PURIFICATION AND CHARACTERIZATION OF 2 DIHYDROXYACETONE KINASES FROM SCHIZOSACCHAROMYCES-POMBE IFO-0354

Two dihydroxyacetone kinases (DHAKs), DHAK I and DHAK II, were purifie d to homogeneity from Schizosaccharomyces pombe IFO 0354. They were im munologically different from each other. Although both of the enzymes had some affinity for glycerol and DL-glyceraldehyde in addition to di hydroxyacetone and glyceraldehyde, V-max values for dihydroxyacetone w ere much higher than those for glycerol and DL-glyceraldehyde. On the basis of the K-m values of both enzymes for dihydroxyacetone, DHAK II plays a more important role than DHAK I in dissimilation of glycerol v ia dihydroxyacetone.