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  • Title: Dihydroxyacetone kinase of methanol-assimilating yeasts. II. Partial purification and some properties of dihydroxyacetone kinase from Candida methylica.
    Author: Hofmann KH, Babel W.
    Journal: Z Allg Mikrobiol; 1981; 21(3):219-24. PubMed ID: 6267834.
    Abstract:
    Dihydroxyacetone kinase (DHAK) from the cell-free extract of methanol-grown Candida methylica was partially purified about 100-fold by a procedure employing streptomycin sulfate fractionation, ammonium sulfate fractionation, negative absorption on Cibacron blue F3G-A sephadex G 200 and DEAE-cellulose column chromatography. The enzyme was stable in 50 mM Tris-HCl buffer pH 7.5 containing 60% glycerol at -18 degrees C. The pH optimum for the activity of DHAK from C. methylica was 7.5. The purified enzyme phosphorylated dihydroxyacetone four times faster than D,L-glyceraldehyde. The apparent MICHAELIS-MENTEN constants for dihydroxyacetone and D,L-glyceraldehyde were 0.011 mM and 0.024 mM. Other C3 compounds including glycerol were not phosphorylated. ITP and UTP were used as phosphate donors with a reaction rate of 11% and 3.1%, respectively, in relation to ATP, whereas the reaction rates of DHAK from C. methylica with CTP or GTP were much lower than 1%. The reaction of DHAK depends upon the presence of divalent cations in the assay. The highest activity was found with Mg2+ ions. The reaction rates with Co2+ or Ca2+ ions were only 57.3% and 30.3%, respectively, in relation to the assay with magnesium ions. Manganese chloride in the assay led to a complete loss of activity.
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