K. Yoshihara et al., PURIFICATION AND CHARACTERIZATION OF 2 DIHYDROXYACETONE KINASES FROM SCHIZOSACCHAROMYCES-POMBE IFO-0354, Applied and environmental microbiology, 62(12), 1996, pp. 4663-4665
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.