of riboflavin 4""",5"""-phosphate (aka cyclic FMN) from FAD. Several alternatively spliced transcript variants have been identified, but the full-length nature of only one has been determined. An enzyme catalyzing the phosphorylation of dibydroxyacetone has been identified in the halophilic alga, Dunaliella parva. Since glycerol and glyceraldehyde are not substrates, the enzyme is referred to as dibydroxyacetone kinase. Dihydroxyacetone kinase was prified 9-fold by ammonium salfate fractionation foilowed by DEAE-ceilulose chromatography.