[Purification and several properties of dihydroxyacetone kinase from the methylotrophic yeast Candida boidinii].

A procedure for isolation of a homogeneous dihydroxyacetone kinase including fractionation by polyethylene glycol and ion-exchange chromatography on polyethylenimine-Biogel has been developed. The enzyme is a dimer with Mr = 139 000 (2.71 000 according to SDS disc electrophoresis) and has a pI of 4.64 and pH optimum of 7.8-8.2. The enzyme phosphorylates dihydroxyacetone and, in a lesser degree, glyceraldehyde. ATP is the most efficient phosphate group donor for the enzyme. When ITP, GTP, CTP and UTP are used, the dihydroxyacetone kinase activity is about 30%.