[Dihydroxyacetone synthase from the methanol-utilizing yeast Candida boidinii].

A procedure for purification of dihydroxyacetone synthase catalyzing the formation of dihydroxyacetone and glyceraldehyde 3-phosphate from formaldehyde and xylulose 5-phosphate has been developed. Using ion-exchangers with increasing affinity for dihydroxyacetone synthase, a homogenous preparation of the enzyme with specific activity of 2 u./mg has been obtained. The enzyme is made up of 2 subunits with m. w. of 76,000, contains thiamine pyrophosphate, requires Mg2+ for its activity and differs from yeast transketolase by substrate specificity and some other properties. The role of dihydroxyacetone synthase in metabolism of methanol-utilizing yeasts is discussed.