Purification and Characterization of Two Dihydroxyacetone Kinases from Schizosaccharomyces pombe IFO 0354
K Yoshihara, Yuko SHIMADA, Shuichi Karita, Tetsuya Kimura, Kazuo Sakka, Kunio Ohmiya
Abstract
K Yoshihara, Yuko SHIMADA, Shuichi Karita, Tetsuya Kimura, Kazuo Sakka, Kunio Ohmiya
Abstract
Two dihydroxyacetone kinases (DHAKs), DHAK I and DHAK II, were purified to homogeneity from Schizosaccharomyces pombe IFO 0354. They were immunologically different from each other. Although both of the enzymes had some affinity for glycerol and dl-glyceraldehyde in addition to dihydroxyacetone and glyceraldehyde, V(infmax) values for dihydroxyacetone were much higher than those for glycerol and dl-glyceraldehyde. On the basis of the K(infm) values of both enzymes for dihydroxyacetone, DHAK II plays a more important role than DHAK I in dissimilation of glycerol via dihydroxyacetone.
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Two dihydroxyacetone kinases (DHAKs), DHAK I and DHAK II, were purified to homogeneity from Schizosaccharomyces pombe IFO 0354. They were immunologically different from each other. Although both of the enzymes had some affinity for glycerol and dl-glyceraldehyde in addition to dihydroxyacetone and glyceraldehyde, V(infmax) values for dihydroxyacetone were much higher than those for glycerol and dl-glyceraldehyde. On the basis of the K(infm) values of both enzymes for dihydroxyacetone, DHAK II plays a more important role than DHAK I in dissimilation of glycerol via dihydroxyacetone.
Key concepts: Dihydroxyacetone, Glyceraldehyde, Schizosaccharomyces pombe, Dihydroxyacetone phosphate, Glycerol kinase, Glycerol, Biochemistry, Glyceraldehyde 3-phosphate dehydrogenase