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  • Title: [Purification and several properties of dihydroxyacetone kinase from the methylotrophic yeast Candida boidinii].
    Author: Bystrykh LV, Trotsenko IuA.
    Journal: Biokhimiia; 1983 Oct; 48(10):1611-6. PubMed ID: 6315084.
    Abstract:
    A procedure for isolation of a homogeneous dihydroxyacetone kinase including fractionation by polyethylene glycol and ion-exchange chromatography on polyethylenimine-Biogel has been developed. The enzyme is a dimer with Mr = 139 000 (2.71 000 according to SDS disc electrophoresis) and has a pI of 4.64 and pH optimum of 7.8-8.2. The enzyme phosphorylates dihydroxyacetone and, in a lesser degree, glyceraldehyde. ATP is the most efficient phosphate group donor for the enzyme. When ITP, GTP, CTP and UTP are used, the dihydroxyacetone kinase activity is about 30%.
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